Title : Neutral endopeptidase activity in the interaction of N-formyl-L-methionyl-L-leucyl-L-phenylalanine with human polymorphonuclear leukocytes.

Pub. Date : 1991 Oct 15

PMID : 1935939






3 Functional Relationships(s)
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1 By using inhibitors of distinct classes of endoproteases, this particular fMet-Leu-Phe degradation was attributed exclusively to an exoplasmic metalloendoprotease that matches the ubiquitous neutral endopeptidase (NEP). Leucine membrane metalloendopeptidase Homo sapiens
2 By using inhibitors of distinct classes of endoproteases, this particular fMet-Leu-Phe degradation was attributed exclusively to an exoplasmic metalloendoprotease that matches the ubiquitous neutral endopeptidase (NEP). Leucine membrane metalloendopeptidase Homo sapiens
3 Based on these and previously reported results, a novel model is proposed in which the fMet-Leu-Phe-induced inflammatory stimulation of PMN involves both NEP and the fMet-Leu-Phe receptor. Leucine membrane metalloendopeptidase Homo sapiens