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生长抑素对S49淋巴瘤cyc-变异体中腺苷酸环化酶的抑制作用及对GTP酶的刺激作用可被胰岛激活蛋白阻断。

Adenylate cyclase inhibition and GTPase stimulation by somatostatin in S49 lymphoma cyc- variants are prevented by islet-activating protein.

作者信息

Aktories K, Schultz G, Jakobs K H

出版信息

FEBS Lett. 1983 Jul 11;158(1):169-73. doi: 10.1016/0014-5793(83)80701-7.

DOI:10.1016/0014-5793(83)80701-7
PMID:6134642
Abstract

cyc--Variants of S49 lymphoma cells are defective in the stimulatory guanine nucleotide site of the adenylate cyclase but contain an inhibitory site. Treatment of cyc- cells with islet-activating protein (IAP), which causes ADP-ribosylation of an Mr 40 000 polypeptide in cyc- membranes, abolishes adenylate cyclase inhibition by GTP and the peptide hormone, somatostatin, but not that induced by GTP gamma S. Furthermore, somatostatin-induced stimulation of GTP hydrolysis is lost. Thus, the data indicate that IAP interferes with the adenylate cyclase system by an action at the inhibitory guanine nucleotide site.

摘要

cyc-——S49淋巴瘤细胞变体在腺苷酸环化酶的刺激性鸟嘌呤核苷酸位点存在缺陷,但含有一个抑制性位点。用胰岛激活蛋白(IAP)处理cyc-细胞,IAP会使cyc-细胞膜中一种分子量为40000的多肽发生ADP核糖基化,这消除了GTP和肽激素生长抑素对腺苷酸环化酶的抑制作用,但对GTPγS诱导的抑制作用没有影响。此外,生长抑素诱导的GTP水解刺激作用丧失。因此,数据表明IAP通过作用于抑制性鸟嘌呤核苷酸位点干扰腺苷酸环化酶系统。

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1
Adenylate cyclase inhibition and GTPase stimulation by somatostatin in S49 lymphoma cyc- variants are prevented by islet-activating protein.生长抑素对S49淋巴瘤cyc-变异体中腺苷酸环化酶的抑制作用及对GTP酶的刺激作用可被胰岛激活蛋白阻断。
FEBS Lett. 1983 Jul 11;158(1):169-73. doi: 10.1016/0014-5793(83)80701-7.
2
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A nucleotide regulatory site for somatostatin inhibition of adenylate cyclase in S49 lymphoma cells.S49淋巴瘤细胞中生长抑素抑制腺苷酸环化酶的核苷酸调节位点。
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