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硫酸铵修饰盘基网柄菌的腺苷酸环化酶和趋化受体。G蛋白效应的证据。

Ammonium sulfate modifies adenylate cyclase and the chemotactic receptor of Dictyostelium discoideum. Evidence for a G protein effect.

作者信息

Khachatrian L, Howlett A, Klein C

出版信息

J Biol Chem. 1987 Jun 15;262(17):8071-6.

PMID:3110144
Abstract

(NH4)2SO4 was found to activate adenylate cyclase in Dictyostelium discoideum membranes. The effect of (NH4)2SO4 on the enzyme was observed after pretreatment of membranes but could not be observed if the salt was added to the assay mixture. Activation was seen when membranes were pretreated with 0.16 M (NH4)2SO4 and was maximal at 0.6-1.0 M. The maximal activation of the enzyme was observed within 3 min of pretreatment and was not readily reversible. The effect was specific for the NH+4 ion since pretreatment of membranes with other NH+4 salts could activate the enzyme, whereas pretreatment with NaCl or KCl could not. Pretreatment of plasma membranes with (NH4)2SO4 eliminated the sensitivity of the enzyme to the inhibitory effect of guanine nucleotides. (NH4)2SO4 pretreatment also significantly attenuated the inhibition by guanine nucleotides of cAMP binding to its plasma membrane receptor. The effect of (NH4)2SO4 on GTP inhibition of cAMP binding to its receptor was even more dramatic when the salt was present in the binding assay. (NH4)2SO4 also increased the ADP-ribosylation by cholera toxin of a 39,000-Da membrane protein. The data support the hypothesis that (NH4)2SO4-induced changes in adenylate cyclase and the cAMP receptor are due to an alteration of a putative G protein.

摘要

已发现硫酸铵((NH4)2SO4)可激活盘基网柄菌(Dictyostelium discoideum)细胞膜中的腺苷酸环化酶。在对细胞膜进行预处理后可观察到(NH4)2SO4对该酶的作用,但如果将盐添加到测定混合物中则无法观察到这种作用。当用0.16 M (NH4)2SO4预处理细胞膜时可观察到激活作用,在0.6 - 1.0 M时激活作用最大。在预处理3分钟内观察到该酶的最大激活,且这种激活不易逆转。该作用对NH4+离子具有特异性,因为用其他NH4+盐预处理细胞膜可激活该酶,而用NaCl或KCl预处理则不能。用(NH4)2SO4预处理质膜消除了该酶对鸟嘌呤核苷酸抑制作用的敏感性。(NH4)2SO4预处理还显著减弱了鸟嘌呤核苷酸对cAMP与其质膜受体结合的抑制作用。当在结合测定中存在该盐时,(NH4)2SO4对GTP抑制cAMP与其受体结合的作用更为显著。(NH4)2SO4还增加了霍乱毒素对一种39,000道尔顿膜蛋白的ADP核糖基化作用。这些数据支持以下假说:(NH4)2SO4诱导的腺苷酸环化酶和cAMP受体的变化是由于一种假定的G蛋白的改变所致。

相似文献

1
Ammonium sulfate modifies adenylate cyclase and the chemotactic receptor of Dictyostelium discoideum. Evidence for a G protein effect.硫酸铵修饰盘基网柄菌的腺苷酸环化酶和趋化受体。G蛋白效应的证据。
J Biol Chem. 1987 Jun 15;262(17):8071-6.
2
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Adenosine 3', 5'-monophosphorothioate (Rp-isomer) induces down-regulation of surface cyclic AMP receptors without receptor activation in Dictyostelium discoideum.3',5'-单磷酸硫代腺苷(Rp-异构体)在盘基网柄菌中可诱导表面环磷酸腺苷受体的下调,而无需受体激活。
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ADP-ribosylation by cholera toxin of membranes derived from brain modifies the interaction of adenylate cyclase with guanine nucleotides and NaF.霍乱毒素对源自大脑的膜进行的ADP核糖基化修饰了腺苷酸环化酶与鸟嘌呤核苷酸及氟化钠的相互作用。
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引用本文的文献

1
The cell density factor CMF regulates the chemoattractant receptor cAR1 in Dictyostelium.细胞密度因子CMF调节盘基网柄菌中的趋化因子受体cAR1。
J Cell Biol. 1996 Sep;134(6):1543-9. doi: 10.1083/jcb.134.6.1543.
2
Ammonia inhibits cAMP-regulated intestinal Cl- transport. Asymmetric effects of apical and basolateral exposure and implications for epithelial barrier function.氨抑制环磷酸腺苷(cAMP)调节的肠道氯离子转运。顶端和基底外侧暴露的不对称效应及其对上皮屏障功能的影响。
J Clin Invest. 1995 Nov;96(5):2142-51. doi: 10.1172/JCI118268.
3
Evidence that a glycolipid tail anchors antigen 117 to the plasma membrane of Dictyostelium discoideum cells.
有证据表明糖脂尾巴将抗原117锚定在盘基网柄菌细胞的质膜上。
Proc Natl Acad Sci U S A. 1988 Aug;85(15):5512-5. doi: 10.1073/pnas.85.15.5512.
4
An unusual protein kinase phosphorylates the chemotactic receptor of Dictyostelium discoideum.一种特殊的蛋白激酶使盘基网柄菌的趋化受体发生磷酸化。
Proc Natl Acad Sci U S A. 1988 Apr;85(7):2181-5. doi: 10.1073/pnas.85.7.2181.
5
Genetics of early Dictyostelium discoideum development.盘基网柄菌早期发育的遗传学
Microbiol Rev. 1988 Mar;52(1):29-49. doi: 10.1128/mr.52.1.29-49.1988.
6
Properties of CAR-kinase: the enzyme that phosphorylates the cAMP chemotactic receptor of D. discoideum.CAR激酶的特性:使盘基网柄菌的cAMP趋化受体磷酸化的酶。
J Protein Chem. 1990 Oct;9(5):565-72. doi: 10.1007/BF01025009.
7
Dual role of GDP in the regulation of the levels of p36 phosphorylation in Dictyostelium discoideum.
J Protein Chem. 1991 Aug;10(4):391-401. doi: 10.1007/BF01025253.