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PMID: 3279957 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Biochemical and biophysical research communications ·Vol. 151 ·No. 2 ·1988-03-15 ·Pages 883-90

Gregory H, Young J, Schröder JM, Mrowietz U, Christophers E

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.

MeSH Terms
Amino Acid Sequence Chemotactic Factors/isolation & purification,metabolism Chymotrypsin Concanavalin A Humans Interleukin-8 Lymphocyte Activation Lymphocytes/immunology Molecular Sequence Data Neutrophils/physiology Peptide Fragments/analysis Phytohemagglutinins Trypsin
Chemicals
Chemotactic Factors Interleukin-8 Peptide Fragments Phytohemagglutinins Concanavalin A Chymotrypsin Trypsin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Gregory H
ICI, Pharmaceuticals Division, Macclesfield Cheshire, Great Britain.
Young J
Schröder J M
Mrowietz U
Christophers E
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1988-03-15
Pages
883-90
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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