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[Proteolytic processing by dipeptidyl aminopeptidase IV generates receptor selectivity for peptide YY (PYY)]. 1993

D Grandt, and P Dahms, and M Schimiczek, and V E Eysselein, and J R Reeve, and R Mentlein
Medizinische Klinik und Poliklinik, Abteilung für Gastroenterologie, Klinikum der Universität, Essen.

Two receptor subtypes, Y1 and Y2, are known to mediate PYY biological activity. PYY 1-36 binds to Y1 and Y2 receptors with equal affinity, whereas the second endogenous form of PYY, PYY 3-36, selectively binds to Y2 receptors. Dipeptidyl cleavage thus transforms an unselective Y agonist into a highly selective Y2 agonist, PYY 3-36. The enzyme responsible for this processing is unknown. Since PYY has a proline in the penultimate position it is protected from the attack of most unspecific exopeptidases. Only a few exopeptidases are theoretically capable of generating PYY 3-36 from PYY 1-36. Of the enzymes tested only the dipeptidyl aminopeptidase IV (DPP IV, E.C. 3.4.14.5) cleaved Tyr-Pro from PYY 1-36 with high activity. Since DPP IV is found on the endothelial surface and brush border membranes it can be considered a candidate enzyme for generating PYY 3-36 in vivo, thereby regulating the ratio of Y1/Y2 receptor stimulation by PYY.

UI MeSH Term Description Entries
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D004152 Dipeptidyl-Peptidases and Tripeptidyl-Peptidases A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain. Dipeptidyl Peptidase,Dipeptidyl Peptidases,Dipeptidylpeptide Hydrolase,Tripeptidyl-Peptidase,Dipeptidylpeptide Hydrolases,Tripeptidyl-Peptidases,Dipeptidyl Peptidases and Tripeptidyl Peptidases,Hydrolase, Dipeptidylpeptide,Peptidase, Dipeptidyl,Tripeptidyl Peptidase,Tripeptidyl Peptidases,Tripeptidyl-Peptidases and Dipeptidyl-Peptidases
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D017476 Receptors, Neuropeptide Y Cell surface proteins that bind neuropeptide Y with high affinity and trigger intracellular changes which influence the behavior of cells. Neuropeptide Y Receptors,Neuropeptide Y Receptor,Receptor, Neuropeptide Y
D018819 Dipeptidyl Peptidase 4 A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation. Antigens, CD26,CD26 Antigens,Dipeptidyl-Peptidase IV,Adenosine Deaminase Complexing Protein 2,CD26 Antigen,Antigen, CD26,Dipeptidyl Peptidase IV
D019894 Peptide YY A 36-amino acid peptide produced by the L cells of the distal small intestine and colon. Peptide YY inhibits gastric and pancreatic secretion. PYY Peptide,Peptide, PYY

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