31 Studies Interaction with Mercury and EDTA
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31 Studies: Chemical Interaction with Mercury and EDTA
Results for your query on September 3, 2000:
Search all fields for: mercury And EDTA
Published in 1966 through 1999
Only select references with abstracts available
Show references published in English only
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Documents: 1 to 31 of 31
1Top Of Menu
Duhr EF, et al; HgEDTA complex inhibits GTP interactions with the E-site
of brain beta-tubulin. (Toxicol Appl Pharmacol, 1993 Oct, Abstract
available) [MEDLINE]
2Kalamegham R, et al; A simple ICP-MS procedure for the determination of
total mercury in whole blood and urine. (J Clin Lab Anal, 1992, Abstract
available) [MEDLINE]
3Gonzalvo MC, et al; Inhibition of paraoxonase activity in human liver
microsomes by exposure to EDTA, metals and mercurials. (Chem Biol
Interact, 1997 Aug, Abstract available) [MEDLINE]
4Mujica A, et al; Human semen ribonuclease. Location, properties and
inhibition by sodium dodecyl sulfate, zinc sulfate and EDTA. (Int J
Fertil, 1976, Abstract available) [MEDLINE]
5Farkas WR, et al; Effects of plumbous ion on guanine metabolism. (J
Inorg Biochem, 1979 Aug, Abstract available) [MEDLINE]
6Guldager B, et al; Metal excretion and magnesium retention in patients
with intermittent claudication treated with intravenous disodium EDTA.
(Clin Chem, 1996 Dec, Abstract available) [MEDLINE]
7Duhr EF, et al; HgEDTA complex inhibits GTP interactions with the E-site
of brain beta-tubulin. (Toxicol Appl Pharmacol, 1993 Oct, Abstract
available) [MEDLINE]
8Nooijen JL, et al; Trace element studies in three patients and a fetus
with Menkes' disease. Effect of copper therapy. (Pediatr Res, 1981 Mar,
Abstract available) [MEDLINE]
9Chau LY, et al; Monoglyceride and diglyceride lipases from human
platelet microsomes. (Biochim Biophys Acta, 1988 Dec, Abstract available)
[MEDLINE]
10Menu Position #10
Murata M, et al; Differential metal response and regulation of human
heavy metal-inducible genes. (J Cell Physiol, 1999 Jul, Abstract
available) [MEDLINE]
11Araki S, et al; Mobilisation of heavy metals into the urine by CaEDTA:
relation to erythrocyte and plasma concentrations and exposure
indicators. (Br J Ind Med, 1986 Sep, Abstract available) [MEDLINE]
12Kumar S, et al; Cyclic adenosine 3':5'-monophosphate phosphodiesterase
activity in malignant and cyclic adenosine 3':5'-monophosphate-induced
"differentiated" neuroblastoma cells. (Cancer Res, 1975 Jan, Abstract
available) [MEDLINE]
13Mitchell RA, et al; Erythrocyte porphobilinogen synthase
(delta-aminolaevulinate dehydratase) activity: a reliable and
quantitative indicator of lead exposure in humans. (Clin Chem, 1977 Jan,
Abstract available) [MEDLINE]
14Noma A, et al; Comparative studies on cholesterol oxidases from
different sources. (Clin Chim Acta, 1976 Dec, Abstract available)
[MEDLINE]
15Warwas M, et al; Cathepsins B1 from human fetal membranes. (Biochim
Biophys Acta, 1976 Apr, Abstract available) [MEDLINE]
16Dunbabin DW, et al; Lead poisoning from Indian herbal medicine
(Ayurveda) [see comments] (Med J Aust, 1992 Dec, Abstract available)
[MEDLINE]
17Alton KB, et al; High-performance liquid chromatographic determination
of N-[2(S)-(mercaptomethyl)-3-(2-methylphenyl)-1-oxopropyl]-L-methionine,
the active plasma metabolite of a prodrug atriopeptidase inhibitor (SCH
42495), using a thiol selective (Au/Hg) amperometric detector. (J
Chromatogr, 1992 Sep, Abstract available) [MEDLINE]
18Szász I, et al; Phosphorylation of the Ca2+ pump intermediate in intact
red cells, isolated membranes and inside-out vesicles. (Mol Cell Biochem,
1978 Dec, Abstract available) [MEDLINE]
19Margel S; A novel approach for heavy metal poisoning treatment, a
model. Mercury poisoning by means of chelating microspheres:
hemoperfusion and oral administration. (J Med Chem, 1981 Oct, Abstract
available) [MEDLINE]
20Menu Position #20
Sandborgh Englund G, et al; No evidence of renal toxicity from amalgam
fillings [see comments] (Am J Physiol, 1996 Oct, Abstract available)
[MEDLINE]
21Pratt CW, et al; The effect of zinc and other divalent cations on the
structure and function of human alpha 2-macroglobulin. (Biochim Biophys
Acta, 1984 Dec, Abstract available) [MEDLINE]
22De Bisschop HC, et al; Stereoselective hydrolysis of soman in human
plasma and serum. (Biochem Pharmacol, 1987 Nov, Abstract available)
[MEDLINE]
23Aposhian HV, et al; Mobilization of heavy metals by newer,
therapeutically useful chelating agents. (Toxicology, 1995 Mar, Abstract
available) [MEDLINE]
24Hainaut P, et al; A structural role for metal ions in the "wild-type"
conformation of the tumor suppressor protein p53. (Cancer Res, 1993 Apr,
Abstract available) [MEDLINE]
25Hainaut P, et al; A structural role for metal ions in the "wild-type"
conformation of the tumor suppressor protein p53. (Cancer Res, 1993 Apr,
Abstract available) [MEDLINE]
26ten Bruggenkate CM, et al; Lead poisoning with pigmentation of the oral
mucosa. Review of the literature and report of a case. (Oral Surg Oral
Med Oral Pathol, 1975 May, Abstract available) [MEDLINE]
27Teng YS, et al; Human erythrocyte pyrimidine nucleoside monophosphate
kinase. Partial purification and properties of two allelic gene products.
(J Biol Chem, 1976 Jul, Abstract available) [MEDLINE]
28Aaseth J; Recent advance in the therapy of metal poisonings with
chelating agents. (Hum Toxicol, 1983 Apr, Abstract available) [MEDLINE]
29Domingo JL; Prevention by chelating agents of metal-induced
developmental toxicity. (Reprod Toxicol, 1995 Mar, Abstract available)
[MEDLINE]
30Menu Position #30
Rabel SR, et al; Determination of intracellular levels of
6-mercaptopurine metabolites in erythrocytes utilizing capillary
electrophoresis with laser-induced fluorescence detection. (Anal Biochem,
1995 Jan, Abstract available) [MEDLINE]
31Shatzman AR, et al; Metal-binding characteristics of the parotid
salivary protein gustin. (Biochim Biophys Acta, 1980 May, Abstract
available) [MEDLINE]
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Record 1 from database: MEDLINE
Return To Top
Title
HgEDTA complex inhibits GTP interactions with the E-site of brain
beta-tubulin.
Author
Duhr EF; Pendergrass JC; Slevin JT; Haley BE
Address
Division of Medicinal Chemistry and Pharmaceutics, College of Pharmacy,
University of Kentucky Medical Center, Lexington.
Source
Toxicol Appl Pharmacol, 1993 Oct, 122:2, 273-80
Abstract
We have found that EDTA and EGTA complexes of Hg2+, which conventional
wisdom has assumed are biologically inert, are potentially injurious to
the neuronal cytoskeleton. Tubulin, a major protein component of the
neuronal cytoskeleton, is the target of multiple toxicants, including
many heavy metal ions. Among the mercurials, inorganic mercuric ion
(Hg2+) is one of the most potent inhibitors of microtubule polymerization
both in vivo and in vitro. In contrast to other heavy metals, the
capacity of Hg2+ to inhibit microtubule polymerization or disrupt formed
microtubules cannot be prevented by the addition of EDTA and EGTA, both
of which bind Hg2+ with very high affinity. To the contrary, the addition
of these two chelating agents potentiates Hg2+ inhibition of tubulin
polymerization. Results herein show that HgEDTA and HgEGTA inhibit
tubulin polymerization by disrupting the interaction of GTP with the
E-site of brain beta-tubulin, an obligatory step in the polymerization of
tubulin. Both HgEDTA and HgEGTA, but not free Hg2+, prevented binding of
[32P]8N3GTP, a photoaffinity nucleotide analog of GTP, to the E-site and
displaced bound [32P]8N3GTP at low micromolar concentrations. This
complete inhibition of photoinsertion into the E-site occurred in a
concentration- and time-dependent fashion and was specific for Hg2+
complexes of EDTA and EGTA, among the chelating agents tested. Given the
ubiquity of Hg2+ in the environment and the widespread use of EDTA in
foodstuffs and medicine, these mercury complexes may pose a potentially
serious threat to human health and play a role in diseases of the
neuronal cytoskeleton.
Language of Publication
English
Unique Identifier
94024905
Return To Top
MeSH Heading (Major)
Brain|*DE/ME; Edetic Acid|*PD; Guanosine Triphosphate|AA/DU/*ME;
Mercury|*PD; Tubulin|*DE/ME
MeSH Heading
Affinity Labels|DU; Animal; Azides|DU; Binding Sites|DE; Human; In Vitro;
Magnesium|PD; Male; Phosphorus Radioisotopes|DU; Photochemistry; Protein
Binding|DE; Rats; Rats, Sprague-Dawley; Support, Non-U.S. Gov't; Support,
U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.
Publication Type
JOURNAL ARTICLE
ISSN
0041-008X
Country of Publication
UNITED STATES
Record 2 from database: MEDLINE
Return To Top
Title
A simple ICP-MS procedure for the determination of total mercury in whole
blood and urine.
Author
Kalamegham R; Ash KO
Address
Department of Pathology, University of Utah Medical Center, Salt Lake
City 84108.
Source
J Clin Lab Anal, 1992, 6:4, 190-3
Abstract
A simple and sensitive procedure for total mercury in whole blood and
urine using inductively coupled plasma-mass spectrometry (ICP-MS) is
described. Specimens are prepared by precipitation-extraction with 50%
v/v hydrochloric acid containing EDTA and cysteine, centrifuged, and
filtered through fritended screening column; the filtrates are directly
analyzed by ICP-MS. The method is linear between 2 and 200 micrograms/L
in the specimen with an absolute sensitivity of 0.2 microgram/L in the
final supernatant. The assay variability at various concentrations
(microgram/L) of mercury are as follows: intra-assay whole blood (n =
20)-4.6 +/- 0.6 (c.v. 12.3%), 18.3 +/- 1.1 (c.v. 6.1%), 56.4 +/- 2.8
(c.v. 5.0%); inter-assay whole blood (n = 15)-5.7 +/- 1.0 (c.v. 16.8%),
19.7 +/- 2.7 (c.v. 13.5%), and 50.1 +/- 6.9 (c.v. 13.7%); urine (n =
20)-9.3 +/- 1.2 (c.v. 12.9%), 29.6 +/- 2.2 (c.v. 7.4%). Recovery of
organic and inorganic mercury from blood samples ranges from 91.6% to
110.2%. The method is suitable for analysis of total mercury, both
organic and inorganic, in whole blood and urine.
Language of Publication
English
Unique Identifier
93019810
Return To Top
MeSH Heading (Major)
Mercury|*BL/*UR; Spectrum Analysis, Mass|*MT/SN
MeSH Heading
Argon; Cysteine; Edetic Acid; Human; Hydrochloric Acid; Methylmercury
Compounds|BL/UR; Sensitivity and Specificity
Publication Type
JOURNAL ARTICLE
ISSN
0887-8013
Country of Publication
UNITED STATES
Record 3 from database: MEDLINE
Return To Top
Title
Inhibition of paraoxonase activity in human liver microsomes by exposure
to EDTA, metals and mercurials.
Author
Gonzalvo MC; Gil F; Hernández AF; Villanueva E; Pla A
Address
Department of Legal Medicine, Faculty of Medicine, Granada, Spain.
Source
Chem Biol Interact, 1997 Aug, 105:3, 169-79
Abstract
Inhibition of paraoxon hydrolase (paraoxonase) activity by 'in vitro'
exposure to EDTA, Mg2+, Co2+, Ba2+, La3+, Zn2+, Cu2+, Hg2+,
p-hydroxymercuribenzoate (p-OH-MB) and phenyl mercuric acetate (PMA) was
investigated in human liver microsomes. Enzyme activity was totally
inhibited by 1 mM EDTA in a time-dependent manner, in contrast to
previous data obtained in rat liver where an EDTA-resistant fraction was
detected. The possible influence of postmortem changes in these results
was checked in a parallel experiment using rat livers with different
postmortem intervals. From our results the existence in human liver of an
EDTA-resistant fraction cannot be discarded. Ba, La and PMA showed
immediate inhibition. By contrast the other compounds tested were
time-dependent inhibitors. Ba and Zn showed the highest IC50 values. Cu
and mercurials (Hg, p-OH-MB, PMA) were the most potent inhibitors of
human liver paraoxonase. Kinetic analysis (Lineweaver-Burk and Dixon
plots) indicated that different inhibitors exhibit different inhibition
patterns: competitive (EDTA, Ba, La, Cu, p-OH-MB and PMA), non
competitive (Zn) and mixed (Hg). The pretreatment of sample with
dithiothreitol (DTT) protects against the inhibitory effect of
mercurials. Furthermore after inhibition by mercurials the activity was
restored by DTT. These results confirmed the essential role of the -SH
groups to maintain the catalytic activity of paraoxonase and suggest the
existence of two types of -SH groups that could differ in their
localization.
Language of Publication
English
Unique Identifier
97437462
Return To Top
MeSH Heading (Major)
Edetic Acid|*PD; Enzyme Inhibitors|*PD; Esterases|*AI/ME; Mercury
Compounds|*PD; Metals|*PD; Microsomes, Liver|DE/*EN
MeSH Heading
Animal; Dithiothreitol|PD; Enzyme Activation; Human; Kinetics; Rats;
Sulfhydryl Compounds|ME; Support, Non-U.S. Gov't
Publication Type
JOURNAL ARTICLE
ISSN
0009-2797
Country of Publication
IRELAND
Record 4 from database: MEDLINE
Return To Top
Title
Human semen ribonuclease. Location, properties and inhibition by sodium
dodecyl sulfate, zinc sulfate and EDTA.
Author
Mujica A; Romero G; Hernandez Montes H
Address
Source
Int J Fertil, 1976, :2, 109-13
Abstract
Optimal conditions were established for RNase activity measurement. The
enzyme was measured in human seminal plasma as well as in spermatozoa.
Results suggest that sperm enzyme may come from seminal plasma
contamination and that RNase may be used as a marker enzyme for seminal
plasma contamination. Sodium dodecylsulfate, a reagent utilized to
produce the solubilization of the spermatozoa, produced a very strong
inhibition of the RNase at low concentrations (530 muM). Zinc sulfate and
EDTA also produced inhibition of the RNase activity. Such inhibition may
be very useful in future studies of RNA metabolism in human spermatozoa.
Language of Publication
English
Unique Identifier
76259358
Order full text for this document
MeSH Heading (Major)
Edetic Acid|*PD; Ribonucleases|*/ME; Semen|*EN; Sodium Dodecyl
Sulfate|*PD; Zinc|*PD
MeSH Heading
Dithiothreitol|PD; Human; Hydrogen-Ion Concentration; Male; Mercury|PD;
Spermatozoa|EN
Publication Type
JOURNAL ARTICLE
ISSN
0020-725X
Country of Publication
UNITED STATES
Record 5 from database: MEDLINE
Return To Top
Title
Effects of plumbous ion on guanine metabolism.
Author
Farkas WR; Stanawitz T
Address
Source
J Inorg Biochem, 1979 Aug, 11:1, 31-8
Abstract
The enzyme guanine aminohydrolase (guanase) is inhibited by low levels of
Pb2+. The inhibition is noncompetitive and the Ki is 3.0 X 10(-6) M. The
only other heavy metals that are inhibitory at low concentrations are
Ag+, which is 36% more, and Hg2+, which is about 50% less inhibitory than
Pb2+. The inhibition of guanase by Pb2+ and Hg2+ is synergistic and the
inhibition of the enzyme was readily reversed by EDTA. The relationship
of these studies with guanase and to the etiology and treatment of
saturnine gout, which appears in humans suffering from lead poisoning, is
discussed.
Language of Publication
English
Unique Identifier
80008188
Return To Top
MeSH Heading (Major)
Aminohydrolases|*AI; Guanine Deaminase|*AI; Lead|*PD
MeSH Heading
Cations, Divalent; Edetic Acid|PD; Gout|EN/ET; Human; Kinetics; Lead
Poisoning|EN; Mercury|PD; Silver|PD; Support, U.S. Gov't, P.H.S.;
Xanthine Oxidase|ME
Publication Type
JOURNAL ARTICLE
ISSN
0162-0134
Country of Publication
UNITED STATES
Record 6 from database: MEDLINE
Return To Top
Title
Metal excretion and magnesium retention in patients with intermittent
claudication treated with intravenous disodium EDTA.
Author
Guldager B; J?rgensen PJ; Grandjean P
Address
Department of Surgery, Hiller?d Hospital, Denmark.
Source
Clin Chem, 1996 Dec, 42:12, 1938-42
Abstract
Sixty patients with intermittent claudication participated in a
double-blind placebo-controlled trial of 20 courses of intravenous
chelation therapy with 3 g of disodium EDTA vs placebo during 5-9 weeks.
After the first infusion, the 24-h urinary excretion of lead and zinc was
approximately 25-fold higher in the EDTA-treated group; relative
differences for copper and calcium were smaller. Urinary magnesium
excretion in the EDTA-treated group was one-third less than in the
control group. After the treatment period, the blood lead concentration
had decreased by approximately 73% and the serum zinc concentration by
approximately 34%; other changes in blood concentrations were negligible.
The loss of essential minerals and the possible redistribution of lead in
the body may constitute a disadvantage that should be taken into account
in repeated intravenous EDTA treatment.
Language of Publication
English
Unique Identifier
97124459
Return To Top
MeSH Heading (Major)
Edetic Acid|*TU; Intermittent Claudication|*DT/ME; Magnesium|BL/*ME/UR;
Metals|*UR
MeSH Heading
Adult; Aged; Aged, 80 and over; Calcium|UR; Copper|BL/UR; Double-Blind
Method; Human; Lead|BL/UR; Mercury|BL; Middle Age; Placebos; Support,
Non-U.S. Gov't; Zinc|BL/UR
Publication Type
CLINICAL TRIAL; JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
ISSN
0009-9147
Country of Publication
UNITED STATES
Record 7 from database: MEDLINE
Return To Top
Title
HgEDTA complex inhibits GTP interactions with the E-site of brain
beta-tubulin.
Author
Duhr EF; Pendergrass JC; Slevin JT; Haley BE
Address
Division of Medicinal Chemistry and Pharmaceutics, College of Pharmacy,
University of Kentucky Medical Center, Lexington.
Source
Toxicol Appl Pharmacol, 1993 Oct, 122:2, 273-80
Abstract
We have found that EDTA and EGTA complexes of Hg2+, which conventional
wisdom has assumed are biologically inert, are potentially injurious to
the neuronal cytoskeleton. Tubulin, a major protein component of the
neuronal cytoskeleton, is the target of multiple toxicants, including
many heavy metal ions. Among the mercurials, inorganic mercuric ion
(Hg2+) is one of the most potent inhibitors of microtubule polymerization
both in vivo and in vitro. In contrast to other heavy metals, the
capacity of Hg2+ to inhibit microtubule polymerization or disrupt formed
microtubules cannot be prevented by the addition of EDTA and EGTA, both
of which bind Hg2+ with very high affinity. To the contrary, the addition
of these two chelating agents potentiates Hg2+ inhibition of tubulin
polymerization. Results herein show that HgEDTA and HgEGTA inhibit
tubulin polymerization by disrupting the interaction of GTP with the
E-site of brain beta-tubulin, an obligatory step in the polymerization of
tubulin. Both HgEDTA and HgEGTA, but not free Hg2+, prevented binding of
[32P]8N3GTP, a photoaffinity nucleotide analog of GTP, to the E-site and
displaced bound [32P]8N3GTP at low micromolar concentrations. This
complete inhibition of photoinsertion into the E-site occurred in a
concentration- and time-dependent fashion and was specific for Hg2+
complexes of EDTA and EGTA, among the chelating agents tested. Given the
ubiquity of Hg2+ in the environment and the widespread use of EDTA in
foodstuffs and medicine, these mercury complexes may pose a potentially
serious threat to human health and play a role in diseases of the
neuronal cytoskeleton.
Language of Publication
English
Unique Identifier
94024905
Return To Top
MeSH Heading (Major)
Brain|*DE/ME; Edetic Acid|*PD; Guanosine Triphosphate|AA/DU/*ME;
Mercury|*PD; Tubulin|*DE/ME
MeSH Heading Affinity Labels|DU; Animal; Azides|DU; Binding Sites|DE;
Human; In Vitro; Magnesium|PD; Male; Phosphorus Radioisotopes|DU;
Photochemistry; Protein Binding|DE; Rats; Rats, Sprague-Dawley; Support,
Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't,
P.H.S.
Publication Type
JOURNAL ARTICLE
ISSN
0041-008X
Country of Publication
UNITED STATES
Record 8 from database: MEDLINE
Return To Top
Return To Menu Position #10
Title
Trace element studies in three patients and a fetus with Menkes' disease.
Effect of copper therapy.
Author
Nooijen JL; De Groot CJ; Van den Hamer CJ; Monnens LA; Willemse J;
Niermeijer MF
Address
Source
Pediatr Res, 1981 Mar, 15:3, 284-9
Abstract
This paper reports the results of a multielement analysis of postmortem
samples of Menkes patients, of which one was untreated and two had been
treated for various lengths of time with intramuscular injections of
copper-EDTA. The findings have been compared with data from a Menkes
fetus and from controls. The results confirm that copper accumulates in
various tissues and demonstrate a further increase in copper levels as a
result of the treatment with copper-EDTA. Although no clinical
improvement was observed, the levels of some copper-containing enzymes
normalized during the copper-therapy. Furthermore, in agreement with the
identification of the copper-binding protein in the kidney as
metallothionein, it was found that not only copper, but also zinc,
cadmium, and mercury are trapped in this tissue. A low copper
concentration in the brain was also found in a Menkes fetus, indicating
that brain damage might already have occurred before birth. Speculation
Until recently, Menkes' disease was considered to be due to copper
deficiency. However, the symptoms are more typical of a storage disease
in which copper is irreversibly trapped in some tissues, in particular in
the kidneys, by metallothionein. This abnormal storage pattern gives rise
to copper deficiency elsewhere in the organism, particularly in the brain
where it may cause irreversible damage in the foetus. Parenteral
administration of copper does not lead to clinical improvement. The only
"therapy" that seems feasible at present is tracing the carriers of the
disease and advising abortion when prenatal diagnosis indicates a male
fetus carrying the disease.
Language of Publication
English
Unique Identifier
81174435
Return To Top
Return To Menu Position #10
MeSH Heading (Major)
Brain Diseases, Metabolic|*DT; Copper|AN/*TU; Menkes Kinky Hair
Syndrome|DI/*DT; Trace Elements|*AN
MeSH Heading
Arsenic|AN; Cadmium|AN; Case Report; Cobalt|AN; Comparative Study; Edetic
Acid; Female; Fetal Diseases|DI; Human; Infant; Iron|AN; Male;
Mercury|AN; Molybdenum|AN; Pregnancy; Selenium|AN; Tissue Distribution;
Zinc|AN
Publication Type
JOURNAL ARTICLE
ISSN
0031-3998
Country of Publication
UNITED STATES
Record 9 from database: MEDLINE
Return To Top
Return To Menu Position #10
Title
Monoglyceride and diglyceride lipases from human platelet microsomes.
Author
Chau LY; Tai HH
Address
Division of Medicinal Chemistry and Pharmacognosy, College of Pharmacy,
University of Kentucky, Lexington 405367-0082.
Source
Biochim Biophys Acta, 1988 Dec, 963:3, 436-44
Abstract
In the present study, we have characterized the properties of both
diglyceride lipase (lipoprotein lipase, EC 3.1.1.24) and monoglyceride
lipases (acylglycerol lipase, EC 3.1.1.23) in an attempt to assess the
potential roles of these two enzymes in the release of arachidonate in
activated human platelets. Diglyceride lipase exhibited maximal activity
at pH 3.5, whereas monoglyceride lipase showed optimal activity at pH
7.0. Neither of the lipases were inhibited by EDTA or stimulated by Ca2+,
Mg2+ or Mn2+. Both enzymes, however, were strongly inhibited by Hg2+ and
Cu2+, indicating the involvement of sulfhydryl groups in catalytic
activity. This suggestion was further supported by their sensitivity
toward sulfhydryl inhibitors, with monoglyceride lipase being more
susceptible to inhibition. Both lipases were found to be inhibited to a
different degree by a variety of antiplatelet drugs blocking aggregation
and arachidonate release. Kinetic studies indicated that dichotomous
metabolism of diacylglycerol to monoacylglycerol and to phosphatidic acid
could occur concurrently, since the apparent Km values for diglyceride
lipase and for diglyceride kinase were comparable. Further studies showed
that the specific activity of monoglyceride lipase was at least 100-fold
higher than that of diglyceride lipase, indicating that the rate-limiting
step in the release of arachidonate was the reaction catalyzed by
diglyceride lipase.
Language of Publication
English
Unique Identifier
89062521
Return To Top
Return To Menu Position #10
MeSH Heading (Major)
Blood Platelets|*EN; Carboxylic Ester Hydrolases|*BL; Lipoprotein
Lipase|*BL; Monoacylglycerol Lipases|*BL
MeSH Heading
Calcium|PD; Copper|PD; Edetic Acid|PD; Heat; Human; Hydrogen-Ion
Concentration; Kinetics; Magnesium|PD; Manganese|PD; Mercury|PD;
Microsomes|EN; Platelet Aggregation Inhibitors|PD; Substrate Specificity;
Sulfhydryl Reagents|PD; Support, Non-U.S. Gov't; Support, U.S. Gov't,
P.H.S.
Publication Type
JOURNAL ARTICLE
ISSN
0006-3002
Country of Publication
NETHERLANDS
Record 10 from database: MEDLINE
Return To Top
Return To Menu Position #10
Title
Differential metal response and regulation of human heavy metal-inducible
genes.
Author
Murata M; Gong P; Suzuki K; Koizumi S
Address
Division of Hazard Assessment, National Institute of Industrial Health,
Kawasaki, Japan.
Source
J Cell Physiol, 1999 Jul, 180:1, 105-13
Abstract
A number of heavy metal-inducible genes have been reported, but their
ranges of response to various metal species are not well known. It is
also unclear if these genes are regulated through common mechanisms. To
answer these questions, we compared induction kinetics of human
metal-inducible genes including the MT-IIA (coding for a metallothionein
isoform), hsp70 (coding for the 70-kDa heat-shock protein), and c-fos
genes in HeLa cells exposed to Zn, Cd, Ag, Hg, Cu(II), Co, or Ni ions.
Transcripts from these three genes were increased after exposure to wide
ranges of metals, but each gene was unique in its induction kinetics.
Generally, induction was observed at lower metal concentrations in the
order of MT-IIA, hsp70, and c-fos. These genes also showed differential
responses in time course: more rapid induction was observed in the order
of c-fos, hsp70, and MT-IIA after exposure to Zn or Cd. Since the
metal-responsive element (MRE) and heat shock element (HSE) of the MT-IIA
and hsp70 genes, respectively, are thought to be the cis-acting DNA
elements that mediate metal response, we compared the properties of
proteins that specifically bind to these elements. MRE-binding activity
was detected only in the extract from cells exposed to Zn. By contrast,
HSE-binding activity was detected in extracts from cells treated with Zn,
Cd, Ag, and Cu. The former was also activated by Zn in vitro, while the
latter was not. Each of these DNA-binding activities showed no affinity
to the recognition sequence of the other. These results demonstrate that
the human metal-inducible genes have broad ranges of response to a
variety of heavy metals, but suggest that they are probably regulated
through independent mechanisms.
Language of Publication
English
Unique Identifier
99288869
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MeSH Heading (Major)
Heat-Shock Proteins 70|*GE; Metallothionein|*GE; Metals, Heavy|*PD;
Proto-Oncogene Proteins c-fos|*GE
MeSH Heading
Blotting, Northern; Cadmium|PD; Chelating Agents|PD; Cobalt|PD;
Copper|PD; Dose-Response Relationship, Drug; DNA-Binding Proteins|ME;
Edetic Acid|PD; Gene Expression|DE; Gold|PD; Hela Cells; Human;
Mercury|PD; Nickel|PD; Nuclear Proteins|ME; Oligonucleotide Probes; RNA,
Messenger|AN; Transcription Factors|ME; Transcription, Genetic|PH;
Zinc|PD
Publication Type
JOURNAL ARTICLE
ISSN
0021-9541
Country of Publication
UNITED STATES
Record 11 from database: MEDLINE
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Title
Mobilisation of heavy metals into the urine by CaEDTA: relation to
erythrocyte and plasma concentrations and exposure indicators.
Author
Araki S; Aono H; Murata K
Address
Source
Br J Ind Med, 1986 Sep, 43:9, 636-41
Abstract
To investigate the effects of calcium disodium ethylenediamine
tetra-acetate (CaEDTA) on the urinary excretion, erythrocyte, and plasma
concentrations and exposure indicators of seven heavy metals, CaEDTA was
administered by intravenous infusion to 20 workers exposed to lead, zinc,
and copper. The workers' blood lead concentrations ranged from 22 to 59
micrograms/dl (mean 38 micrograms/dl (1.8 mumol/l]. The 24 hour urinary
excretion of metals after CaEDTA administration (mobilisation yield) was
on average 13 times the background excretion for lead, 11 times for zinc,
3.8 times for manganese, 3.4 times for cadmium, 1.3 times for copper, and
1.1 times for chromium; no significant increase was found for mercury.
The mobilisation yield of lead (MPb) was significantly correlated with
whole blood and erythrocyte concentrations and the urinary excretion of
lead but not with its plasma concentration; similarly, the mobilisation
yield of cadmium was significantly correlated with its erythrocyte
concentration. In addition, MPb was significantly correlated with
intra-erythrocytic enzyme delta-aminolaevulinic acid dehydratase activity
and urinary coproporphyrin excretion. The relation between the
mobilisation yield of heavy metals and their body burden (and toxic
signs) is discussed in the light of these findings.
Language of Publication
English
Unique Identifier
87000506
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MeSH Heading (Major)
Edetic Acid|*PD; Erythrocytes|*ME; Metals|*ME
MeSH Heading
Adult; Cadmium|ME; Chromium|ME; Copper|ME; Environmental Exposure; Human;
Lead|ME; Male; Manganese|ME; Mercury|ME; Middle Age; Zinc|ME
Publication Type
JOURNAL ARTICLE
ISSN
0007-1072
Country of Publication
ENGLAND
Record 12 from database: MEDLINE
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Title
Cyclic adenosine 3':5'-monophosphate phosphodiesterase activity in
malignant and cyclic adenosine 3':5'-monophosphate-induced
"differentiated" neuroblastoma cells.
Author
Kumar S; Becker G; Prasad KN
Address
Source
Cancer Res, 1975 Jan, 35:1, 82-7
Abstract
The regulation of cyclic adenosine 3:5-monophosphate (cyclic AMP)
phosphodiesterase activity in homogenates of malignant and cyclic
AMP-induced "differentiated" neuroblastoma cells was studied.
Neuroblastoma cells of at least three mouse and one human clone had both
the low (2 to 4 muM) and the high (66 to 106 muM) Km phosphodiesterase.
In cyclic AMP-induced differentiated cells the values of Km were
decreased, whereas the values of Vmax appeared to be slightly increased.
Magnesium and manganese stimulated phosphodiesterase activity. Calcium,
zinc, copper, mercury, ethylenediaminetetraacetic acid, and imidazole
completely inhibited phosphodiesterase activity in malignant cells,
whereas the above agents, except ethylenediaminetetraacetic acid, only
partially inhibited enzyme activity in differentiated cells.
Ethylenediaminetetraacetic acid completely reduced phosphodiesterase
activity in differentiated cells. The pH optimum for phosphodiesterase
activity was about 8 in both malignant and differentiated cells. The
present studies show that the values of Km and Vmax and the sensitivity
of phosphodiesterase activity to divalent ions change in cyclic
AMP-induced differentiated neuroblastoma cells, and therefore we propose
that the reverse may be true during malignant transformation of nerve
cells.
Language of Publication
English
Unique Identifier
75074120
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MeSH Heading (Major)
Cell Differentiation|*; Cyclic AMP|ME/*PD; Neuroblastoma|*EN; Phosphoric
Diester Hydrolases|*ME
MeSH Heading
Adenylate Cyclase|ME; Animal; Calcium|PD; Caudate Nucleus|EN; Clone
Cells; Copper|PD; Depression, Chemical; Edetic Acid|PD; Human;
Hydrogen-Ion Concentration; Imidazoles|PD; Magnesium|PD; Manganese|PD;
Mercury|PD; Mice; Stimulation, Chemical; Support, U.S. Gov't, Non-P.H.S.;
Time Factors; Zinc|PD
Publication Type
JOURNAL ARTICLE
ISSN
0008-5472
Country of Publication
UNITED STATES
Record 13 from database: MEDLINE
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Title
Erythrocyte porphobilinogen synthase (delta-aminolaevulinate dehydratase)
activity: a reliable and quantitative indicator of lead exposure in
humans.
Author
Mitchell RA; Drake JE; Wittlin LA; Rejent TA
Address
Source
Clin Chem, 1977 Jan, 23:1, 105-11
Abstract
We assessed optimal conditions for assay of porphobillinogen synthase (EC
4.2.1.24) activity in human blood containing abnormally high
concentrations of lead. Zn2+and -SH, both required for complete
activation of the enzyme, had additive effects. Using a modified method
based on these studies, we found blood lead concentration to be strictly
proportional to ln(activated/nonactivated) enzyme activity. One brand of
commercially available "lead-free" tubes contained a substance that
interfered with this relationship. In vitro studies, with the modified
assay, showed ALAD to be activated by low concentrations but inactivated
by high concentrations of Hg2+, Cd2+, and ethylenediaminetetraacetate. We
fouund no genetically influenced differences among unexposed individuals
when in(activated/nonactivated) enzyme activities were compared. The
technique is suitable for use in screening for lead poisoning in humans.
Language of Publication
English
Unique Identifier
77089786
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MeSH Heading (Major)
Erythrocytes|*EN; Hydro-Lyases|*BL; Lead Poisoning|*DI/*EN;
Porphobilinogen Synthase|*BL
MeSH Heading
Cadmium|PD; Edetic Acid|PD; Enzyme Activation|DE; Glutathione|PD; Human;
Kinetics; Lead|BL/PD; Mercury|PD; Sodium|PD; Zinc|PD
Publication Type
JOURNAL ARTICLE
ISSN
0009-9147
Country of Publication
UNITED STATES
Record 14 from database: MEDLINE
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Title
Comparative studies on cholesterol oxidases from different sources.
Author
Noma A; Nakayama K
Address
Source
Clin Chim Acta, 1976 Dec, 73:3, 487-96
Abstract
1. Comparison of the characteristics of cholesterol oxidases from
different sources was made by a new polarographic method for measurement
of the oxygen-consumption rate. 2. A pH optimum of 7.0 was observed for
cholesterol oxidases isolated from Nocardia and Brevibacterium, pH 5.0
for the enzyme from Schizophyllum and pH 7.5 for the enzyme from
Streptomyces. 3. In the system used in the present study, Ca2+ and Mg2+
had no effect on these enzyme activities. On the other hand, the
Schizophyllum enzyme was strongly inhibited by increasing concentrations
of Cu2+, whereas the brevibacterium enzyme was slightly activated by them
and Nocardia and Streptomyces enzymes were not affected. Hg2+ strongly
inhibited the activities of enzymes the Schizophyllum enzyme. 4. Using
serum as substrate, the cholesterol oxidases employed, except for the
enzyme from Streptomyces, were not active without detergent in the
reaction mixture. Effects of various detergents at various concentrations
on the enzyme activities were studied. 5. Results of studies on the
reaction of cholesterol oxidases on free cholesterol in low-and
high-density lipoproteins were also compared.
Language of Publication
English
Unique Identifier
77067450
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MeSH Heading (Major)
Cholesterol|*BL; Hydroxysteroid Dehydrogenases|*ME
MeSH Heading
Brevibacterium|EN; Calcium|PD; Comparative Study; Copper|PD;
Detergents|PD; Edetic Acid|PD; Human; Hydrogen-Ion Concentration;
Kinetics; Magnesium|PD; Mercury|PD; Nocardia|EN; Osmolar Concentration;
Schizophyllum|EN; Species Specificity; Streptomyces|EN
Publication Type
JOURNAL ARTICLE
ISSN
0009-8981
Country of Publication
NETHERLANDS
Record 15 from database: MEDLINE
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Title
Cathepsins B1 from human fetal membranes.
Author
Warwas M; Dobryszycka W
Address
Source
Biochim Biophys Acta, 1976 Apr, 429:2, 573-80
Abstract
Cathepsins B1 (EC 3.4.22.1) were isolated from fetal membranes of human
placenta, i.e. amnion and chorion-decidua. Purification of the enzymes
was achieved by the freezing-thawing technique, ammonium sulphate
fractionation and Sephadex gel filtration. Cathepsis B1 separated either
from amnion or from chorion-decidua exhibited optimum activity at pH 6.2,
and an optimum temperature between 42-45 degrees C. They were inhibited
by heavy metals, and compounds which react with the thiol groups.
Isoelectric focusing demonstrated three isoenzymes of cathepsin B1
originating from chorion-decidua, while only one band was found for the
enzyme from amnion.
Language of Publication
English
Unique Identifier
76161400
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MeSH Heading (Major)
Amnion|*EN; Cathepsins|IP/*ME; Chorion|*EN; Fetal Membranes|*EN
MeSH Heading
Cations, Divalent; Edetic Acid|PD; Female; Human; Hydrogen-Ion
Concentration; Hydroxymercuribenzoates|PD; Iodoacetates|PD; Kinetics;
Mercury|PD; Organ Specificity; Pregnancy
Publication Type
JOURNAL ARTICLE
ISSN
0006-3002
Country of Publication
NETHERLANDS
Record 16 from database: MEDLINE
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Title
Lead poisoning from Indian herbal medicine (Ayurveda) [see comments]
Author
Dunbabin DW; Tallis GA; Popplewell PY; Lee RA
Address
Flinders Medical Centre, Bedford Park, Sa.
Source
Med J Aust, 1992 Dec, 157:11-12, 835-6
Abstract
OBJECTIVE: To present a case of lead poisoning following ingestion of
Indian herbal medicine. CLINICAL FEATURES: A 37-year-old man presented
with a history of abdominal pain, anorexia and malaise. He had recently
returned from a trip to India where he had been taking two different
herbal tonics. Investigation revealed low-grade hepatitis and normocytic
anaemia with prominent basophilic stippling. The blood lead concentration
was high, and analysis of the herbal tablets revealed a very high lead
content. INTERVENTION AND OUTCOME: The patient required narcotic
analgesia for abdominal pain and was treated with chelation therapy with
calcium ethylenediaminetetra-acetate (calcium EDTA) for five days which
resulted in a high urinary excretion of lead and resolution of his
symptoms over a period of several days. CONCLUSION: Lead poisoning in
Australia is usually the result of chronic industrial exposure, but
practitioners should be aware of the possibility of poisoning from other
domestic sources such as unglazed pottery, cosmetics and herbal remedies,
especially those from Asia and India, in which lead may be present in
high concentration. Patients from Asia who present with unexplained
anaemia or abdominal symptoms should be asked about exposure to such
sources.
Language of Publication
English
Unique Identifier
93086568
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MeSH Heading (Major)
Lead Poisoning|*ET; Medicine, Ayurvedic|*; Medicine, Herbal|*; Plants,
Medicinal|*/CH
MeSH Heading
Adult; Arsenic|AN; Case Report; Human; Lead|AN; Male; Mercury|AN
Publication Type
JOURNAL ARTICLE
ISSN
0025-729X
Country of Publication
AUSTRALIA
Record 17 from database: MEDLINE
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Title
High-performance liquid chromatographic determination of
N-[2(S)-(mercaptomethyl)-3-(2-methylphenyl)-1-oxopropyl]-L-methionine,
the active plasma metabolite of a prodrug atriopeptidase inhibitor (SCH
42495), using a thiol selective (Au/Hg) amperometric detector.
Author
Alton KB; Hernandez A; Alvarez N; Patrick JE
Address
Department of Drug Metabolism and Pharmacokinetics, Schering-Plough
Research Institute, Bloomfield, NJ 07003.
Source
J Chromatogr, 1992 Sep, 579:2, 307-17
Abstract
A high-performance liquid chromatographic assay for the determination of
N-[2(S)-(mercaptomethyl)-3-(2-methylphenyl)-1-oxopropyl]-L-methionine
(SCH 42354; II), the active metabolite of the atriopeptidase inhibitor
prodrug,
N-[2(S)-(acetylthiomethyl)-3-(2-methylphenyl)-1-oxopropyl]-L-methi onine
ethyl ester (SCH 42495; I), in human plasma was validated for use in
clinical pharmacokinetic studies. Plasma (200 microliters) was processed
by protein precipitation with acetone containing the internal standard,
N-[2(S)-(mercaptomethyl)-3-(2-methylphenyl)-1-oxopropyl]-L- ethionine
(III). Compound II was recovered (ca. 90%) in the supernatant after
centrifugation and prepared for injection by the addition of 0.15 M
monochloroacetic acid containing 0.2 mM EDTA. Separation of II and III
was accomplished on commercially available reversed-phase C8 columns
designed for the separation of basic compounds. Both compounds were
detected using amperometric detection (+0.125 V versus Ag/AgCl) on a
thin-layer Au/Hg amalgam electrode. The lower limit of quantitation was
10 ng/ml, where the inter-assay precision (coefficient of variation) was
+/- 11.4% and the inter-assay accuracy (bias) was +1.0%. No endogenous
interferences were observed in the extracts obtained from drug-free
plasma. The detector response (using either peak area or height ratios of
II to III) was linear from 0.01 to 1.0 micrograms/ml. Compound II was
stable in plasma supplemented with EDTA and sodium hydrogensulfite for at
least 3 months when stored frozen at -78 degrees C; no significant
decomposition of II was observed following three freeze-thaw cycles. The
feasibility of this liquid chromatographic assay with electrochemical
detection was demonstrated with plasma samples from hypertensive subjects
administered 100 mg of compound I.
Language of Publication
English
Unique Identifier
93055121
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MeSH Heading (Major)
Chromatography, High Pressure Liquid|*MT; Methionine|*AA/BL/ME;
Neprilysin|*AI/BL/ME
MeSH Heading
Gold; Human; Hypertension|BL; Mercury; Sulfhydryl Compounds
Publication Type
JOURNAL ARTICLE
ISSN
0021-9673
Country of Publication
NETHERLANDS
Record 18 from database: MEDLINE
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Title
Phosphorylation of the Ca2+ pump intermediate in intact red cells,
isolated membranes and inside-out vesicles.
Author
Szász I; Hasitz M; Sarkadi B; Gárdos G
Address
Source
Mol Cell Biochem, 1978 Dec, 22:2-3, 147-52
Abstract
Ca2+-entry into intact red cells containing [32P]-ATP increases the
phosphorylation of the 150 000 dalton polypeptide of the membrane. This
phosphorylation occurs even in Mg2+-depleted red cells. Extracellular
lanthanum applied during ATP-depletion further increases the Ca2+-induced
phosphorylation. In fragmented membranes or resealed insideout vesicles
(IOVs) membrane bound Mg2+ is sufficient to catalyze the phosphorylation
of spectrin 2 and Band 3 polypeptides with low concentrations (less than
micron of [32P]-ATP. In Ca-EDTA buffers one single polypeptide is
phosphorylated which is located in the 150 000 molecular weight region.
KmCa for phosphorylation is much lower (0.2 micron) than for active Ca2+
transport (40 micron) in IOVs. Lanthanum induced phosphorylation (up to
250 micron Lafree) is significantly greater than Ca2+-induced
phosphorylation. Hg2+ inhibits both Ca2+ and La3+ induced
phosphorylation. Ca2+-induced labelling can be rapidly "chased" by
unlabelled ATP+Mg2+, but not with EGTA+Mg2+. Dephosphorylation in Ca2+
phosphorylated membranes and IOVs is significantly inhibited by La3+. It
can be concluded that the mechanism of La3+ and Hg2+ inhibition of the
Ca2+ pump is different in intact cells and isolated membranes or Iovs.
Language of Publication
English
Unique Identifier
79134711
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MeSH Heading (Major)
Calcium|*BL/PD; Erythrocyte Membrane|DE/*ME; Erythrocytes|DE/*ME;
Membrane Proteins|*BL; Phosphoproteins|*BL
MeSH Heading
Biological Transport, Active|DE; Human; Lanthanum|PD; Mercury|PD;
Phosphorylation
Publication Type
JOURNAL ARTICLE
ISSN
0300-8177
Country of Publication
NETHERLANDS
Record 19 from database: MEDLINE
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Title
A novel approach for heavy metal poisoning treatment, a model. Mercury
poisoning by means of chelating microspheres: hemoperfusion and oral
administration.
Author
Margel S
Address
Source
J Med Chem, 1981 Oct, 24:10, 1263-6
Abstract
The chelating drugs BAL (2,3-dimercaptopropanol), EDTA
(ethylenediaminetetraacetic acid), and penicillamine
(2-amino-3-mercapto-3-methylbutanoic acid), which are used for metal
poisoning, are toxic and there is a real need for alternatives,
especially for severe cases. A novel approach for treatment of
heavy-metal poisoning is under investigation in our group. The approach
utilizes the synthesis of chelating microspheres specific for the desired
metallic compound. The microspheres are suggested for use in severe cases
by means of hemoperfusion, as a first aid, and then by oral
administration. As a model this approach was tried for mercury poisoning.
Polymercaptal microspheres of 0.8 micrometer average size were
synthesized. The microspheres have a high surface area, have a high
affinity toward organic and inorganic mercury compounds, and can compete
easily with albumin and cysteine in the ability to bind mercury
compounds. These microspheres also were encapsulated with agarose--a
blood compatible polymer--and were tried successfully for plasma
perfusion (in 10 min, 40% of CH3HgCl and of HgCl2 were removed from 20
ppm of poisoned plasma).
Language of Publication
English
Unique Identifier
82122390
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MeSH Heading (Major)
Chelating Agents|*AD/ME; Hemoperfusion|*; Mercury Poisoning|*TH
MeSH Heading
Administration, Oral; Human; Mercury|ME; Microspheres; Models, Biological
Publication Type
JOURNAL ARTICLE
ISSN
0022-2623
Country of Publication
UNITED STATES
Record 20 from database: MEDLINE
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Title
No evidence of renal toxicity from amalgam fillings [see comments]
Author
Sandborgh Englund G; Nygren AT; Ekstrand J; Elinder CG
Address
Department of Dental Toxicology, Karolinska Institute, Huddinge, Sweden.
Source
Am J Physiol, 1996 Oct, 271:4 Pt 2, R941-5
Abstract
Dental amalgam continuously releases mercury. Studies of sheep [Boyd et
al., Am. J. Physiol. 261 (Regulatory Integrative Comp. Physiol. 30):
R1010-R1014, 1991] showed decreased renal function after placement of
amalgam fillings. In this study, renal function was investigated in 10
healthy volunteers before and after amalgam removal. The subjects had an
average of 18 tooth surfaces filled with amalgam, which was removed
during one dental session. One week before and sixty days after removal,
the glomerular filtration rate (GFR) was determined by 51Cr-EDTA
clearance technique. Blood and urine samples were collected for analysis
of mercury, creatinine, beta 2-microglobulin,
N-acetyl-beta-glucosaminidase (NAG), and albumin 1 wk before and 1, 2,
and 60 days after amalgam removal. The plasma mercury concentration
increased significantly 1 day after removal. Sixty days later,
significantly lower mercury levels were found in blood, plasma, and
urine. The GFR values were similar before and after mercury exposure
(mean 94 and 94 ml/min per 1.73 m2, respectively). No detectable effects
occurred on excretion of NAG, beta 2-microglobulin, or albumin. It is
concluded that no signs of renal toxicity could be found in conjunction
with mercury released from amalgam fillings.
Language of Publication
English
Unique Identifier
97053473
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MeSH Heading (Major)
Dental Amalgam|*AE; Kidney|*DE; Mercury|*AE/BL
MeSH Heading
beta 2-Microglobulin|UR; Acetylglucosaminidase|UR; Adult; Albuminuria|UR;
Creatinine|ME; Female; Glomerular Filtration Rate|DE; Human; Male; Middle
Age; Support, Non-U.S. Gov't; Time Factors
Publication Type
JOURNAL ARTICLE
ISSN
0002-9513
Country of Publication
UNITED STATES
Record 21 from database: MEDLINE
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Title
The effect of zinc and other divalent cations on the structure and
function of human alpha 2-macroglobulin.
Author
Pratt CW; Pizzo SV
Address
Source
Biochim Biophys Acta, 1984 Dec, 791:2, 123-30
Abstract
Zinc binding to human alpha 2-macroglobulin was studied to assess its
involvement in the structure and function alpha 2-macroglobulin.
Equilibrium dialysis experiments indicated multiple classes of
zinc-binding sites, the one of highest affinity having a site number of
20 and a Kd value of 8 X 10(-7) M. Native alpha 2-macroglobulin and alpha
2-macroglobulin-trypsin complexes bound comparable amount of zinc. The
proteinase inhibitory activity of alpha 2-macroglobulin was not affected
by zinc binding at physiological concentrations nor by the removal of
zinc by EDTA. Above 25 microM zinc, alpha 2-macroglobulin activity
decreased, although binding of [125I]trypsin was not affected. When
nondenaturing gel electrophoresis was performed, the preparation of alpha
2-macroglobulin migrated as half-molecules at increasing zinc
concentration. Experiments with other divalent cations correlated
decreases in alpha 2-macroglobulin activity with apparent dissociation of
the alpha 2-macroglobulin tetramer in the presence of copper and mercury,
but not barium, cadmium or nickel. While zinc binding to alpha
2-macroglobulin does not function in proteinase inhibition, it might be
involved in zinc transport in vivo. At nonphysiological concentrations,
zinc and other divalent cations are useful as probes of protein
quaternary structure.
Language of Publication
English
Unique Identifier
85072921
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MeSH Heading (Major)
alpha-Macroglobulins|AI/*ME/PD; Zinc|ME/*PD
MeSH Heading
Binding Sites; Cations, Divalent; Copper|PD; Dialysis; Electrophoresis,
Polyacrylamide Gel; Human; Macromolecular Systems; Mercury|PD; Protease
Inhibitors|PD; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't,
P.H.S.; Trypsin|ME
Publication Type
JOURNAL ARTICLE
ISSN
0006-3002
Country of Publication
NETHERLANDS
Record 22 from database: MEDLINE
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Title
Stereoselective hydrolysis of soman in human plasma and serum.
Author
De Bisschop HC; De Meerleer WA; Van Hecke PR; Willems JL
Address
Technical Division of the Army, Department for Nuclear, Biological and
Chemical Protection, Vilvoorde, Belgium.
Source
Biochem Pharmacol, 1987 Nov, 36:21, 3579-85
Abstract
The contribution of various human serum and plasma fractions to the total
hydrolysis rate constants of the four isomers of soman is studied.
Spontaneous hydrolysis (as measured in buffer) occurs at a faster rate
for the C(+)P(+)- and C(-)P(-)-isomers. A stereoselectively catalyzed
hydrolysis of soman occurs in serum fractions IV and V (albumin). In
fraction V the C(+)P(+)- and C(-)P(-)-isomers are hydrolyzed at a faster
rate than their respective epimers, while in fraction IV-1 a
stereoselective effect towards C(+)P(+)-soman is found. All the
forementioned contributions, however, are negligible in comparison with
the stereoselective enzymatic hydrolysis of the P(+)-isomers. The latter
reaction is characterized by a significant lowering of the activation
energy as compared with the spontaneous hydrolysis of the P(+)-isomers.
Such a lowering in activation energy is not found for the hydrolysis of
the P(-)-isomers in whole serum or plasma; hence it can be concluded that
a phosphorylphosphatase hydrolyzes the P(+)-isomers in a stereoselective
way, the P(-)-isomers either not being affected by this (these) enzyme(s)
or the mechanism of catalysis being fundamentally different. This
conclusion is in agreement with the observations on the influence of Hg2+
on the hydrolysis of soman in serum; the hydrolysis of the P(+)-isomers
is significantly inhibited by 1 mM of Hg2+ while the P(-)-hydrolysis is
unaffected by this concentration of Hg2+. The action of some potential
inhibitors on this phosphorylphosphatase activity was studied.
Iodoacetate did not inhibit nor did Ba2+, Sr2+, Co2+ or Mn2+ show a
significant effect on the hydrolysis of the P(+)-isomers. On the other
hand the hydrolytic activity in serum was nearly completely inhibited by
EDTA but restored upon addition of Ca2+. These findings suggest that this
enzymatic activity can be classified as an arylesterase (paraoxonase).
Finally, the influence of pH on the hydrolytic activity shows a different
pattern for C(+)P(+)- and C(-)P(+)-soman, which may suggest that more
than one enzyme is involved in the degradation of soman.
Language of Publication
English
Unique Identifier
88049757
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MeSH Heading (Major)
Soman|*BL
MeSH Heading
Calcium|PD; Human; Hydrogen-Ion Concentration; Hydrolysis; Mercury|PD;
Stereoisomerism; Tromethamine
Publication Type
JOURNAL ARTICLE
ISSN
0006-2952
Country of Publication
ENGLAND
Record 23 from database: MEDLINE
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Title
Mobilization of heavy metals by newer, therapeutically useful chelating
agents.
Author
Aposhian HV; Maiorino RM; Gonzalez Ramirez D; Zuniga Charles M; Xu Z;
Hurlbut KM; Junco Munoz P; Dart RC; Aposhian MM
Address
Department of Molecular and Cellular Biology, University of Arizona,
Tucson 85721, USA.
Source
Toxicology, 1995 Mar, 97:1-3, 23-38
Abstract
Four chelating agents that have been used most commonly for the treatment
of humans intoxicated with lead, mercury, arsenic or other heavy metals
and metalloids are reviewed as to their advantages, disadvantages,
metabolism and specificity. Of these, CaNa2EDTA and dimercaprol (British
anti-lewisite, BAL) are becoming outmoded and can be expected to be
replaced by meso-2,3-dimercaptosuccinic acid (DMSA, succimer) for
treatment of lead intoxication and by the sodium salt of
2,3-dimercapto-1-propanesulfonic acid (DMPS, Dimaval) for treating lead,
mercury or arsenic intoxication. Meso-2,3-DMSA and DMPS are
biotransformed differently in humans. More than 90% of the DMSA excreted
in the urine is found in the form of a mixed disulfide in which each of
the sulfur atoms of DMSA is in disulfide linkage with an L-cysteine
molecule. After DMPS administration, however, acyclic and cyclic
disulfides of DMPS are found in the urine. The Dimaval-mercury challenge
test holds great promise as a diagnostic test for mercury exposure,
especially for low level mercurialism. Urinary mercury after Dimaval
challenge may be a better biomarker of low level mercurialism than
unchallenged urinary mercury excretion.
Language of Publication
English
Unique Identifier
95232791
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MeSH Heading (Major)
Chelating Agents|*TU; Metals|PK/*PO
MeSH Heading
Animal; Dimercaprol|ME/TU; Edetic Acid|ME/TU; Human; Succimer|ME/TU;
Support, U.S. Gov't, P.H.S.; Unithiol|ME/TU
Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0300-483X
Country of Publication
IRELAND
Record 24 from database: MEDLINE
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Title
A structural role for metal ions in the "wild-type" conformation of the
tumor suppressor protein p53.
Author
Hainaut P; Milner J
Address
Department of Biology, University of York, Heslington, United Kingdom.
Source
Cancer Res, 1993 Apr, 53:8, 1739-42
Abstract
In human tumors, many different point mutations of the p53 gene knock out
suppressor function and induce the p53 polypeptide to adopt an
immunologically distinct, "mutant" conformation. Here we show that
exposure to the metal chelator 1,10-phenanthroline induces wild-type p53
to adopt the mutant conformation and that this process is reversible.
Conversion to mutant phenotype also occurs after exposure to (a) an
organic mercurial reagent targeting cysteinyl residues and (b) low
concentrations of mercury or cadmium. We propose that binding of metal
ions, most probably zinc, to conserved cysteinyl residues stabilizes the
tertiary structure of wild-type p53.
Language of Publication
English
Unique Identifier
93223179
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MeSH Heading (Major)
Metals|*PD; Protein p53|*CH
MeSH Heading
Amino Acid Sequence; Animal; Cysteine|CH; Edetic Acid|PD; Egtazic
Acid|PD; Human; Mice; Molecular Sequence Data; Protein Conformation|DE;
Rabbits; Support, Non-U.S. Gov't; Zinc|ME/PD
Publication Type
JOURNAL ARTICLE
ISSN
0008-5472
Country of Publication
UNITED STATES
Record 25 from database: MEDLINE
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Title
A structural role for metal ions in the "wild-type" conformation of the
tumor suppressor protein p53.
Author
Hainaut P; Milner J
Address
Department of Biology, University of York, Heslington, United Kingdom.
Source
Cancer Res, 1993 Apr, 53:8, 1739-42
Abstract
In human tumors, many different point mutations of the p53 gene knock out
suppressor function and induce the p53 polypeptide to adopt an
immunologically distinct, "mutant" conformation. Here we show that
exposure to the metal chelator 1,10-phenanthroline induces wild-type p53
to adopt the mutant conformation and that this process is reversible.
Conversion to mutant phenotype also occurs after exposure to (a) an
organic mercurial reagent targeting cysteinyl residues and (b) low
concentrations of mercury or cadmium. We propose that binding of metal
ions, most probably zinc, to conserved cysteinyl residues stabilizes the
tertiary structure of wild-type p53.
Language of Publication
English
Unique Identifier
93223179
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MeSH Heading (Major)
Metals|*PD; Protein p53|*CH
MeSH Heading
Amino Acid Sequence; Animal; Cysteine|CH; Edetic Acid|PD; Egtazic
Acid|PD; Human; Mice; Molecular Sequence Data; Protein Conformation|DE;
Rabbits; Support, Non-U.S. Gov't; Zinc|ME/PD
Publication Type
JOURNAL ARTICLE
ISSN
0008-5472
Country of Publication
UNITED STATES
Record 26 from database: MEDLINE
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Title
Lead poisoning with pigmentation of the oral mucosa. Review of the
literature and report of a case.
Author
ten Bruggenkate CM; Lopes Cardozo E; Maaskant P; van der Waal I
Address
Source
Oral Surg Oral Med Oral Pathol, 1975 May, 39:5, 747-53
Abstract
Some general aspects of the pathogenesis and the clinical and oral
symptoms of chronic lead intoxication are presented. Treatment procedures
are briefly discussed. The case of a patient suffering from plumbism is
described. A typical Burtonian line was present in the mouth. By electron
microprobe analysis, it was shown that this line was mainly the result of
lead and, to a minor extent, the result of mercury-, copper-, and
iron-bearing pigment in the subepithelial tissue.
Language of Publication
English
Unique Identifier
75195263
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MeSH Heading (Major)
Gingival Diseases|*CI; Lead Poisoning|*CO/DI/DT; Pigmentation
Disorders|*CI
MeSH Heading
Adult; Biopsy; Calcium|AD/TU; Edetic Acid|AD/TU; Human; Injections,
Intravenous; Male
Publication Type
JOURNAL ARTICLE
ISSN
0030-4220
Country of Publication
UNITED STATES
Record 27 from database: MEDLINE
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Title
Human erythrocyte pyrimidine nucleoside monophosphate kinase. Partial
purification and properties of two allelic gene products.
Author
Teng YS; Chen SH; Scott CR
Address
Source
J Biol Chem, 1976 Jul, 251:14, 4179-83
Abstract
Human pyrimidine nucleoside monophosphate kinase is a polymorphic enzyme
having two allelic gene products, UMPK 1 and UMPK 2, in several
populations. A procedure is described for the partial purification of
this enzyme from human red blood cells resulting in a 1500-fold
purification of the enzyme for UMPK 1 and 583-fold for UMPK 2. The
purified enzyme preparation catalyzed the phosphorylation of UMP, CMP,
and dCMP, and used ATP as the preferred phosphate donor. The heavy
metals, mercury, and copper, were found to be strong inhibitors of
pyrimidine nucleoside monophosphate kinase activity. EDTA was found to
protect the enzyme from inactivation by the heavy metals, and
2-mercaptoethanol stabilized the enzyme during purification. UMPK 1 and
UMPK 2 were found to have similar kinetic properties; however, UMPK 2 had
a slower electrophoretic mobility and greater thermolability than UMPK 1.
Language of Publication
English
Unique Identifier
76213295
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MeSH Heading (Major)
Alleles|*; Erythrocytes|*EN; Isoenzymes|*BL; Phosphotransferases|*BL/IP;
Polymorphism (Genetics)|*
MeSH Heading
Cations, Divalent; Drug Stability; Heat; Human; Kinetics;
Structure-Activity Relationship; Support, U.S. Gov't, P.H.S.
Publication Type
JOURNAL ARTICLE
ISSN
0021-9258
Country of Publication
UNITED STATES
Record 28 from database: MEDLINE
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Title
Recent advance in the therapy of metal poisonings with chelating agents.
Author
Aaseth J
Address
Source
Hum Toxicol, 1983 Apr, 2:2, 257-72
Abstract
1 A survey is given of the use of chelating agents in the treatment of
metal poisonings. 1 The complexing agents in established clinical use are
the polyaminopolycarboxylic acid EDTA (ethylenediamine tetraacetate) and
the thiols BAL (2, 3-dimercaptopropanol) and D-penicillamine.
Desferrioxamine is useful in the treatment of iron overloading. 2 The
theoretical foundation of the metal-ligand interaction and some general
principles of value in the search for new metal antidotes are outlined. 3
Recent research has shown that 2, 3-dimercaptosuccinic acid (DMS) and 2,
3-dimercaptopropane-1-sulphonate (DMPS) are effective in mercury and
arsenic poisonings. 4 DMS and DMPS are of significantly lower toxicity
than BAL, and they can be administered orally or intravenously. 5 A
particularly low toxicity of DMS is reported from clinical and
experimental studies, and this agent may be useful against several metal
poisonings including mercury, lead and gold.
Language of Publication
English
Unique Identifier
83236439
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MeSH Heading (Major)
Chelating Agents|ME/TO/*TU; Metals|*PO
MeSH Heading
Animal; Brain|ME; Chemistry; Drug Stability; Human; Kinetics; Support,
Non-U.S. Gov't
Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0144-5952
Country of Publication
ENGLAND
Record 29 from database: MEDLINE
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Title
Prevention by chelating agents of metal-induced developmental toxicity.
Author
Domingo JL
Address
Laboratory of Toxicology and Biochemistry, School of Medicine, Rovira i
Virgili University, Reus, Spain.
Source
Reprod Toxicol, 1995 Mar, 9:2, 105-13
Abstract
Chelating agents such as calcium disodium ethylenediaminetetraacetate
(EDTA), 2,3-dimercaptopropanol (BAL), or D-penicillamine (D-PA) have been
widely used for the past 4 decades as antidotes for the treatment of
acute and chronic metal poisoning. In recent years,
meso-2,3-dimercaptosuccinic acid (DMSA), sodium
2,3-dimercapto-1-propanesulfonate (DMPS) and sodium
4,5-dihydroxybenzene-1,3-disulfonate (Tiron) have also shown to be
effective to prevent against toxicity induced by a number of heavy
metals. The purpose of the present article was to review the protective
activity of various chelating agents against the embryotoxic and
teratogenic effects of well-known developmental toxicants (arsenic,
cadmium, lead, mercury, uranium, and vanadium). DMSA and DMPS were found
to be effective in alleviating arsenate- and arsenite-induced
teratogenesis, whereas BAL afforded only some protection against
arsenic-induced embryo/fetal toxicity. Also, DMSA, DMPS, and Tiopronin
were effective in ameliorating methyl mercury-induced developmental
toxicity. Although the embryotoxic and teratogenic effects of vanadate
were significantly reduced by Tiron, no significant amelioration of
uranium-induced embryotoxicity was observed after treatment with this
chelator.
Language of Publication
English
Unique Identifier
95315648
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MeSH Heading (Major)
Abnormalities, Drug-Induced|*PC; Chelating Agents|*TU; Fetal
Development|*DE; Metals|*PO/TO
MeSH Heading
Animal; Female; Human; Pregnancy
Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0890-6238
Country of Publication
UNITED STATES
Record 30 from database: MEDLINE
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Title
Determination of intracellular levels of 6-mercaptopurine metabolites in
erythrocytes utilizing capillary electrophoresis with laser-induced
fluorescence detection.
Author
Rabel SR; Stobaugh JF; Trueworthy R
Address
Department of Pharmaceutical Chemistry, University of Kansas, Lawrence
66045.
Source
Anal Biochem, 1995 Jan, 224:1, 315-22
Abstract
Capillary electrophoresis proved to be a useful technique for the
analysis of intracellular levels of 6-thioguanosine mono-, di-, and
triphosphate with analysis times of 20 min. Conditions required for
baseline separation of the thioguanine nucleotides consisted of a 25 mM
KH2PO4 (pH 8.0) buffer and a separation voltage of +28 kV. Laser-induced
fluorescence detection (lambda ex = 325 nm, lambda em = 410 nm) of the
thioguanine nucleotide metabolites of 6-mercaptopurine (6-MP) was
possible following oxidation of the thiol functionality. Tedious
extraction procedures involving mercury cellulose resins or phenyl
mercury adduct formation, which had been required previously for the
selective extraction of thiopurines from erythrocytes, were unnecessary
due to the overall specificity of the approach. However, the inclusion of
50 mM EDTA in the sample preparation was required to inhibit the
anabolic/catabolic enzymatic activity, which was responsible for the
degradation of the analytes. The method demonstrated linearity from 5 to
1700 pmol/100 microliters red blood cells for the three analytes (RSDs <
or = 8%). The feasibility of the method was demonstrated for the
quantitation of 6-thioguanine nucleotides in patients receiving either
oral or intravenous 6-MP therapy.
Language of Publication
English
Unique Identifier
95225456
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MeSH Heading (Major)
Erythrocytes|*CH; Guanine Nucleotides|*BL; Guanosine Diphosphate|*AA/BL;
Guanosine Triphosphate|*AA/BL; Thionucleotides|*BL; 6-Mercaptopurine|*ME
MeSH Heading
Electrophoresis; Fluorescence; Human; Support, Non-U.S. Gov't; Support,
U.S. Gov't, P.H.S.
Publication Type
JOURNAL ARTICLE
ISSN
0003-2697
Country of Publication
UNITED STATES
Record 31 from database: MEDLINE
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Title
Metal-binding characteristics of the parotid salivary protein gustin.
Author
Shatzman AR; Henkin RI
Address
Source
Biochim Biophys Acta, 1980 May, 623:1, 107-18
Abstract
Metal binding characteristics of the parotid salivary protein gustin have
been examined. When purified to apparent homogeneity, gustin contains 1
gatom Zn/mol which is tightly bound (Kd at pH 7.2, 4.5--10(-11) M). This
tightly bound zinc can be removed with strong chelators such as
diethyldithiocarbamic acid and 1,10-o-phenanthroline at pH 4.5, but not
with EDTA or Chelex 100. Removal of the metal ion causes no appreciable
conformational change in the protein. The apoprotein can be reconstituted
by dialysis against Zn2+-containing buffer, a process favored by pH
greater than 6.0. Only cobalt is able to bind to the apoprotein at this
strong binding site. Cobalt binding is appreciably weaker than that of
zinc (Kd at pH 7.2, 1.3--10(-7) M) and is maximal at pH 7.0. The weaker
binding of cobalt is also illustrated by the loss of 37% of bound cobalt
after 96 h of dialysis at pH 7.2, conditions under which the zinc content
of gustin does not change. A second gatom Zn/mol may be loosely bound to
gustin, but is easily removed by dialysis against metal ion-free buffer.
Other metal ions such as copper, nickel, iron or manganese, but not
cadmium or mercury, bind loosely to this second zinc site and are removed
with ease. Zinc appears to be involved in the formation of the complex
between gustin and glycoproteins which are present in human parotid
saliva in vivo.
Language of Publication
English
Unique Identifier
80198516
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MeSH Heading (Major)
Parotid Gland|*ME; Salivary Proteins|*ME; Zinc|*ME
MeSH Heading
Ageusia|PP; Apoproteins|ME; Chromatography, Gel; Circular Dichroism;
Cobalt|ME; Glycoproteins|ME; Human; Support, U.S. Gov't, P.H.S.
Publication Type
JOURNAL ARTICLE
ISSN
0006-3002
Country of Publication
NETHERLANDS
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