PURIFICATION AND CHARACTERIZATION OF THE INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR PROTEIN FROM RAT VAS-DEFERENS

被引:99
作者
MOUREY, RJ
VERMA, A
SUPATTAPONE, S
SNYDER, SH
机构
[1] JOHNS HOPKINS UNIV,SCH MED,DEPT NEUROSCI,725 N WOLFE ST,BALTIMORE,MD 21205
[2] JOHNS HOPKINS UNIV,SCH MED,DEPT PHARMACOL,BALTIMORE,MD 21205
[3] JOHNS HOPKINS UNIV,SCH MED,DEPT PSYCHIAT,BALTIMORE,MD 21205
[4] JOHNS HOPKINS UNIV,SCH MED,DEPT PHARMACEUT SCI,BALTIMORE,MD 21205
关键词
D O I
10.1042/bj2720383
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Among rat peripheral tissues examined, Ins(1,4,5)P3 receptor binding is highest in the vas deferens, with levels about 25% of those of the cerebellum. We have purified the InsP3 receptor binding protein from rat vas deferens membranes 600-fold. The purified protein displays a single 260 kDa band on SDS/PAGE, and the native protein has an apparent molecular mass of 1000 kDa, the same as in cerebellum. The inositol phosphate specificity, pH-dependence and influence of various reagents are the same for purified vas deferens and cerebellar receptors. Whereas particulate InsP3 binding in cerebellum is potently inhibited by Ca2+, particulate and purified vas deferens receptor binding of InsP3 is not influenced by Ca2+. Vas deferens appears to lack calmedin activity, but the InsP3 receptor is sensitive to Ca2+ inhibition conferred by brain calmedin. The vas deferens may prove to be a valuable tissue for characterizing functional aspects of InsP3 receptors.
引用
收藏
页码:383 / 389
页数:7
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