Neutrophil chemotactic activity of N-terminal peptides from the calpain small subunit

Biochem Biophys Res Commun. 1990 Jun 29;169(3):1242-7. doi: 10.1016/0006-291x(90)92030-4.

Abstract

On the basis of previous findings that N-acetyl nonapeptide from the human calpain I large subunit has chemotactic activity for neutrophils, a series of peptides with the N-terminal sequence of the calpain small subunit were synthesized and their chemotactic activity was examined. Potent activity was found in N-acetyl tetra, hepta, octa, nona and a larger peptide of 13 residues, although N-acetyl tripeptide showed only weak activity and N-acetyl penta and hexa peptides showed almost no activity. Since the small subunit is identical in calpains I and II, the results indicate that both calpains could be precursor proteins of chemotactic factors for neutrophils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Calpain*
  • Chemotactic Factors*
  • Chemotaxis, Leukocyte*
  • Dose-Response Relationship, Drug
  • Humans
  • Molecular Sequence Data
  • Neutrophils / physiology*
  • Peptide Fragments / chemical synthesis

Substances

  • Chemotactic Factors
  • Peptide Fragments
  • Calpain