在酵母双杂交筛选中鉴定猿猴亲环素A为钙网蛋白结合蛋白，并证明亲环素A与钙网蛋白相互作用。

Identification of simian cyclophilin A as a calreticulin-binding protein in yeast two-hybrid screen and demonstration of cyclophilin A interaction with calreticulin.

作者信息

Reddy P A, Atreya C D

机构信息

Section of Viral Pathogenesis and Adverse Reactions, Laboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA.

出版信息

Int J Biol Macromol. 1999 Aug;25(4):345-51. doi: 10.1016/s0141-8130(99)00053-7.

DOI:10.1016/s0141-8130(99)00053-7

PMID:10456775

Abstract

Cyclophilin A (CyPA) was identified as one of the calreticulin (CR)-binding proteins in a yeast two-hybrid screen utilizing simian cDNA expression-library. The simian CyPA protein had 96% identity with that of human, differing only at eight amino acid residues. We further established CyPA-CR interaction by incubation of glutathione transferase-fused CyPA (GST-CyPA) and CR proteins with CV-1 cyto-lysates, followed by CR and CyPA-specific immuno-blot analysis. The immunosuppressive drug cyclosporin A, a CyPA ligand, did not inhibit CyPA-CR interaction. Our results established a new property of CyPA binding activity to CR. Since CR is a Ca2+-binding protein, CR-CyPA interactions may be important in signaling pathways for induction of Ca2+-dependent cellular processes.

摘要

在利用猿猴cDNA表达文库进行的酵母双杂交筛选中，亲环素A（CyPA）被鉴定为钙网蛋白（CR）结合蛋白之一。猿猴CyPA蛋白与人类的具有96%的同一性，仅在八个氨基酸残基处有所不同。我们通过将谷胱甘肽转移酶融合的CyPA（GST-CyPA）和CR蛋白与CV-1细胞裂解物一起孵育，随后进行CR和CyPA特异性免疫印迹分析，进一步证实了CyPA-CR相互作用。免疫抑制药物环孢素A是一种CyPA配体，它并不抑制CyPA-CR相互作用。我们的结果确定了CyPA与CR结合活性的新特性。由于CR是一种Ca2+结合蛋白，CR-CyPA相互作用可能在诱导Ca2+依赖性细胞过程的信号通路中起重要作用。