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S-100蛋白和膜联蛋白II2-p11(2)(钙结合蛋白I)协同作用,调节胶质纤维酸性蛋白中间丝的组装状态。

S-100 protein and annexin II2-p11(2) (calpactin I) act in concert to regulate the state of assembly of GFAP intermediate filaments.

作者信息

Bianchi R, Garbuglia M, Verzini M, Giambanco I, Spreca A, Donato R

机构信息

Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.

出版信息

Biochem Biophys Res Commun. 1995 Mar 28;208(3):910-8. doi: 10.1006/bbrc.1995.1421.

DOI:10.1006/bbrc.1995.1421
PMID:7702620
Abstract

S-100 protein and annexin II2-p11(2) were reported to inhibit and to stimulate the assembly of glial fibrillary acidic protein (GFAP), respectively, in a Ca(2+)-dependent manner. Here we show by a number of experimental approaches that S-100 protein contrasts all the effects of annexin II2-p11(2) on GFAP assembly and, conversely, that annexin II2-p11(2) contrasts the inhibitory effects of S-100 protein on GFAP assembly, in a dose-dependent manner in both cases. Altogether, these data suggest that two specific Ca2+ effectors, i.e., annexin II2-p11(2) and S-100 protein, might regulate the state of assembly of glial filaments in a concerted manner.

摘要

据报道,S-100蛋白和膜联蛋白II2-p11(2)分别以Ca(2+)依赖的方式抑制和刺激胶质纤维酸性蛋白(GFAP)的组装。在这里,我们通过多种实验方法表明,S-100蛋白与膜联蛋白II2-p11(2)对GFAP组装的所有影响相反,反之亦然,膜联蛋白II2-p11(2)与S-100蛋白对GFAP组装的抑制作用相反,在两种情况下均呈剂量依赖性。总之,这些数据表明,两种特定的Ca2+效应物,即膜联蛋白II2-p11(2)和S-100蛋白,可能以协同方式调节胶质丝的组装状态。

相似文献

1
S-100 protein and annexin II2-p11(2) (calpactin I) act in concert to regulate the state of assembly of GFAP intermediate filaments.S-100蛋白和膜联蛋白II2-p11(2)(钙结合蛋白I)协同作用,调节胶质纤维酸性蛋白中间丝的组装状态。
Biochem Biophys Res Commun. 1995 Mar 28;208(3):910-8. doi: 10.1006/bbrc.1995.1421.
2
Annexin II2-p11(2) (calpactin I) stimulates the assembly of GFAP in a calcium- and pH-dependent manner.膜联蛋白II2-p11(2)(凝溶胶蛋白I)以钙和pH依赖的方式刺激胶质纤维酸性蛋白的组装。
Biochem Biophys Res Commun. 1995 Mar 28;208(3):901-9. doi: 10.1006/bbrc.1995.1420.
3
Characterization of type III intermediate filament regulatory protein target epitopes: S-100 (beta and/or alpha) binds the N-terminal head domain; annexin II2-p11(2) binds the rod domain.III型中间丝调节蛋白靶抗原表位的特性:S-100(β和/或α)结合N端头部结构域;膜联蛋白II2-p11(2)结合杆状结构域。
Biochim Biophys Acta. 1996 Oct 11;1313(3):268-76. doi: 10.1016/0167-4889(96)00099-7.
4
Calpactin I binds to the glial fibrillary acidic protein (GFAP) and cosediments with glial filaments in a Ca(2+)-dependent manner: implications for concerted regulatory effects of calpactin I and S100 protein on glial filaments.凝溶胶蛋白I以钙离子依赖的方式与胶质纤维酸性蛋白(GFAP)结合,并与胶质细丝共沉降:对凝溶胶蛋白I和S100蛋白对胶质细丝的协同调节作用的启示。
Biochim Biophys Acta. 1994 Sep 29;1223(3):361-7. doi: 10.1016/0167-4889(94)90096-5.
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S-100 protein binds to annexin II and p11, the heavy and light chains of calpactin I.S-100蛋白与膜联蛋白II以及钙结合蛋白I的重链和轻链p11相结合。
Biochim Biophys Acta. 1992 Nov 10;1160(1):67-75. doi: 10.1016/0167-4838(92)90039-g.
6
Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments.膜联蛋白VI与S100A1和S100B结合,并阻断S100A1和S100B抑制结蛋白和胶质纤维酸性蛋白组装成中间丝的能力。
Cell Calcium. 1998 Sep;24(3):177-91. doi: 10.1016/s0143-4160(98)90127-0.
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Mechanism of S100 protein-dependent inhibition of glial fibrillary acidic protein (GFAP) polymerization.
Biochim Biophys Acta. 1994 Sep 29;1223(3):354-60. doi: 10.1016/0167-4889(94)90095-7.
8
S-100 protein, but not calmodulin, binds to the glial fibrillary acidic protein and inhibits its polymerization in a Ca(2+)-dependent manner.
J Biol Chem. 1993 Jun 15;268(17):12669-74.
9
Assembly, disassembly, and exchange of glial fibrillary acidic protein.胶质纤维酸性蛋白的组装、拆卸及交换
Glia. 1991;4(1):101-10. doi: 10.1002/glia.440040112.
10
Distribution of glial fibrillary acidic protein (GFAP) in the intermediate filaments of the cultured cells from a patient with tuberous sclerosis.胶质纤维酸性蛋白(GFAP)在结节性硬化症患者培养细胞中间丝中的分布。
J Dermatol. 1990 Jul;17(7):395-402. doi: 10.1111/j.1346-8138.1990.tb01665.x.

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