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淀粉样β蛋白前体的表达可保护神经细胞免受β-淀粉样蛋白和谷氨酸毒性的影响,并改变它们与细胞外基质的相互作用。

The expression of amyloid beta protein precursor protects nerve cells from beta-amyloid and glutamate toxicity and alters their interaction with the extracellular matrix.

作者信息

Schubert D, Behl C

机构信息

Salk Institute for Biological Studies, San Diego, CA 92186-5800.

出版信息

Brain Res. 1993 Dec 3;629(2):275-82. doi: 10.1016/0006-8993(93)91331-l.

Abstract

The biological function of amyloid beta protein precursor (ABPP) in nerve cells is examined by transfecting it into the B103 clonal nerve cell line which makes no ABPP and asking if a variety of biological activities are altered. Although ABPP is expressed by the transfected cells at high levels, there are no detectable differences between the ABPP negative clones and the clones expressing ABPP with respect to growth rate in high serum medium, dibutyryl-cyclic AMP-induced differentiation, or morphology on plastic culture dishes. There are, however, significant differences in a number of properties between the two groups of cell lines. Cells expressing ABPP adhere more rapidly and have an enhanced rate of neurite outgrowth on collagen substrata. They also grow more rapidly in low serum medium. Finally, the expression of ABPP weakly but significantly protects the nerve cells from amyloid beta protein and glutamate toxicity.

摘要

通过将淀粉样β蛋白前体(ABPP)转染到不产生ABPP的B103克隆神经细胞系中,并询问各种生物学活性是否发生改变,来研究其在神经细胞中的生物学功能。尽管转染细胞高水平表达ABPP,但在高血清培养基中的生长速率、二丁酰环磷腺苷诱导的分化或塑料培养皿上的形态方面,ABPP阴性克隆与表达ABPP的克隆之间没有可检测到的差异。然而,两组细胞系在许多特性上存在显著差异。表达ABPP的细胞黏附更快,在胶原蛋白基质上神经突生长速率加快。它们在低血清培养基中也生长得更快。最后,ABPP的表达对神经细胞具有微弱但显著的保护作用,使其免受淀粉样β蛋白和谷氨酸毒性的影响。

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