TAILIEUCHUNG - Báo cáo khoa học: Characterization of membrane-bound prolyl endopeptidase from brain

Prolyl oligopeptidase (POP) is a serine protease that cleaves small peptides at the carboxyl side of an internal proline residue. Substance P, arginine– vasopressin, thyroliberin and gonadoliberin are proposed physiological substrates of this protease. POP has been implicated in a variety of brain processes, including learning, memory, and mood regulation, as well as in pathologies such as neurodegeneration, hypertension, and psychiatric disor-ders. | ỊFEBS Journal Characterization of membrane-bound prolyl endopeptidase from brain Jofre Tenorio-Laranga1 Jarkko I. Venalainen2 Pekka T. Mannisto3 and J. A. Garcia-Horsman1 3 1 Centro de Investigacion Príncipe Felipe Valencia Spain 2 Department of Pharmacology and Toxicology University of Kuopio Finland 3 Division of Pharmacology and Toxicology University of Helsinki Finland Keywords neuropeptides neurotransmission peptide metabolism prolyl endopeptidase prolyl oligopeptidase Correspondence J. A. Garcia-Horsman Division of Pharmacology and Toxicology University of Helsinki Viikinkaari 5E 00014 Helsinki Finland Fax 358 9 191 59471 Tel 358 9 191 59459 E-mail Received 7 March 2008 revised 3 July 2008 accepted 4 July 2008 doi Prolyl oligopeptidase POP is a serine protease that cleaves small peptides at the carboxyl side of an internal proline residue. Substance P argininevasopressin thyroliberin and gonadoliberin are proposed physiological substrates of this protease. POP has been implicated in a variety of brain processes including learning memory and mood regulation as well as in pathologies such as neurodegeneration hypertension and psychiatric disorders. Although POP has been considered to be a soluble cytoplasmic peptidase significant levels of activity have been detected in membranes and in extracellular fluids such as serum cerebrospinal fluid seminal fluid and urine suggesting the existence of noncytoplasmic forms. Furthermore a closely associated membrane prolyl endopeptidase PE activity has been previously detected in synaptosomes and shown to be different from the cytoplasmic POP activity. Here we isolated purified and characterized this membrane-bound PE herein referred to as mPOP. Although when attached to membranes mPOP presents certain features that distinguish it from the classical POP our results indicate that this protein has the same amino acid sequence as POP except for the possible addition .

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