Preferential cleavage of amino- and carboxyl-terminal oligopeptides from vasoactive intestinal polypeptide by human recombinant enkephalinase (neutral endopeptidase, EC 3.4.24.11).
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.
Goetzl
E J
EJ
Howard Hughes Medical Institute, San Francisco, CA 94143-0724.
Sreedharan
S P
SP
Turck
C W
CW
Bridenbaugh
R
R
Malfroy
B
B
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*
D006020:Glycopeptides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D014660:Vasoactive Intestinal Peptide; D015260:Neprilysin; C008890:phosphoramidon