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一种识别A链神经突促进肽的110 kDa非整合素细胞表面层粘连蛋白的鉴定。

Identification of a 110-kDa nonintegrin cell surface laminin-binding protein which recognizes an A chain neurite-promoting peptide.

作者信息

Kleinman H K, Weeks B S, Cannon F B, Sweeney T M, Sephel G C, Clement B, Zain M, Olson M O, Jucker M, Burrous B A

机构信息

Laboratory of Developmental Biology, National Institute of Dental Research, Bethesda, Maryland 20892.

出版信息

Arch Biochem Biophys. 1991 Nov 1;290(2):320-5. doi: 10.1016/0003-9861(91)90547-v.

DOI:10.1016/0003-9861(91)90547-v
PMID:1834017
Abstract

Laminin is a potent promoter of neurite outgrowth, and a synthetic peptide of 19 amino acids, PA22-2, from the A chain has been found to promote process formation. Using peptide affinity chromatography, we have identified a 110-kDa, cell surface ligand from both neural cells and brain which binds this sequence. This binding protein does not share immunological identity with the B1 chain of integrin, and reduction does not alter its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Antibody to the 110-kDa protein stained cellular processes in vivo. Sequence analysis of the first 18 amino acids from the amino terminus yielded almost exact sequence identity with nucleolin, a major 110-kDa nucleolar phosphoprotein. Antibody to nucleolin, however, does not interact with the neural-derived, laminin-peptide-binding 110-kDa protein. The 110-kDa protein appears to be a ligand for a specific site on laminin.

摘要

层粘连蛋白是神经突生长的有效促进剂,并且已发现来自A链的一种19个氨基酸的合成肽PA22 - 2可促进突起形成。利用肽亲和色谱法,我们已从神经细胞和大脑中鉴定出一种与该序列结合的110 kDa细胞表面配体。这种结合蛋白与整合素的B1链不具有免疫同源性,并且还原作用不会改变其在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳中的迁移率。针对110 kDa蛋白的抗体在体内对细胞突起进行了染色。从氨基末端开始的前18个氨基酸的序列分析产生了与核仁素几乎完全相同的序列,核仁素是一种主要的110 kDa核仁磷蛋白。然而,针对核仁素的抗体并不与神经来源的、与层粘连蛋白肽结合的110 kDa蛋白相互作用。110 kDa蛋白似乎是层粘连蛋白上一个特定位点的配体。

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