کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5506726 | 1400302 | 2016 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mouse fibroblasts null for the long isoform of β1,4-galactosyltransferase-I show defective cell-matrix interactions
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: 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](/preview/png/5506726.png)
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 478, Issue 3, 23 September 2016, Pages 1248-1253
Journal: Biochemical and Biophysical Research Communications - Volume 478, Issue 3, 23 September 2016, Pages 1248-1253
نویسندگان
Brooke H. Elder, Barry D. Shur,