Potential Role of Dipeptidyl Peptidase IV in the Pathophysiology of Heart Failure

International Journal of Molecular Sciences

Thiago A. Salles²  Leonardo dos Santos¹  Valério G. Barauna¹  Adriana C. C. Girardi² 

[1] Department of Physiological Sciences, Federal University of Espírito Santo, Vitoria 29043-900, ES, Brazil; E-Mails:;Laboratory of Genetics and Molecular Cardiology, Heart Institute (InCor), University of São Paulo Medical School, São Paulo 05403-000, SP, Brazil; E-Mail:

关键词: glucagon-like peptide-1;    brain natriuretic peptide;    stromal cell-derived factor-1;    renal function;    cardiac dysfunction;    natriuresis;    cardioprotection;    renoprotection;   

DOI  :  10.3390/ijms16024226

来源: mdpi

【 摘 要 】

Dipeptidyl peptidase IV (DPPIV) is a widely expressed multifunctional serine peptidase that exists as a membrane-anchored cell surface protein or in a soluble form in the plasma and other body fluids. Numerous substrates are cleaved at the penultimate amino acid by DPPIV, including glucagon-like peptide-1 (GLP-1), brain natriuretic peptide (BNP) and stromal cell-derived factor-1 (SDF-α), all of which play important roles in the cardiovascular system. In this regard, recent reports have documented that circulating DPPIV activity correlates with poorer cardiovascular outcomes in human and experimental heart failure (HF). Moreover, emerging evidence indicates that DPPIV inhibitors exert cardioprotective and renoprotective actions in a variety of experimental models of cardiac dysfunction. On the other hand, conflicting results have been found when translating these promising findings from preclinical animal models to clinical therapy. In this review, we discuss how DPPIV might be involved in the cardio-renal axis in HF. In addition, the potential role for DPPIV inhibitors in ameliorating heart disease is revised, focusing on the effects of the main DPPIV substrates on cardiac remodeling and renal handling of salt and water.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.