Greenberg Oral Chelation Study-page 18

*Links to Toxic Metal Information
ATSDR (Agency for Toxic Substances and Disease Registry) www.atsdr.cdc.gov Cellphysics.org non-profit, therapy education & research www.cellphysics.org

References
11. www.dmps.cc
12. www.DMPSbackfire.com
13. Frumkin, H. et al, Environ Health Perspect. 2001 Feb.109 (2): 167-71
14. Duhr EF, et al HgEDTA Complex Inhibits GTP Interactions with the E-site of Brain beta-Tubulin. Toxicol Appl Pharmacol 122(2):273-280 (1993)
15. Huggins, H.A DDS and Levy, T.E. MD Uninformed Consent Hampton Roads Publishing Co. Inc .Charlottesville, VA 1999

Duhr EF, Pendergrass JC, Slevin JT & Haley BE, HgEDTA complex inhibits GTP interactions with the E-site of brain betatubulin. Toxicol Appl Pharmacol 122(2):273-280 (1993)

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."

AMALGAM: http://www. listserv.gmd.de/archives/amalgam.html

For More Information:
Alan Greenberg MD, can be contacted at: Science Formulas Inc.
Attn: Dr Alan Greenberg
6800 Fort Smallwood Rd. Baltimore, MD 21226 Phone: 410-636-0730 x223 Fax 410-636-0819 Email: dralan@jetblast.net