Degradation of ACTH/MSH(4-10) and its synthetic analog semax by rat serum enzymes: an inhibitor study.
Degradation of the behaviorally active peptide ACTH/MSH(4-10) and its synthetic analog semax was studied in serum in the presence of several specific peptidase inhibitors. Bestatin and puromycin were used to inhibit aminopeptidase activity, lisinopril for angiotensin-converting enzyme, phosphoramidon for neutral endopeptidase 24.11, and Z-Pro-prolinal for prolyl endopeptidase. Bestatin inhibited up to 66%, puromycin about 33%, and lisinopril about 15% of total degrading activity against both ACTH/MSH(4-10) and semax. Involvement of neutral endopeptidase and prolyl endopeptidase in hydrolysis of the two peptides was less definitive. These studies showed that aminopeptidases and angiotensin-converting enzyme are responsible for the major part of the hydrolysis of ACTH/MSH(4-10) and semax in rat serum.
Laboratory of Regulatory Peptides, Institute of Molecular Genetics, Russian Academy of Sciences, Moscow.
V N
VN
Potaman
L Y
LY
Alfeeva
A A
AA
Kamensky
V N
VN
Nezavibatko
D000324:Adrenocorticotropic Hormone / Q000031:analogs & derivatives* / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D010450:Endopeptidases / Q000097:blood*; D009074:Melanocyte-Stimulating Hormones / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology*; D051381:Rats; D017208:Rats, Wistar
D010446:Peptide Fragments; D011480:Protease Inhibitors; C048487:ACTH (4-7), Pro-Gly-Pro-; D000324:Adrenocorticotropic Hormone; D009074:Melanocyte-Stimulating Hormones; D010450:Endopeptidases; C011394:ACTH (4-10)