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[Proteolytic processing by dipeptidyl aminopeptidase IV generates receptor selectivity for peptide YY (PYY)]
D Grandt1, P Dahms, M Schimiczek
1Medizinische Klinik und Poliklinik, Abteilung für Gastroenterologie, Klinikum der Universität, Essen.
Medizinische Klinik (Munich, Germany : 1983)
|March 15, 1993
Summary
Dipeptidyl peptidase IV (DPP IV) enzyme cleaves PYY 1-36 into PYY 3-36, a selective Y2 receptor agonist. This processing regulates PYY
Area of Science:
- Biochemistry
- Endocrinology
- Pharmacology
Context:
- Peptide YY (PYY) exerts biological activity through Y1 and Y2 receptor subtypes.
- PYY 1-36 is an unselective agonist, binding to both Y1 and Y2 receptors.
- PYY 3-36 selectively binds to Y2 receptors, indicating a transformation in receptor affinity.
Purpose:
- To identify the enzyme responsible for processing PYY 1-36 into PYY 3-36.
- To investigate the role of specific exopeptidases in PYY metabolism.
- To understand the mechanism regulating Y1/Y2 receptor stimulation by PYY.
Summary:
- Dipeptidyl cleavage transforms PYY 1-36 into PYY 3-36, a selective Y2 receptor agonist.
- The proline residue in PYY 1-36 protects it from most exopeptidases.
- Dipeptidyl aminopeptidase IV (DPP IV) efficiently cleaved Tyr-Pro from PYY 1-36, generating PYY 3-36.
- DPP IV's presence on endothelial and brush border membranes suggests its in vivo role in PYY processing.
Impact:
- DPP IV is identified as a candidate enzyme for generating PYY 3-36 in vivo.
- This enzymatic processing regulates the ratio of Y1/Y2 receptor stimulation by PYY.
- Findings contribute to understanding PYY signaling and potential therapeutic modulation.