Mouse fibroblasts null for the long isoform of β1,4-galactosyltransferase-I show defective cell-matrix interactions.
Mouse fibroblasts null for the long isoform of β1,4-galactosyltransferase-I show defective cell-matrix interactions.
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DOI：
10.1016/j.bbrc.2016.08.102
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发表时间：
2016-09-23
影响因子：
3.1
通讯作者：
Shur BD
中科院分区：
文献类型：
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作者：
Elder BH;Shur BD
β 1，4半乳糖基转移酶-I（GalT-I）表达为两种几乎相同的多肽，仅胞质结构域长度不同。较长的同种型已被认为是细胞外糖苷配体（如层粘连蛋白）的细胞表面受体。为了更严格地测试长GalT-I同种型在细胞与层粘连蛋白相互作用期间的功能，我们创建了多个独立的成纤维细胞系，其不能表达长同种型，但正常表达短GalT-I同种型，并且似乎具有正常的细胞内半乳糖基化。缺乏长GalT-I同种型的细胞不能在层粘连蛋白底物以及对照细胞上粘附和扩散，但保留与纤连蛋白的接近正常的相互作用，其不依赖于表面GalT-I功能。长GalT-I同种型的损失也导致肌动蛋白应力纤维的损失、局灶性粘连和外消旋GT3活化。
β1,4 Galactosyltransferase-I (GalT-I) is expressed as two nearly identical polypeptides that differ only in the length of their cytoplasmic domains. The longer isoform has been implicated as a cell surface receptor for extracellular glycoside ligands, such as laminin. To more stringently test the function of the long GalT-I isoform during cell interactions with laminin, we created multiple independent fibroblastic cell lines that fail to express the long isoform, but which express the short GalT-I isoform normally and appear to have normal intracellular galactosylation. Cells devoid of the long GalT-I isoform are unable to adhere and spread on laminin substrates as well as control cells, but retain near normal interactions with fibronectin, which do not rely upon surface GalT-I function. The loss of the long GalT-I isoform also leads to a loss of actin stress fibers, focal adhesions and rac GTPase activation.
DOI：
10.1083/jcb.107.5.1863
发表时间：
1988-11
期刊：
The Journal of cell biology
影响因子：
--
作者：
Runyan RB;Versalovic J;Shur BD
通讯作者：
Shur BD