Nath Pulak Ranjan, Isakov Noah
The Shraga Segal Department of Microbiology, Immunology and Genetics, Faculty of Health Sciences and the Cancer Research Center, Ben Gurion University of the Negev, P.O.B. 653, Beer Sheva 84105, Israel.
The Shraga Segal Department of Microbiology, Immunology and Genetics, Faculty of Health Sciences and the Cancer Research Center, Ben Gurion University of the Negev, P.O.B. 653, Beer Sheva 84105, Israel.
Immunol Lett. 2015 Jan;163(1):120-31. doi: 10.1016/j.imlet.2014.11.002. Epub 2014 Nov 13.
Peptidyl-prolyl isomerase (PPIase) catalyzes the interconversion of a specific Pro-imide bond between the cis and trans conformations. Two families of PPIases, cyclophilins and FKBPs, have been extensively studied because of their high affinity for immunosuppressive drugs in particular cyclosporine A and FK506. Despite apparent differences, these protein families share conserved amino acid sequences in their catalytic domains and impose similar enzymatic functions to their substrates. PPIases have been implicated in multiple aspects of cell cycle regulation and cellular processes related to a number of human pathologies, including cancer. More recent studies provide evidence for participation of PPIases in regulation of immune cell functions. In this review, we focus on the role of cyclophilins and FKBPs in the regulation of innate and adaptive immunity functions. PPIase-mediated isomerization of proteins represents a unique signaling mechanism that regulates normal immune functions and contributes to the development of immunopathologies. PPIases may therefore serve as useful diagnostic tools and potential therapeutic targets.
肽基脯氨酰异构酶（PPIase）催化特定脯氨酸-亚胺键在顺式和反式构象之间的相互转换。亲环蛋白和FK506结合蛋白这两个PPIase家族已得到广泛研究，因为它们对免疫抑制药物，尤其是环孢素A和FK506具有高亲和力。尽管存在明显差异，但这些蛋白质家族在其催化结构域中共享保守的氨基酸序列，并对其底物发挥相似的酶功能。PPIase与细胞周期调控的多个方面以及与包括癌症在内的许多人类疾病相关的细胞过程有关。最近的研究为PPIase参与免疫细胞功能的调节提供了证据。在本综述中，我们重点关注亲环蛋白和FK506结合蛋白在先天免疫和适应性免疫功能调节中的作用。PPIase介导的蛋白质异构化代表了一种独特的信号传导机制，可调节正常免疫功能并促进免疫病理的发展。因此，PPIase可能是有用的诊断工具和潜在的治疗靶点。
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