Mercury contamination of rat amylin mimics vasoactivity and cytotoxic effects.

Rat amylin differs from human amylin (hIAPP) in that it lacks a fibril-forming capacity. As a consequence, toxic effects have been reported for human but not for rat amylin. This report demonstrates how a mercury contamination of commercial rat amylin imitates peptide-related vasoactive and cytotoxic effects on preparations of isolated blood vessels. The source of mercury contamination was believed related to the peptide synthesis. Thiol groups of cysteine-containing peptides are often protected by acetamidomethyl (Acm) which is cleaved by mercuric acetate.

Nitric oxide-dependent vasorelaxation and endothelial cell damage caused by mercury chloride.

Mercury and its derivatives are known to constrict vascular smooth muscle cells. However, little is known about the role of endothelial cells in mercury-induced vasoreactivity. Using isolated, norepinephrine preconstricted rat aorta and pulmonary artery rings with intact endothelium, we demonstrate that mercury chloride (HgCl2) induces an endothelial-dependent vasorelaxation which was totally blocked by the nitric oxide inhibitor L-NAME. Besides this vasorelaxant effect, treatment with HgCl2 resulted in functional and morphological alterations of the endothelial cells. On aortic rings, endothelial cells were partly lifted from the basal membrane when incubated for 20 min in HgCl2 (10(-7) M)-containing buffer. At a concentration of 10(-6) M, the endothelial cells were completely denuded and acetylcholine vasorelaxation was abolished. Endothelial cell structure and function was preserved by incubating the vessels in HgCl2-containing rat blood instead of buffer. We conclude that HgCl2 induces an endothelial-dependent vasorelaxation and alters structure and function of vascular endothelial cells.