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αB晶状体蛋白在牛关节软骨细胞培养物中组成性表达。

Alpha B crystallin is constitutively expressed in cultures of bovine articular chondrocytes.

作者信息

Bennardini F, Juliano C, Benetti D, Mian M, Chiesi M, Mattana A, Franconi F

机构信息

Istituto di Chimica Biologica, Facoltà di Farmacia, Università di Sassari, Italia.

出版信息

Biochem Biophys Res Commun. 1995 Mar 17;208(2):742-7. doi: 10.1006/bbrc.1995.1400.

DOI:10.1006/bbrc.1995.1400
PMID:7695631
Abstract

alpha B crystallin is a small heat shock protein constitutively expressed in the mammalian lens and in a variety of extraocular tissues. We report here the presence of alpha B crystallin also in bovine articular chondrocytes by means of an immunoblot and immunofluorescence analysis carried out with anti-alpha B crystallin polyclonal antibodies. The expression level of alpha B crystallin can be further induced by a short heat shock treatment of chondrocytes as well as cell treatment with cadmium bromide or calcium ionophore A 23187. The level of alpha B crystallin expression is not modified by treating chondrocytes with interleukin-1 and phorbol 12-myristate 13-acetate. In some preparations the antibodies recognise two bands of alpha B crystallin, probably corresponding to different degrees of protein phosphorylation, but in cells treated with phorbol ester a single band is constantly observed, indicating a complete phosphorylation of alpha B crystallin.

摘要

αB晶状体蛋白是一种小分子热休克蛋白,在哺乳动物晶状体及多种眼外组织中组成性表达。我们在此报告,通过使用抗αB晶状体蛋白多克隆抗体进行免疫印迹和免疫荧光分析,发现牛关节软骨细胞中也存在αB晶状体蛋白。软骨细胞经短暂热休克处理以及用溴化镉或钙离子载体A 23187处理后,αB晶状体蛋白的表达水平可进一步诱导。用白细胞介素-1和佛波醇12-肉豆蔻酸酯13-乙酸酯处理软骨细胞不会改变αB晶状体蛋白的表达水平。在某些制剂中,抗体可识别αB晶状体蛋白的两条条带,可能对应不同程度的蛋白质磷酸化,但在用佛波醇酯处理的细胞中,始终观察到一条条带,表明αB晶状体蛋白已完全磷酸化。

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Alpha B crystallin is constitutively expressed in cultures of bovine articular chondrocytes.αB晶状体蛋白在牛关节软骨细胞培养物中组成性表达。
Biochem Biophys Res Commun. 1995 Mar 17;208(2):742-7. doi: 10.1006/bbrc.1995.1400.
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引用本文的文献

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Alpha B-Crystallin Protects Rat Articular Chondrocytes against Casein Kinase II Inhibition-Induced Apoptosis.αB-晶状体蛋白保护大鼠关节软骨细胞免受酪蛋白激酶II抑制诱导的凋亡。
PLoS One. 2016 Nov 16;11(11):e0166450. doi: 10.1371/journal.pone.0166450. eCollection 2016.