Structure determination of a human lymphocyte derived neutrophil activating peptide (LYNAP)

Biochem Biophys Res Commun. 1988 Mar 15;151(2):883-90. doi: 10.1016/s0006-291x(88)80364-4.

Abstract

Phytohemagglutinin or Concanavalin A-stimulated human T-lymphocytes produce a factor (LYNAP) with potent chemotactic and enzyme degranulating activity in peripheral human neutrophils. Sequence analysis of LYNAP established an apparently novel 72 residue polypeptide structure. Examination of protein data bases showed that LYNAP had about 30% sequence homology with recently characterised connective tissue activating proteins produced by platelets. Furthermore, it was subsequently found that the amino acid sequence is largely the same as that predicted from a cDNA clone derived from mRNA elevated in peripheral human leukocytes stimulated by mitogens.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Chemotactic Factors / isolation & purification*
  • Chemotactic Factors / metabolism
  • Chymotrypsin
  • Concanavalin A
  • Humans
  • Interleukin-8
  • Lymphocyte Activation
  • Lymphocytes / immunology*
  • Molecular Sequence Data
  • Neutrophils / physiology*
  • Peptide Fragments / analysis
  • Phytohemagglutinins
  • Trypsin

Substances

  • Chemotactic Factors
  • Interleukin-8
  • Peptide Fragments
  • Phytohemagglutinins
  • Concanavalin A
  • Chymotrypsin
  • Trypsin