Identification of dipeptidyl peptidase 3 as the Angiotensin-(1–7) degrading peptidase in human HK-2 renal epithelial cells-Reference-Cited by-同舟云学术

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Identification of dipeptidyl peptidase 3 as the Angiotensin-(1–7) degrading peptidase in human HK-2 renal epithelial cells

Published:2016-09 Issue: Volume:83 Page:29-37
ISSN:0196-9781
Container-title:Peptides
language:en
Short-container-title:Peptides

Author:

Cruz-Diaz Nildris,Wilson Bryan A.,Pirro Nancy T.,Brosnihan K. Bridget,Marshall Allyson C.,Chappell Mark C.

Funder

PRIME Institutional Research and Academic Career Development Award

American Heart Association (AHA)

NIH

AHA

Groskert Heart

Wake Forest Venture

Farley-Hudson Foundation (Jacksonville, NC)

Publisher

Elsevier BV

Subject

Cellular and Molecular Neuroscience,Endocrinology,Physiology,Biochemistry

Reference28 articles.

1. Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences;Abramic;Biol. Chem.,2000

2. Highly reactive cysteine residues are part of the substrate binding site of mammalian dipeptidyl peptidases III;Abramic;Int. J. Biochem. Cell Biol.,2004

3. Angiotensin-(1–7) abolishes AGE-induced cellular hypertrophy and myofibroblast transformation via inhibition of ERK 1/2;Alzayadneh;Cell. Signalling,2014

4. Emerging evidence for a functional angiotensin-converting enzyme 2-angiotensin-(1–7) mas receptor axis; more than regulation of blood pressure?;Chappell;Hypertension,2007

5. Nonclassical renin-angiotensin system and renal function;Chappell;Compr. Physiol.,2012

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