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Characterization of Membrane-Bound Neuropeptide-Degrading Activities in Aplysia Californica

Characterization of Membrane-Bound Neuropeptide-Degrading Activities in Aplysia Californica CHARACTERIZATION OF MEMBRANE-BOUND NEUROPEP- TIDE-DEGRADING ACTIVITIES IN APLYSIA CALIFORNICA by LUC DESGROSEILLERS, WAFA BAWAB, RAQUEL S. ALOYZ and PHILIPPE CRINE (Department of Biochemistry, University of Montreal, P. O. Box 6128, Station Centre Ville, Mon- treal, Canada, H3C3J7) SUMMARY We are investigating the role of membrane-bound peptidases in the inactivation of neuropeptides in Aplysia. We found neuropeptide-degrading enzymes in all tested tissues of Aplysia. This activity was very sensitive to amastatin, suggesting that the major enzyme was an aminopeptidase. Accordingly, this enzyme hydrolysed [3H]leu- enkephalin at the tyr1-gly2 bond and FMRFamide at the Phc1-Met2 bond as determined by HPLC analysis of cleavage products. Enzymatic studies in the absence or presence of aminopeptidase inhibitors revealed that this enzyme is a metallopeptidase with the same enzymatic characteristics as the mammalian aminopeptidase N. However, the enzyme from Aplysia was able to hydrolyse substrates known to be resistant to mammalian aminopeptidases due to the presence of a D-amino acid. Inhibition of this aminopep- tidase with amastatin allowed us to characterize a second enkephalin-degrading enzyme in the kidney plasma membranes. This enzyme cleaved leu-enkephalin at the Gly3-Phe4 bond and its activity is sensitive to neutral endopeptidase inhibitors. After separation of kidney membrane proteins by http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Netherlands Journal of Zoology (in 2003 continued as Animal Biology) Brill

Characterization of Membrane-Bound Neuropeptide-Degrading Activities in Aplysia Californica

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Publisher
Brill
Copyright
© 1993 Koninklijke Brill NV, Leiden, The Netherlands
ISSN
0028-2960
eISSN
1568-542X
DOI
10.1163/156854293X00539
Publisher site
See Article on Publisher Site

Abstract

CHARACTERIZATION OF MEMBRANE-BOUND NEUROPEP- TIDE-DEGRADING ACTIVITIES IN APLYSIA CALIFORNICA by LUC DESGROSEILLERS, WAFA BAWAB, RAQUEL S. ALOYZ and PHILIPPE CRINE (Department of Biochemistry, University of Montreal, P. O. Box 6128, Station Centre Ville, Mon- treal, Canada, H3C3J7) SUMMARY We are investigating the role of membrane-bound peptidases in the inactivation of neuropeptides in Aplysia. We found neuropeptide-degrading enzymes in all tested tissues of Aplysia. This activity was very sensitive to amastatin, suggesting that the major enzyme was an aminopeptidase. Accordingly, this enzyme hydrolysed [3H]leu- enkephalin at the tyr1-gly2 bond and FMRFamide at the Phc1-Met2 bond as determined by HPLC analysis of cleavage products. Enzymatic studies in the absence or presence of aminopeptidase inhibitors revealed that this enzyme is a metallopeptidase with the same enzymatic characteristics as the mammalian aminopeptidase N. However, the enzyme from Aplysia was able to hydrolyse substrates known to be resistant to mammalian aminopeptidases due to the presence of a D-amino acid. Inhibition of this aminopep- tidase with amastatin allowed us to characterize a second enkephalin-degrading enzyme in the kidney plasma membranes. This enzyme cleaved leu-enkephalin at the Gly3-Phe4 bond and its activity is sensitive to neutral endopeptidase inhibitors. After separation of kidney membrane proteins by

Journal

Netherlands Journal of Zoology (in 2003 continued as Animal Biology) – Brill

Published: Jan 1, 1993

Keywords: neuropeptide degradation; enzyme inhibitors; aminopeptidase; Aplysia californica; SDS-PAGE; neutral endopeptidase; RP-HPLC

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