Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases

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Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases.

Peptidyl-prolyl cis-trans-isomerases are a highly conserved family of immunophilins. The three peptidyl-prolyl cis-trans-isomerase subfamilies are cyclophilins, FK-506-binding proteins, and parvulins. Peptidyl-prolyl cis-trans-isomerases are expressed in multiple human tissues and regulate different cellular functions, e.g. calcium handling, protein folding, and gene expression. Moreover, these...

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Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis.

Immunophilins are defined as receptors for immunosuppressive drugs including cyclosporin A, FK506, and rapamycin. The cyclosporin A receptors are referred to as cyclophilins (CYPs) and FK506- and rapamycin-binding proteins are abbreviated as FKBPs. These two groups of proteins (collectively called immunophilins) share little sequence homology, but both have peptidyl prolyl cis/trans isomerase (...

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Peptidyl-prolyl isomerases: a new twist to transcription.

Peptidyl-prolyl isomerases (PPIs) catalyse the cis-trans isomerisation of peptide bonds N-terminal to proline residues in polypeptide chains. They have roles in the folding of newly synthesised proteins and in the function of the immune system. In addition, members of the parvulin-like family of PPIs have been implicated in cell cycle control. Their activity is directed by the prior phosphoryla...

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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 three different classes of PPIases and increasing interest in the development of specific PPIase ...

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Prolyl isomerases in yeast.

Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1). Remarkably, two of these proteins, cyclop...

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ژورنال

عنوان ژورنال: Cardiovascular Research

سال: 2015

ISSN: 1755-3245,0008-6363

DOI: 10.1093/cvr/cvv096