Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease
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...
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iium-552762017-07-18T00:30:05Z http://irep.iium.edu.my/55276/ Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease Rostam, Muhamad Ashraf Piva, Terence J. Rezaei, Hossein B. Kamato, Danielle Little, Peter J. Zheng, Wenhua Osman, Narin QP Physiology 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. Wiley Online Library 2015-02 Article PeerReviewed application/pdf en http://irep.iium.edu.my/55276/1/3.%20Rostam-2015-Peptidyl-prolyl%20isomerases_%20Functi.pdf application/pdf en http://irep.iium.edu.my/55276/7/55267-Peptidyl-prolyl%20isomerases_SCOPUS.pdf 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 http://onlinelibrary.wiley.com/doi/10.1111/1440-1681.12335/full 10.1111/1440-1681.12335 |
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QP Physiology Rostam, Muhamad Ashraf Piva, Terence J. Rezaei, Hossein B. Kamato, Danielle Little, Peter J. Zheng, Wenhua Osman, Narin Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease |
description |
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. |
format |
Article |
author |
Rostam, Muhamad Ashraf Piva, Terence J. Rezaei, Hossein B. Kamato, Danielle Little, Peter J. Zheng, Wenhua Osman, Narin |
author_facet |
Rostam, Muhamad Ashraf Piva, Terence J. Rezaei, Hossein B. Kamato, Danielle Little, Peter J. Zheng, Wenhua Osman, Narin |
author_sort |
Rostam, Muhamad Ashraf |
title |
Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease |
title_short |
Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease |
title_full |
Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease |
title_fullStr |
Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease |
title_full_unstemmed |
Peptidyl-prolyl isomerases: Functionality and potential therapeutic targets in cardiovascular disease |
title_sort |
peptidyl-prolyl isomerases: functionality and potential therapeutic targets in cardiovascular disease |
publisher |
Wiley Online Library |
publishDate |
2015 |
url |
http://irep.iium.edu.my/55276/ http://irep.iium.edu.my/55276/ http://irep.iium.edu.my/55276/ http://irep.iium.edu.my/55276/1/3.%20Rostam-2015-Peptidyl-prolyl%20isomerases_%20Functi.pdf http://irep.iium.edu.my/55276/7/55267-Peptidyl-prolyl%20isomerases_SCOPUS.pdf |
first_indexed |
2023-09-18T21:18:08Z |
last_indexed |
2023-09-18T21:18:08Z |
_version_ |
1777411700649099264 |