CLONING AND CHARACTERIZATION OF CYCLOPHILIN C-ASSOCIATED PROTEIN - A CANDIDATE NATURAL CELLULAR LIGAND FOR CYCLOPHILIN-C

被引：95

作者：

FRIEDMAN, J ^{[1
]}

TRAHEY, M ^{[1
]}

WEISSMAN, I ^{[1
]}

机构：

[1] STANFORD UNIV,MED CTR,SCH MED,DEPT DEV BIOL,STANFORD,CA 94305

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 14期

关键词：

CYCLOPHILIN; CYCLOSPORINE-A; PROLINE ISOMERASE; SIGNAL TRANSDUCTION;

D O I：

10.1073/pnas.90.14.6815

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We report the protein purification and the cloning and characterization of a cDNA encoding the proteins that bind with high affinity to cyclophilin C (Cyp-C) in the absence of cyclosporin A. Transfection of this cDNA into COS cells directs the production of a glycoprotein of 77 kDa that binds to Cyp-C in the absence, but not the presence, of cyclosporin A. Homology comparisons reveal that this protein and gene, termed CyCAP for Cyp-C-associated protein, possess a cysteine-rich domain (scavenger receptor cysteine-rich domain) found in a variety of cell-surface molecules; the rest of the sequence is apparently specific. This result raises the possibility that Cyp-C serves as a mediator or regulator of an as-yet-unidentified signal or cellular process initiated via the Cyp-C-associated protein.

引用

页码：6815 / 6819

页数：5