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C1GALT1-specific chaperone 1

Cosmc, C1GALT1C1
This gene encodes a type II transmembrane protein that is similar to the core 1 beta1,3-galactosyltransferase 1, which catalyzes the synthesis of the core-1 structure, also known as Thomsen-Friedenreich antigen, on O-linked glycans. This gene product lacks the galactosyltransferase activity itself, but instead acts as a molecular chaperone required for the folding, stability and full activity of the core 1 beta1,3-galactosyltransferase 1. Mutations in this gene have been associated with Tn syndrome. Alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Dec 2009] (from NCBI)
Top mentioned proteins: T-synthase, IgA, CAN, IgA1, CD45
Papers on Cosmc
Increased miR-374b promotes cell proliferation and the production of aberrant glycosylated IgA1 in B cells of IgA nephropathy.
Liu et al., Nanjing, China. In Febs Lett, Jan 2016
Here we report that expression of phosphatase and tensin homolog (PTEN) and Cosmc is decreased in B cells, and correlates with B cell number and the aberrant glycosylation of IgA1 in IgAN.
Promoters of Human Cosmc and T-synthase Genes Are Similar in Structure, Yet Different in Epigenetic Regulation.
Ju et al., Amsterdam, Netherlands. In J Biol Chem, Aug 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.
Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.
Reis et al., Copenhagen, Denmark. In Mol Cell Proteomics, Jun 2015
Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
COSMC knockdown mediated aberrant O-glycosylation promotes oncogenic properties in pancreatic cancer.
Wolters-Eisfeld et al., Hamburg, Germany. In Mol Cancer, 2014
Since the role of Tn antigen expression in PDAC is insufficiently understood we analyzed the impact of COSMC mediated Tn antigen expression in two human PDAC cell lines on cellular oncogenic properties.
The Breast Cancer-Associated Glycoforms of MUC1, MUC1-Tn and sialyl-Tn, Are Expressed in COSMC Wild-Type Cells and Bind the C-Type Lectin MGL.
Burchell et al., London, United Kingdom. In Plos One, 2014
The presence of active T synthase suggests that loss of the private chaperone for T synthase, COSMC, does not explain the expression of Tn and STn in breast cancer cells.
DNA methylation in Cosmc promoter region and aberrantly glycosylated IgA1 associated with pediatric IgA nephropathy.
Shen et al., Beijing, China. In Plos One, 2014
The expression of the specific molecular chaperone of core1ß1, 3galactosyl transferase (Cosmc) is known to be reduced in IgAN.
Aberrant Cosmc genes result in Tn antigen expression in human colorectal carcinoma cell line HT-29.
Hu et al., Yantai, China. In Int J Clin Exp Pathol, 2014
The Tn antigen, which arises from mutation in the Cosmc gene is one of the most common tumor associated carbohydrate antigens.
Capsaicin induces high expression of BAFF and aberrantly glycosylated IgA1 of tonsillar mononuclear cells in IgA nephropathy patients.
Peng et al., China. In Hum Immunol, 2014
RESULTS: In the absence and presence of capsaicin, the BAFF expression and IgA1 secretion were higher in IgAN patients than that in non-IgAN patients, meanwhile, the gene expression of C1GALT1 and Cosmc and IgA1 O-glycosylation level were significantly lower.
The Cosmc connection to the Tn antigen in cancer.
Cummings et al., Atlanta, United States. In Cancer Biomark, 2014
Formation of the active form of the T-synthase requires a unique molecular chaperone termed Cosmc, encoded by Cosmc on the X-chromosome (Xq24 in humans, Xc3 in mice).
Accounting for eXentricities: analysis of the X chromosome in GWAS reveals X-linked genes implicated in autoimmune diseases.
Keinan et al., Ithaca, United States. In Plos One, 2013
(3) We replicated a previous association of FOXP3, a transcription factor that regulates T-cell development and function, with vitiligo; and (4) we discovered that C1GALT1C1 exhibits sex-specific effect on disease risk in both IBDs.
Tn and sialyl-Tn antigens, aberrant O-glycomics as human disease markers.
Cummings et al., Atlanta, United States. In Proteomics Clin Appl, 2013
The major pathological mechanism for expression of the Tn and STn antigens is compromised T-synthase activity, resulting from alteration of the X-linked gene that encodes for Cosmc, a molecular chaperone specifically required for the correct folding of T-synthase to form active enzyme.
Tight complex formation between Cosmc chaperone and its specific client non-native T-synthase leads to enzyme activity and client-driven dissociation.
Cummings et al., Atlanta, United States. In J Biol Chem, 2012
Results show that soluble Cosmc directly interacts in a specific manner with denatured, but not native, T-synthase to form a noncovalent and reversible complex that results in the acquisition of T-synthase catalytic activity.
[Effect of methylation modification on the expression of Cosmc gene in peripheral B lymphocyte of IgA nephropathy patients].
Ma et al., Chengdu, China. In Sichuan Da Xue Xue Bao Yi Xue Ban, 2011
The mRNA expression level of Cosmc gene in IgA nephropathy patients was significantly lower than that of controls. De-methylation modification up regulated the Cosmc gene expression significantly.
Co-translational function of Cosmc, core 1 synthase specific molecular chaperone, revealed by a cell-free translation system.
Narimatsu et al., Tsukuba, Japan. In Febs Lett, 2011
Results indicate that Cosmc mediates the co-translational activation of C1GalT and that it may prevent the unfavorable aggregation of C1GalT.
The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum.
Cummings et al., Atlanta, United States. In J Biol Chem, 2011
The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum
The Tn antigen-structural simplicity and biological complexity.
Cummings et al., Atlanta, United States. In Angew Chem Int Ed Engl, 2011
Expression of active T-synthase is uniquely dependent on the molecular chaperone Cosmc, which is encoded by a gene on the X chromosome.
Abnormalities of glycogenes in tonsillar lymphocytes in IgA nephropathy.
Makino et al., Okayama, Japan. In Adv Otorhinolaryngol, 2010
Gene expression of β1,3-galactosyltransferase (β3GalT), Cosmc, UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyl-transferase 2, were significantly down regulated in tonsillar CD19-positive B lymphocytes from IgAN patients compared to control as determined by real-time RT-PCR.
Cosmc is an essential chaperone for correct protein O-glycosylation.
Cummings et al., Atlanta, United States. In Proc Natl Acad Sci U S A, 2010
Cosmc is an essential chaperone for correct protein O-glycosylation.
A mutant chaperone converts a wild-type protein into a tumor-specific antigen.
Schreiber et al., Chicago, United States. In Science, 2006
a somatic mutation in the chaperone gene Cosmc abolished function of a glycosyltransferase, disrupting O-glycan Core 1 synthesis & creating a tumor-specific glycopeptidic neo-epitope consisting of a monosaccharide and a specific wild-type protein sequence
Protein glycosylation: chaperone mutation in Tn syndrome.
Cummings et al., Oklahoma City, United States. In Nature, 2005
Tn syndrome is associated with a somatic mutation in Cosmc, a gene on the X chromosome that encodes a molecular 'chaperone' that is required for the proper folding and hence full activity of T-synthase
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