Results 151 to 160 of about 1,085 (173)

The Cosmc connection to the Tn antigen in cancer [PDF]

open access: possibleCancer Biomarkers, 2014
The Tn antigen is a tumor-associated carbohydrate antigen that is not normally expressed in peripheral tissues or blood cells. Expression of this antigen, which is found in a majority of human carcinomas of all types, arises from a blockage in the normal O-glycosylation pathway in which glycans are extended from the common precursor GalNAcα1-O-Ser/Thr (
Tongzhong, Ju   +4 more
openaire   +2 more sources

Co-translational function of Cosmc, core 1 synthase specific molecular chaperone, revealed by a cell-free translation system [PDF]

open access: yesFEBS Letters, 2011
The core 1 structure of the mucin type O-glycan is synthesized by core 1 β1,3-galactosyltransferase (C1GalT). Core 1 synthase specific molecular chaperone (Cosmc), a molecular chaperone specific for C1GalT, is essential for the expression of functional ...
Tomomi Kubota   +2 more
exaly   +2 more sources

The Transmembrane Domain of the Molecular Chaperone Cosmc Directs Its Localization to the Endoplasmic Reticulum* [PDF]

open access: yesJournal of Biological Chemistry, 2011
The molecular basis for retention of integral membrane proteins in the endoplasmic reticulum (ER) is not well understood. We recently discovered a novel ER molecular chaperone termed Cosmc, which is essential for folding and normal activity of the Golgi enzyme T-synthase.
Tongzhong Ju   +2 more
exaly   +3 more sources

The Endoplasmic Reticulum Chaperone Cosmc Directly Promotes in Vitro Folding of T-synthase* [PDF]

open access: yesJournal of Biological Chemistry, 2010
The T-synthase is the key beta 3-galactosyltransferase essential for biosynthesis of core 1 O-glycans (Gal beta 1-3GalNAc alpha 1-Ser/Thr) in animal cell glycoproteins. Here we describe the novel ability of an endoplasmic reticulum-localized molecular chaperone termed Cosmc to specifically interact with partly denatured T-synthase in vitro to cause ...
Rajindra P Aryal   +2 more
exaly   +3 more sources

Identification of a Novel Protein Binding Motif within the T-synthase for the Molecular Chaperone Cosmc* [PDF]

open access: yesJournal of Biological Chemistry, 2014
Prior studies suggested that the core 1 β3-galactosyltransferase (T-synthase) is a specific client of the endoplasmic reticulum chaperone Cosmc, whose function is required for T-synthase folding, activity, and consequent synthesis of normal O-glycans in all vertebrate cells.
Rajindra P Aryal   +2 more
exaly   +3 more sources

Functional Assays for the Molecular Chaperone Cosmc

2010
Mucin type O-glycosylation involves sequential actions of several glycosyltransferases in the Golgi apparatus. Among those enzymes, a single gene product termed core 1 beta3-galactosyltransferase (T-synthase) in vertebrates is the key enzyme that converts the precursor Tn antigen GalNAcalpha1-Ser/Thr to the core 1 structure, Galbeta1-3GalNAcalpha1-Ser ...
Tongzhong, Ju, Richard D, Cummings
openaire   +2 more sources

Promoters of Human Cosmc and T-synthase Genes Are Similar in Structure, Yet Different in Epigenetic Regulation* [PDF]

open access: yesJournal of Biological Chemistry, 2015
The T-synthase (core 1 β3-galactosyltransferase) and its molecular chaperone Cosmc regulate the biosynthesis of mucin type O-glycans on glycoproteins, and evidence suggests that both T-synthase and Cosmc are transcriptionally suppressed in several human diseases, although the transcriptional regulation of these two genes is not understood.
Yujing Li   +2 more
exaly   +4 more sources

The Cosmc-mediated effects of neutrophil elastase on T antigen expression in BEAS-2B cells

Respiratory Physiology and Neurobiology, 2020
Mucin 5AC (MUC5AC) is a highly O-glycosylated mucin secreted by human bronchial epithelial cells during pulmonary inflammatory diseases. T antigen, a component of the MUC5AC glycans, is the product of the O-glycosylation transferase T-synthase and its chaperone Cosmc.
Victor P Kolosov, Juliy M Perelman
exaly   +3 more sources

C1GALT1C1 (COSMC) Mutations in Four Individuals with Tn+ Phenotype.

Blood, 2007
Abstract Tn is a cryptantigen located on O-linked oligosaccharides of cell membrane glycoproteins and is composed of N-acetylgalactosamine a -linked to serine or threonine of the protein backbone. Tn is expressed on hemopoietic cells of individuals with the rare idiopathic Tn syndrome, characterized by a variable pattern of Tn expression
Vanja Karamatic Crew   +5 more
openaire   +1 more source

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