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一种钙调蛋白依赖性的Ca2+调节的Mg2+依赖性ATP酶是否参与肝微粒体对钙的摄取？

Does a calmodulin-dependent Ca2+-regulated Mg2+-dependent ATPase contribute to hepatic microsomal calcium uptake?

作者信息

Schütze S, Söling H D

机构信息

Zentrum Innere Medizin, Univerität Göttingen, Federal Republic of Germany.

出版信息

Biochem J. 1987 May 1;243(3):729-37. doi: 10.1042/bj2430729.

DOI:10.1042/bj2430729
PMID:2959269
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1147919/
Abstract

Solubilization of microsomal proteins followed by calmodulin affinity chromatography resulted in the separation of two distinct Ca2+-Mg2+-ATPases (Ca2+-regulated Mg2+-dependent ATPases), one being insensitive to calmodulin (ATPase-1), the other being stimulated about 5-fold by calmodulin (ATPase-2). ATPase-2 accounts for only 8% of total microsomal Ca2+-Mg2+-ATPase-activity. ATPase-1 and -2 can also be distinguished by different pH optima, different sensitivity towards inhibition by vanadate and LaCl3, and different apparent Mr values of the phosphoenzyme intermediates (115,000 and 150,000 for ATPase-1 and ATPase-2 respectively). ATPase-1 from liver co-migrated with Ca2+-Mg2+-ATPase from rat skeletal-muscle sarcoplasmic reticulum, whereas ATPase-2 from liver co-migrated with calmodulin-dependent Ca2+-Mg2+-ATPase derived from rat skeletal-muscle sarcolemma. After separation of parenchymal and nonparenchymal liver cells, a calmodulin-dependent Ca2+-Mg2+-ATPase of Mr 150,000 was found only in the non-parenchymal cells. The kinetic parameters of ATPase-2 and the similarity of the apparent Mr of its phosphoenzyme intermediate to that of skeletal-muscle sarcolemma Ca2+-Mg2+-ATPase makes it likely that the calmodulin-sensitive Ca2+-Mg2+-ATPase found in rat liver microsomal fractions reflects a contamination with plasma membranes (possibly from non-parenchymal cells) rather than a true location in the endoplasmic reticulum of parenchymal liver cells.

摘要

微粒体蛋白经溶解后，再通过钙调蛋白亲和层析法，分离出两种不同的Ca2+-Mg2+-ATP酶（Ca2+调节的Mg2+依赖性ATP酶），一种对钙调蛋白不敏感（ATP酶-1），另一种被钙调蛋白刺激约5倍（ATP酶-2）。ATP酶-2仅占微粒体Ca2+-Mg2+-ATP酶总活性的8%。ATP酶-1和-2也可通过不同的最适pH值、对钒酸盐和LaCl3抑制的不同敏感性以及磷酸化酶中间体不同的表观Mr值（ATP酶-1和ATP酶-2分别为115,000和150,000）来区分。肝脏中的ATP酶-1与大鼠骨骼肌肌浆网中的Ca2+-Mg2+-ATP酶共迁移，而肝脏中的ATP酶-2与源自大鼠骨骼肌肌膜的钙调蛋白依赖性Ca2+-Mg2+-ATP酶共迁移。在分离实质肝细胞和非实质肝细胞后，仅在非实质细胞中发现了Mr为150,000的钙调蛋白依赖性Ca2+-Mg2+-ATP酶。ATP酶-2的动力学参数及其磷酸化酶中间体的表观Mr与骨骼肌肌膜Ca2+-Mg2+-ATP酶的相似性表明，大鼠肝脏微粒体组分中发现的钙调蛋白敏感的Ca2+-Mg2+-ATP酶可能反映了质膜（可能来自非实质细胞）的污染，而不是实质肝细胞内质网中的真实定位。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/818a/1147919/9bd88917205a/biochemj00256-0114-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/818a/1147919/92dd7c904930/biochemj00256-0113-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/818a/1147919/9bd88917205a/biochemj00256-0114-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/818a/1147919/92dd7c904930/biochemj00256-0113-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/818a/1147919/9bd88917205a/biochemj00256-0114-a.jpg

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本文引用的文献

1
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Biochim Biophys Acta. 1962 May 14;55:571-83. doi: 10.1016/0006-3002(62)90836-3.
2
Calcium uptake in isolated hepatic plasma-membrane vesicles.分离的肝细胞膜囊泡对钙的摄取
Eur J Biochem. 1982 Dec;129(1):7-12. doi: 10.1111/j.1432-1033.1982.tb07014.x.
3
Localization of calmodulin in rat tissues.钙调蛋白在大鼠组织中的定位。
J Membr Biol. 1990 Oct;118(1):49-53. doi: 10.1007/BF01872203.
Proc Natl Acad Sci U S A. 1980 Jan;77(1):366-70. doi: 10.1073/pnas.77.1.366.
4
Lack of desensitization against alpha-agonists and vasopressin in the liver.
FEBS Lett. 1983 Mar 7;153(1):174-8. doi: 10.1016/0014-5793(83)80142-2.
5
Kinetic properties of the Ca2+-accumulation system of a rat liver microsomal fraction.大鼠肝微粒体组分钙积累系统的动力学特性
Biochem J. 1982 Jul 15;206(1):73-9. doi: 10.1042/bj2060073.
6
Calmodulin purification and fluorescent labeling.钙调蛋白的纯化与荧光标记。
Methods Enzymol. 1983;102:1-8. doi: 10.1016/s0076-6879(83)02003-0.
7
Changes in the sarcoplasmic reticulum ATPase protein under denaturing conditions used for sodium dodecyl sulfate--polyacrylamide gel electrophoresis.用于十二烷基硫酸钠-聚丙烯酰胺凝胶电泳的变性条件下肌浆网ATP酶蛋白的变化。
Arch Biochem Biophys. 1981 Jun;209(1):237-40. doi: 10.1016/0003-9861(81)90276-9.
8
The Ca2+-pumping ATPase of heart sarcolemma. Characterization, calmodulin dependence, and partial purification.心脏肌膜的钙离子泵ATP酶。特性、钙调蛋白依赖性及部分纯化
J Biol Chem. 1981 Apr 10;256(7):3263-70.
9
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10
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