Binding of human syndecan to extracellular matrix proteins.
Binding of human syndecan to extracellular matrix proteins.
复制标题
人多聚糖与细胞外基质蛋白的结合。
DOI：
10.1016/s0021-9258(18)38239-5
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
M. Jalkanen
中科院分区：
文献类型：
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作者：
K. Elenius;M. Salmivirta;P. Inki;M. Mali;M. Jalkanen
我们从人乳腺细胞系（HBL-100）中分离出一种细胞表面蛋白聚糖。发现该蛋白聚糖是小鼠多配体聚糖的人等效物，因为（i）其具有与鼠多配体聚糖相同的生物化学性质，包括大小、电荷、浮力密度和糖胺聚糖组成，（ii）其核心蛋白具有与鼠多配体聚糖相同的大小，如通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳所研究的，和（iii）用多配体蛋白聚糖胞质结构域的抗肽抗体检测核心蛋白。当用小鼠多配体蛋白聚糖cDNA探测时，HBL-100细胞也显示出多配体蛋白聚糖mRNA的高表达。人类多配体蛋白聚糖的胞外域显示结合I型胶原纤维和纤连蛋白，但不层粘连蛋白，复制的结合特性的小鼠多配体蛋白聚糖。非常有趣的是，多配体蛋白聚糖不与玻连蛋白结合，玻连蛋白已知含有肝素结合结构域，并且是培养细胞的血清的主要粘附因子之一。已知多配体聚糖改变其糖胺聚糖组成，产生多配体聚糖的组织类型特异性多态形式（Sanderson，R.，和Bernfield，M.（1988）Proc. Natl. Acad. Sci.联合S.A. 85，9562-9566）。因此，该家族的成员可能代表结构相关的基质受体的集合，这些受体可能由于胞外域糖基化的变化而在它们的相互作用中不同。
We have isolated a cell surface proteoglycan from a human mammary cell line (HBL-100). This proteoglycan was found to be a human equivalent to mouse syndecan, because (i) it has identical biochemical properties with murine syndecan, including size, charge, buoyant density, and glycosaminoglycan composition, (ii) its core protein has identical size with murine syndecan as studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and (iii) the core protein is detected with anti-peptide antibody for the cytoplasmic domain of syndecan. HBL-100 cells also showed high expression of syndecan mRNAs, when probed with mouse syndecan cDNA. The ectodomain of the human syndecan revealed binding to type I collagen fibrils and fibronectin but not to laminin, duplicating the binding properties of murine syndecan. Very interestingly, syndecan did not bind to vitronectin, which is known to contain a heparin binding domain and is one of the major adhesive factors of serum for cultured cells. Syndecans are known to change their glycosaminoglycan composition yielding tissue-type specific polymorphic forms of syndecan (Sanderson, R., and Bernfield, M. (1988) Proc. Natl. Acad. Sci. U. S.A. 85, 9562-9566). The members of this family may thus represent a collection of structurally related matrix receptors that could differ in their interactions due to variation of the ectodomain glycosylation.