title: Preferential cleavage of amino- and carboxyl-terminal oligopeptides from vasoactive intestinal polypeptide by human recombinant enkephalinase (neutral endopeptidase, EC 3.4.24.11).
abstract: Human recombinant enkephalinase (neutral endopeptidase, EC 3.4.24.11) cleaved synthetic vasoactive intestinal peptide (VIP1-28) with time-and peptidase concentration-dependence, which left less than 30% intact after 30 micrograms was incubated at 37 degrees C with 0.1 micrograms and 10 micrograms of peptidase for 120 min and 15 min, respectively. The rank order of relative rates of peptidolysis amino-terminal to hydrophobic amino acids was Ala4 and Val5 greater than Tyr22 and Ile26 much greater than Leu13 and Met17. The many effects of VIP1-28 on epithelial cell and leukocyte functions thus may be influenced by degradation of the mediator by enkephalinase at the surface of target cells.
authors.affiliation: Howard Hughes Medical Institute, San Francisco, CA 94143-0724.
authors.forename: E J
authors.initials: EJ
authors.lastname: Goetzl
authors.forename: S P
authors.initials: SP
authors.lastname: Sreedharan
authors.forename: C W
authors.initials: CW
authors.lastname: Turck
authors.forename: R
authors.initials: R
authors.lastname: Bridenbaugh
authors.forename: B
authors.initials: B
authors.lastname: Malfroy
mesh_terms: D006020:Glycopeptides / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D015260:Neprilysin / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D014660:Vasoactive Intestinal Peptide / Q000378:metabolism*
chemical_list: D006020:Glycopeptides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D014660:Vasoactive Intestinal Peptide; D015260:Neprilysin; C008890:phosphoramidon