胶质纤维酸性蛋白（GFA）的氨基酸序列数据；对中间丝细分为上皮和非上皮成员的意义。
Amino acid sequence data on glial fibrillary acidic protein (GFA); implications for the subdivision of intermediate filaments into epithelial and non-epithelial members.
作者信息
Geisler N, Weber K
出版信息
EMBO J. 1983;2(11):2059-63. doi: 10.1002/j.1460-2075.1983.tb01700.x.
Abstract
Determination of 50% of the sequence of the astrocyte-specific intermediate filament (IF) protein documents the hypervariable regions as well as parts of the coiled-coil array of glial fibrillary acidic protein (GFA). The results show that the four non-epithelial IF proteins (myogenic desmin, mesenchymal vimentin, GFA and neurofilament 68 K protein) known to form homopolymers are much more closely related than the epithelial keratins, which seem to form heteropolymers only. Of the four non-epithelial proteins, desmin and vimentin are the most closely related, since GFA has a shorter non-alpha-helical array at the amino terminus. We discuss the possibility that the non-alpha-helical terminal arrays, because of their sequence and length variability, are responsible for differences of distinct IF with respect to physical-chemical properties such as the low ionic strength-induced depolymerization into protofilaments.
摘要
对星形胶质细胞特异性中间丝（IF）蛋白50%的序列测定揭示了高变区以及胶质纤维酸性蛋白（GFA）卷曲螺旋阵列的部分区域。结果表明，已知能形成同聚物的四种非上皮性IF蛋白（肌源性结蛋白、间充质波形蛋白、GFA和神经丝68K蛋白）比似乎仅形成异聚物的上皮角蛋白关系更为密切。在这四种非上皮性蛋白中，结蛋白和波形蛋白关系最为密切，因为GFA在氨基末端的非α螺旋阵列较短。我们讨论了这样一种可能性，即非α螺旋末端阵列由于其序列和长度的变异性，导致不同的中间丝在物理化学性质上存在差异，例如在低离子强度下解聚成原丝。
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