Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease

Rostam, Muhamad Ashraf and Piva, Terence J. and Rezaei, Hossein B. and Kamato, Danielle and Little, Peter J. and Zheng, Wenhua and Osman, Narin (2015) Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease. Clinical and Experimental Pharmacology and Physiology, 42 (2). pp. 117-124. E-ISSN 1440-1681

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Abstract

Peptidyl-prolyl cis/trans isomerases (PPIases) are a conserved group of enzymes that catalyse the conversion between cis and trans 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 cis/trans 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.

Item Type:	Article (Review)
Additional Information:	7744/55276
Uncontrolled Keywords:	atherosclerosis, cardiovascular disease, peptidylprolyl isomerase, Pin1
Subjects:	Q Science > QP Physiology
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button):	Kulliyyah of Allied Health Sciences > Department of Nutrition Sciences
Depositing User:	Dr Muhamad Ashraf Rostam
Date Deposited:	23 Mar 2017 09:40
Last Modified:	18 Jul 2017 08:30
URI:	http://irep.iium.edu.my/id/eprint/55276

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