کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8326343 | 1539972 | 2007 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Requirement of N-glycosylation for the secretion of recombinant extracellular domain of human Fas in HeLa cells
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کلمات کلیدی
Helix pomatiaMAASNAWGAConAPNAFASGlcNAcSambucus nigra agglutininPHAConcanavalin AMaackia amurensis agglutinin - Maackia amurensis آگلوتیینینpeanut agglutinin - آگلوتینین بادام زمینیBenzyl - بنزیلApoptosis - خزان یاختهایHeLa cells - سلول های هلاMass spectrometry - طیف سنجی جرمیMALDI - مالدیMannose - مانوزMan - مردN-acetylglucosamine - نیتستیگلوکوزامینGal - گالGalactose - گالاکتوزمی glycosyltransferases - گلیکوزیلتransferasesGlycosylation - گلیکوزیله شدنGlycoprotein - گلیکوپروتئینWheat germ agglutinin - گیاه گندم آگلوتیینینmatrix-assisted laser desorption ionization - یونیزاسیون لیزر جذب ماتریس
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Apoptosis has been shown to be associated with altered glycosylation patterns and biosynthesis of glycoproteins. A major cell surface receptor involved in the induction of apoptosis is Fas that is activated by binding Fas ligand but can also be activated by binding anti-Fas antibody. In order to determine whether the Fas receptor is glycosylated, the extracellular domain of human Fas (shFas) was expressed as a cleavable fusion protein (shFas-Fc) in HeLa cells. These cells were shown to express activities of glycosyltransferases involved in N- and O-glycan biosynthesis. The secreted shFas-Fc was shown to be a glycoprotein with heterogeneous glycan chains. MALDI mass spectrometry revealed a disperse molecular weight of shFas with an average of 23.4Â kDa. Western blots of shFas-Fc secreted from tunicamycin treated transfected HeLa cells showed that only N-glycosylated glycoforms were secreted, while the unglycosylated shFas-Fc remained intracellular. The results suggest that both N-glycosylation sites of the extracellular domain of Fas are occupied with large N-glycans that play a role in the expression of the glycoprotein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 39, Issue 9, 2007, Pages 1625-1636
Journal: The International Journal of Biochemistry & Cell Biology - Volume 39, Issue 9, 2007, Pages 1625-1636
نویسندگان
Yi Li, Xiaojing Yang, Alana H.T. Nguyen, Inka Brockhausen,