Peptidyl‐prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease. (February 2015)

• Record Type: Journal Article
• Authors: Rostam, Muhamad A; Piva, Terrence J; Rezaei, Hossein B; Kamato, Danielle; Little, Peter J; Zheng, Wenhua; Osman, Narin
• Is Part Of: Clinical and experimental pharmacology and physiology. Volume 42:Number 2(2015:Feb.)
• Page Start: 117
• Page End: 124
• Publication Date: 2015-02
• Subjects: Clinical pharmacology -- Periodicals; Pharmacology, Experimental -- Periodicals; Physiology, Experimental -- Periodicals; Physiology, Pathological -- Periodicals; 615.1
• DOI: 10.1111/1440-1681.12335
• Languages: English
• ISSNs: 0305-1870

Abstract

<abstract abstract-type="main" id="cep12335-abs-0001"> <title>Summary</title> <p>Peptidyl‐prolyl <italic>cis</italic>/<italic>trans</italic> isomerases (PPIases) are a conserved group of enzymes that catalyse the conversion between <italic>cis</italic> and <italic>trans</italic> conformations of proline imidic peptide bonds. These enzymes play critical roles in regulatory mechanisms of cellular function and pathophysiology of disease. There are three different classes of PPIases and increasing interest in the development of specific PPIase inhibitors. Cyclosporine A, FK506, rapamycin and juglone are known PPIase inhibitors. Herein, we review recent advances in elucidating the role and regulation of the PPIase family in vascular disease. We focus on peptidyl‐prolyl <italic>cis</italic>/<italic>trans</italic> isomerase NIMA‐interacting 1 (Pin1), an important member of the PPIase family that plays a role in cell cycle progression, gene expression, cell signalling and cell proliferation. In addition, Pin1 may be involved in atherosclerosis. The unique role of Pin1 as a molecular switch that impacts on multiple downstream pathways necessitates the evaluation of a highly specific Pin1 inhibitor to aid in potential therapeutic drug discovery.</p> </abstract>