Characterization of hadrucalcin, a peptide from Hadrurus gertschi scorpion venom with pharmacological activity on ryanodine receptors.

ABSTRACT:

Background and purpose

Members of the calcin family, presently including imperatoxin A, maurocalcin, opicalcins and hemicalcin, are basic, 33-mer peptide activators of ryanodine receptors (RyRs), the calcium channels of the sarcoplasmic reticulum (SR) that provide the majority of calcium for muscle contraction. Here we describe hadrucalcin, a novel member of this family.

Experimental approach

Hadrucalcin was isolated from the venom of Hadrurus gertschi. Amino acid sequence and mass were determined by Edman degradation and mass spectrometry respectively. A cDNA library was constructed to generate clones for DNA sequence determination. Biological activity of native toxin was confirmed with [(3)H]ryanodine binding, by using SR vesicles from cardiac and skeletal muscle, and with

SUBMITTER: Schwartz EF 

PROVIDER: S-EPMC2707986 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature