Abstract
We showed that Tspan-1, a tetraspanin overexpressed in many human cancers, harbours oligosaccharides at all four potential N-glycosylation sites. Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates. Glycosylation seemed to be required for correct folding and subsequent transition through the endoplasmic reticulum.
Keywords: EGFP fusion proteins, ovarian carcinoma cells, glycosylation, Tetraspanins
Protein & Peptide Letters
Title: Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promotes Its Transition Through the Endoplasmic Reticulum
Volume: 16 Issue: 10
Author(s): Claus-Jurgen Scholz, Georg Sauer and Helmut Deissler
Affiliation:
Keywords: EGFP fusion proteins, ovarian carcinoma cells, glycosylation, Tetraspanins
Abstract: We showed that Tspan-1, a tetraspanin overexpressed in many human cancers, harbours oligosaccharides at all four potential N-glycosylation sites. Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates. Glycosylation seemed to be required for correct folding and subsequent transition through the endoplasmic reticulum.
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Cite this article as:
Scholz Claus-Jurgen, Sauer Georg and Deissler Helmut, Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promotes Its Transition Through the Endoplasmic Reticulum, Protein & Peptide Letters 2009; 16 (10) . https://dx.doi.org/10.2174/092986609789071234
DOI https://dx.doi.org/10.2174/092986609789071234 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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