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胶质纤维酸性蛋白的分子特性、分布及异质性:施万细胞、卫星细胞、肠神经胶质细胞和星形胶质细胞的免疫印迹及免疫组织化学研究

Molecular identity, distribution and heterogeneity of glial fibrillary acidic protein: an immunoblotting and immunohistochemical study of Schwann cells, satellite cells, enteric glia and astrocytes.

作者信息

Jessen K R, Thorpe R, Mirsky R

出版信息

J Neurocytol. 1984 Apr;13(2):187-200. doi: 10.1007/BF01148114.

Abstract

Glial fibrillary acidic protein has been firmly established as the predominant component of astrocyte intermediate filaments. It has also been detected immunohistochemically in the glial cells of the enteric nervous system and some Schwann cells in the P.N.S. The molecular identity of this GFAP immunoreactivity in the P.N.S. has so far not been investigated. This study compares GFAP in the C.N.S. and P.N.S. of adult rats both immunochemically and immunohistochemically. Using SDS polyacrylamide gel electrophoresis combined with immunoblotting, and a polyclonal antiserum to brain GFAP, we show that the peripheral GFAP immunoreactivity resides in a polypeptide with a molecular weight of 49 kd, which is identical to that of rat brain GFAP. Furthermore, we find that this GFAP reactivity can be detected immunohistochemically in Schwann cells in a wide variety of nerves in the P.N.S. and in some satellite cells in both sensory and sympathetic ganglia, in addition to enteric glia. The pattern of distribution of GFAP filaments in Schwann cells suggests that, in the nerves surveyed, they may be expressed by most or all non-myelin forming Schwann cells but not by myelin-forming Schwann cells. We also show, using a monoclonal antibody to GFAP (anti-GFAP-3) in both immunohistochemical and immunoblotting studies, that the GFAP found in most peripheral glia is not identical to that of astrocytes since it lacks an antigenic determinant, defined by this monoclonal antibody, which is present in astrocytes. An exception to this finding is seen in the myenteric plexuses where immunohistochemically detectable GFAP is found in some, but not all, of the enteric glia, using the monoclonal antibody. Thus, the results suggest that GFA polypeptides may be a heterogeneous group, that share some common determinants and a common molecular weight, and show a widespread and complex distribution in the glia of both the C.N.S. and P.N.S.

摘要

胶质纤维酸性蛋白已被确认为星形胶质细胞中间丝的主要成分。免疫组织化学方法也在肠神经系统的神经胶质细胞以及周围神经系统的一些雪旺细胞中检测到了该蛋白。迄今为止,尚未对周围神经系统中这种胶质纤维酸性蛋白免疫反应性的分子特性进行研究。本研究采用免疫化学和免疫组织化学方法,对成年大鼠中枢神经系统和周围神经系统中的胶质纤维酸性蛋白进行了比较。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳结合免疫印迹法,以及针对脑胶质纤维酸性蛋白的多克隆抗血清,我们发现周围神经胶质纤维酸性蛋白免疫反应性存在于一种分子量为49kd的多肽中,这与大鼠脑胶质纤维酸性蛋白相同。此外,我们发现,除了肠神经胶质细胞外,在周围神经系统的多种神经中的雪旺细胞以及感觉和交感神经节的一些卫星细胞中,均可通过免疫组织化学方法检测到这种胶质纤维酸性蛋白反应性。雪旺细胞中胶质纤维酸性蛋白丝的分布模式表明,在所研究的神经中,它们可能由大多数或所有非形成髓鞘的雪旺细胞表达,而不由形成髓鞘的雪旺细胞表达。我们还通过免疫组织化学和免疫印迹研究,使用针对胶质纤维酸性蛋白的单克隆抗体(抗胶质纤维酸性蛋白-3)表明,大多数周围神经胶质细胞中发现的胶质纤维酸性蛋白与星形胶质细胞中的不同,因为它缺乏由该单克隆抗体定义的、存在于星形胶质细胞中的一个抗原决定簇。使用该单克隆抗体进行免疫组织化学检测时,在肌间神经丛中发现了一个例外情况,其中一些但并非所有肠神经胶质细胞中均可检测到胶质纤维酸性蛋白。因此,结果表明,胶质纤维酸性蛋白多肽可能是一个异质群体,它们具有一些共同的决定簇和共同的分子量,并且在中枢神经系统和周围神经系统的神经胶质细胞中均呈现广泛而复杂的分布。

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