THE COUPLING OF PERTUSSIS-TOXIN-SENSITIVE G-PROTEINS TO PHOSPHOLIPASE A(2) AND ADENYLYL-CYCLASE IN CHO CELLS EXPRESSING BOVINE RHODOPSIN
THE COUPLING OF PERTUSSIS-TOXIN-SENSITIVE G-PROTEINS TO PHOSPHOLIPASE A(2) AND ADENYLYL-CYCLASE IN CHO CELLS EXPRESSING BOVINE RHODOPSIN
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DOI：
10.1006/excr.1995.1006
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发表时间：
1995-01-01
影响因子：
3.7
通讯作者：
WEISS, ER
中科院分区：
文献类型：
--
作者：
DICKERSON, CD;WEISS, ER
在正常表达嘌呤能受体的CHO细胞中，检测了G蛋白偶联受体对磷脂酶A(2)的调节。据报道，嘌呤能受体激活该细胞系中的磷脂酶C和磷脂酶A(2)。相比之下，牛视紫质本身不能激活磷脂酶A(2)。然而，光感受器确实以光依赖的方式增强了嘌呤能受体介导的磷脂酶A(2)的激活。嘌呤能受体对磷脂酶A(2)的刺激和视紫红质介导的活性增强都是完全对百日咳毒素敏感的，提示磷脂酶A(2)是由G(I)家族G蛋白的一个成员调节的。这两种受体也抑制腺苷环化酶的活性。视紫红质介导的腺苷环化酶抑制是百日咳毒素敏感的，而嘌呤能受体抑制是钙敏感的，但不是百日咳毒素敏感的。这些结果表明：(1)视紫红质类似于在培养细胞中表达时通常与G(I)偶联的其他受体；(2)视紫红质和嘌呤能受体通过不同的途径调节CHO细胞中的腺苷环化酶和磷脂酶A(2)。(C)1995年学术出版社。
The regulation of phospholipase A(2) by G protein-coupled receptors is examined in CHO cells which normally express the purinergic receptor and have been transfected with bovine rhodopsin. The purinergic receptor has been reported to activate both phospholipase C and phospholipase A(2) in this cell line. In contrast, bovine rhodopsin by itself is not able to activate phospholipase A(2). However, the photoreceptor does potentiate purinergic receptor-mediated phospholipase A(2) activation in a light-dependent manner. Both the purinergic receptor stimulation of phospholipase A(2) and the enhanced activity mediated by rhodopsin are completely pertussis toxin-sensitive, suggesting the regulation of phospholipase A(2) by a member of the G(i) family of G proteins. Both of these receptors also inhibit adenylyl cyclase activity. Rhodopsin-mediated inhibition of adenylyl cyclase is pertussis toxin-sensitive, whereas inhibition by the purinergic receptor is calcium-sensitive but not pertussis toxin-sensitive. These results suggest (1) that rhodopsin is similar to other receptors that normally couple to G(i) when expressed in cultured cells and (2) that regulation of adenylyl cyclase and PLA(2) in CHO cells by rhodopsin and the purinergic receptor occur via distinct pathways. (C) 1995 Academic Press, Inc.