Literature DB >> 1361094

Proline-specific aminopeptidases: potential role in bradykinin degradation.

G Vanhoof1, I de Meester, D Hendriks, F Goossens, M van Sande, S Scharpé, A Yaron.   

Abstract

The N-terminus of bradykinin is shown to be sequentially degraded by the human proline-specific aminopeptidases aminopeptidase P (EC 3.4.11.9) and dipeptidyl peptidase IV (EC 3.4.14.5). Additional evidence is provided for the hypothesis that these proline-specific aminopeptidases play an essential role in the degradation of peptides containing an N-terminal Xaa-Pro sequence.

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Year:  1992        PMID: 1361094

Source DB:  PubMed          Journal:  Agents Actions Suppl        ISSN: 0379-0363


  3 in total

1.  Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans.

Authors:  A Beauvais; M Monod; J Wyniger; J P Debeaupuis; E Grouzmann; N Brakch; J Svab; A G Hovanessian; J P Latgé
Journal:  Infect Immun       Date:  1997-08       Impact factor: 3.441

2.  Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site.

Authors:  Shalini Iyer; Penelope J La-Borde; Karl A P Payne; Mark R Parsons; Anthony J Turner; R Elwyn Isaac; K Ravi Acharya
Journal:  FEBS Open Bio       Date:  2015-04-02       Impact factor: 2.693

3.  Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease.

Authors:  Vanessa Drendel; Bianca Heckelmann; Chia-Yi Chen; Juliane Weisser; Guadalupe Espadas; Christoph Schell; Eduard Sabido; Martin Werner; Cordula A Jilg; Oliver Schilling
Journal:  Oncotarget       Date:  2017-10-19
  3 in total

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