کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9882206 | 1536547 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cys351 and Cys361 of the Na+/glucose cotransporter are important for both function and cell-surface expression
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Here, we identify Cys351 and Cys361 as novel residues critical for the function and plasma membrane targeting of the Na+/glucose transporter-1 (SGLT1). HEK-293 cells expressing the C351A and C361A mutants showed no detectable Na+-coupled uptake for α-methyl glucoside (AMG). Cell-surface biotinylation and Western blot revealed that the two mutants were overexpressed in 293 cells; however, none of them exhibited normal cell-surface expression. When reconstituted in proteoliposomes, mutant SGLT1s demonstrated significantly lower affinity for AMG compared with the wild-type transporter. Incubation with the reducing agent dithiothreitol did not alter the catalytic activity of wild-type protein, but surprisingly, it nearly restored the ability of SGLT1-C351A and -C361A to bind and translocate AMG. Thus, the C351A and C361A mutations might cause a global reorganization of the disulfide bonds of SGLT1. Furthermore, we showed that a double mutation (C351A/C361A) restored the cell-surface expression of the single C-to-A mutants (C351A and C361A).
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 438, Issue 1, 1 June 2005, Pages 63-69
Journal: Archives of Biochemistry and Biophysics - Volume 438, Issue 1, 1 June 2005, Pages 63-69
نویسندگان
Xiaobing Xia, Gang Wang, Yanchun Peng, Jimmy Jen,