Glutamate carboxypeptidase II does not process amyloid-beta peptide

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10189921" target="_blank" >RIV/00216208:11310/13:10189921 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/13:00424007

Výsledek na webu

<a href="http://dx.doi.org/10.1096/fj.12-225094" target="_blank" >http://dx.doi.org/10.1096/fj.12-225094</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1096/fj.12-225094" target="_blank" >10.1096/fj.12-225094</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Glutamate carboxypeptidase II does not process amyloid-beta peptide

Popis výsledku v původním jazyce

The accumulation of amyloid- (A) peptide is thought to be a major causative mechanism of Alzheimer's disease. A accumulation could be caused by dysregulated processing of amyloid precursor protein, yielding excessive amounts of A, and/or by inefficient proteolytic degradation of the peptide itself. Several proteases have been described as A degradation enzymes, most notably metalloendopeptidases, aspartic endopeptidases, and some exopeptidases. Recently a report suggested that another metallopeptidase,glutamate carboxypeptidase II (GCPII), can also cleave A. GCPII is a zinc exopeptidase that cleaves glutamate from N-acetyl-l-aspartyl-l-glutamate in the central nervous system and from pteroylpoly--glutamate in the jejunum. GCPII has been proposed as apromising therapeutic target for disorders caused by glutamate neurotoxicity. However, an A-degrading activity of GCPII would compromise potential pharmaceutical use of GCPII inhibitors, because the enzyme inhibition might lead to increas

Název v anglickém jazyce

Glutamate carboxypeptidase II does not process amyloid-beta peptide

Popis výsledku anglicky

The accumulation of amyloid- (A) peptide is thought to be a major causative mechanism of Alzheimer's disease. A accumulation could be caused by dysregulated processing of amyloid precursor protein, yielding excessive amounts of A, and/or by inefficient proteolytic degradation of the peptide itself. Several proteases have been described as A degradation enzymes, most notably metalloendopeptidases, aspartic endopeptidases, and some exopeptidases. Recently a report suggested that another metallopeptidase,glutamate carboxypeptidase II (GCPII), can also cleave A. GCPII is a zinc exopeptidase that cleaves glutamate from N-acetyl-l-aspartyl-l-glutamate in the central nervous system and from pteroylpoly--glutamate in the jejunum. GCPII has been proposed as apromising therapeutic target for disorders caused by glutamate neurotoxicity. However, an A-degrading activity of GCPII would compromise potential pharmaceutical use of GCPII inhibitors, because the enzyme inhibition might lead to increas

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP304%2F12%2F0847" target="_blank" >GAP304/12/0847: Glutamátkarboxypeptidasa II a její role v růstu nádorů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

FASEB Journal

ISSN

0892-6638

e-ISSN

—

Svazek periodika

27

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

2626-2632

Kód UT WoS článku

000328841000012

EID výsledku v databázi Scopus

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