Endogenous lectin from terminally differentiated epidermal cells.
Endogenous lectin from terminally differentiated epidermal cells.
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来自终末分化表皮细胞的内源性凝集素。
DOI：
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
S. J. Chen
中科院分区：
文献类型：
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作者：
M. Brysk;S. Rajaraman;P. Penn;S. J. Chen
我们从人角质层中分离出一种伴刀豆球蛋白A（Con-A）结合糖蛋白，通过非离子去污剂提取、凝集素亲和层析和制备型凝胶电泳。该糖蛋白在十二烷基硫酸钠凝胶电泳中以40千道尔顿的单一条带迁移，有或没有2-巯基乙醇存在。通过等电聚焦显示，其在pH 5.6和7.6之间具有不均匀分布。该糖蛋白富含组氨酸（10.4%），但与其他富含组氨酸的蛋白质（表皮聚丝蛋白和来自血清的富含组氨酸的糖蛋白）不同。不与L-岩藻糖或α-D-半乳糖特异性凝集素结合。我们制备了一种单特异性多克隆抗体的40千道尔顿糖蛋白，在超微结构水平上，它cytoimmunolocalizes专门角质层的膜。糖蛋白的一个独特特征是它是一种内源性凝集素：它能凝集胰蛋白酶化和谷氨酰胺固定的兔红细胞。发现氨基糖对血凝的抑制作用最大，糖浓度低至10（-5）mM。在细胞表面结合的这种高亲和力表明，这种糖蛋白是一种主要的碳水化合物结合交联分子，将角质层中相邻的角质细胞结合在一起。我们推测这种凝集素在角质层的粘附和脱屑中起作用。
We isolated a concanavalin A (Con-A)-binding glycoprotein from human stratum corneum by nonionic detergent extraction, lectin affinity chromatography, and preparative gel electrophoresis. This glycoprotein migrates as a single band at 40 kilodaltons at sodium-dodecyl-sulfate gel electrophoresis with or without the presence of 2-mercaptoethanol. It was shown to have a heterogeneous distribution between pH 5.6 and 7.6 by isoelectric focusing. The glycoprotein is histidine rich (10.4%) but is distinct from other histidine-rich proteins (epidermal filaggrin and the histidine-rich glycoprotein from serum). It does not bind to lectins specific for L-fucose or alpha-D-galactose. We prepared a monospecific polyclonal antibody to the 40-kilodalton glycoprotein; at the ultrastructural level, it cytoimmunolocalizes exclusively to the membranes of the stratum corneum. A unique feature of the glycoprotein is that it is an endogenous lectin: it hemagglutinates trypsinized and gluteraldehyde-fixed rabbit erythrocytes. The inhibition of its hemagglutination was found to be greatest with amino sugars, down to a saccharide concentration of 10(-5) mM. Such a high affinity of binding at the cell surface suggests that this glycoprotein is a major carbohydrate-binding, cross-linking molecule that holds adjacent corneocytes together in the stratum corneum. We hypothesize that this lectin plays a role in the adhesion and desquamation of the stratum corneum.
影响因子：
6.5
作者：
ELIAS, PM
通讯作者：
ELIAS, PM