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阳离子在调节己糖激酶I和II与线粒体结合中的相互作用。

Interactions between cations in modifying the binding of hexokinases I and II to mitochondria.

作者信息

Imai N, Akimoto H, Oda M, Okazaki H, Ishibashi S, Kurokawa M

机构信息

Department of Physiological Chemistry, Hiroshima University School of Medicine, Japan.

出版信息

Mol Cell Biochem. 1988 May;81(1):37-41. doi: 10.1007/BF00225651.

DOI:10.1007/BF00225651
PMID:3173344
Abstract

Interactions between cations in modifying the binding of hexokinases I and II to mitochondria was examined with reference to the intracellular condition. Mitochondria-binding of either of hexokinases I and II, both prepared from mouse ascites ELD cells, was markedly increased by Mg2+ as has been known well. However, even in the absence of Mg2+, marked binding was attained by 100 mM K+ alone especially for hexokinase I, which seemed generally more ready to bind to mitochondria. On the other hand, the effect of Mg2+ to increase the binding was reduced by the addition of K+, and the decreasing effect of K+ was much more marked for hexokinase II than I. These results indicate that, in addition to Mg2+, monovalent cations as represented by K+, also have marked effect on the binding, and the effect is different for each hexokinases I and II, which may be responsible for the difference in the intracellular distribution between these hexokinases.

摘要

参照细胞内环境,研究了阳离子在调节己糖激酶I和II与线粒体结合中的相互作用。从小鼠腹水ELD细胞制备的己糖激酶I和II与线粒体的结合,如所知,均被Mg2+显著增强。然而,即使在没有Mg2+的情况下,仅100 mM K+就能实现显著结合,尤其是对于己糖激酶I,它似乎通常更容易与线粒体结合。另一方面,添加K+会降低Mg2+增加结合的效果,且K+对己糖激酶II的降低作用比对I更显著。这些结果表明,除了Mg2+之外,以K+为代表的单价阳离子对结合也有显著影响,且对己糖激酶I和II的影响不同,这可能是这些己糖激酶在细胞内分布差异的原因。

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本文引用的文献

1
Characterization of hexokinase isoenzyme types I and II in ascites tumor cells by an interaction with mitochondrial membrane.
Mol Cell Biochem. 1982 Jun 25;45(3):151-7. doi: 10.1007/BF00230083.
2
Brain hexokinase, the prototype ambiquitous enzyme.脑己糖激酶,典型的普遍存在的酶。
Curr Top Cell Regul. 1980;16:1-54. doi: 10.1016/b978-0-12-152816-4.50005-4.
3
Polyamines stimulate the binding of hexokinase type II to mitochondria.多胺刺激II型己糖激酶与线粒体的结合。
Biochim Biophys Acta. 1983 Aug 23;759(1-2):92-8. doi: 10.1016/0304-4165(83)90193-9.
4
Difference in hydrophobicity between mitochondria-bindable and non-bindable forms of hexokinase purified from rat brain.从大鼠脑中纯化得到的可与线粒体结合和不可与线粒体结合的己糖激酶形式之间的疏水性差异。
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Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria.大鼠肝线粒体外膜中己糖激酶结合蛋白与线粒体孔蛋白同一性的证据。
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Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical.大鼠肝脏线粒体外膜的孔蛋白和己糖激酶结合蛋白是相同的。
FEBS Lett. 1982 May 17;141(2):189-92. doi: 10.1016/0014-5793(82)80044-6.
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Mitochondrial hexokinase. Release, rebinding, and location.线粒体己糖激酶。释放、重新结合及定位
J Biol Chem. 1967 Apr 10;242(7):1635-45.
8
Multiple forms of hexokinase. Activities associated with subcellular particulate and soluble fractions of normal and streptozotocin diabetic rat tissues.己糖激酶的多种形式。正常和链脲佐菌素诱导的糖尿病大鼠组织的亚细胞颗粒和可溶部分的相关活性。
J Biol Chem. 1970 Aug 25;245(16):4081-96.
9
Possible processing of mitochondria-bindable hexokinase to the nonbindable form by a lysosomal protease in rat liver.大鼠肝脏中溶酶体蛋白酶可能将可结合线粒体的己糖激酶加工成不可结合形式。
Arch Biochem Biophys. 1987 Aug 15;257(1):56-62. doi: 10.1016/0003-9861(87)90542-x.
10
An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria.完整的疏水N端序列对于大鼠脑己糖激酶与线粒体的结合至关重要。
Arch Biochem Biophys. 1985 Jan;236(1):328-37. doi: 10.1016/0003-9861(85)90633-2.