Structure determination of a human lymphocyte derived neutrophil activating peptide (LYNAP).
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.
Gregory
H
H
ICI, Pharmaceuticals Division, Macclesfield Cheshire, Great Britain.
Young
J
J
Schröder
J M
JM
Mrowietz
U
U
Christophers
E
E
D000595:Amino Acid Sequence; D002630:Chemotactic Factors / Q000302:isolation & purification* / Q000378:metabolism; D002918:Chymotrypsin; D003208:Concanavalin A; D006801:Humans; D016209:Interleukin-8; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000276:immunology*; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000502:physiology*; D010446:Peptide Fragments / Q000032:analysis; D010835:Phytohemagglutinins; D014357:Trypsin
D002630:Chemotactic Factors; D016209:Interleukin-8; D010446:Peptide Fragments; D010835:Phytohemagglutinins; D003208:Concanavalin A; D002918:Chymotrypsin; D014357:Trypsin