Mercury contamination of rat amylin mimics vasoactivity and cytotoxic effects

Peptides. 2003 Aug;24(8):1157-62. doi: 10.1016/j.peptides.2003.07.010.

Abstract

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.

MeSH terms

  • Acetylcholine / metabolism
  • Amyloid / metabolism
  • Amyloid / pharmacology*
  • Amyloid / toxicity
  • Animals
  • Anti-Ulcer Agents / metabolism
  • Anti-Ulcer Agents / pharmacology*
  • Anti-Ulcer Agents / toxicity
  • Californium / metabolism
  • Humans
  • Islet Amyloid Polypeptide
  • Male
  • Mass Spectrometry
  • Mercury / metabolism*
  • Mercury / toxicity
  • Pulmonary Artery / drug effects*
  • Rats

Substances

  • Amyloid
  • Anti-Ulcer Agents
  • Islet Amyloid Polypeptide
  • Californium
  • Mercury
  • Acetylcholine