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Peptidyl‐prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease
Author(s) -
Rostam Muhamad A,
Piva Terrence J,
Rezaei Hossein B,
Kamato Danielle,
Little Peter J,
Zheng Wenhua,
Osman Narin
Publication year - 2015
Publication title -
clinical and experimental pharmacology and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.752
H-Index - 103
eISSN - 1440-1681
pISSN - 0305-1870
DOI - 10.1111/1440-1681.12335
Subject(s) - pin1 , fkbp , peptidylprolyl isomerase , isomerase , prolyl isomerase , cis trans isomerases , biology , cell growth , cyclophilin , enzyme , microbiology and biotechnology , biochemistry , gene
Summary Peptidyl‐prolyl cis / trans isomerases ( PPI ases) 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 PPI ases and increasing interest in the development of specific PPI ase inhibitors. Cyclosporine A, FK 506, rapamycin and juglone are known PPI ase inhibitors. Herein, we review recent advances in elucidating the role and regulation of the PPI ase family in vascular disease. We focus on peptidyl‐prolyl cis / trans isomerase NIMA ‐interacting 1 (Pin1), an important member of the PPI ase 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.