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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promotes Its Transition Through the Endoplasmic Reticulum

Author(s): Claus-Jurgen Scholz, Georg Sauer and Helmut Deissler

Volume 16, Issue 10, 2009

Page: [1244 - 1248] Pages: 5

DOI: 10.2174/092986609789071234

Price: $65

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


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