The Arabidopsis thaliana elongator complex subunit 2 epigenetically affects root development.
Jinan, China. In J Exp Bot, Aug 2015
The key transcription factors responsible for maintaining root stem cell and QC identity, such as AP2 transcription factors PLT1 (PLETHORA1) and PLT2 (PLETHORA2), GRAS transcription factors such as SCR (SCARECROW) and SHR (SHORT ROOT) and WUSCHEL-RELATED HOMEOBOX5 transcription factor WOX5, were all strongly down-regulated in the mutant.
The Cosmc connection to the Tn antigen in cancer.
Atlanta, United States. In Cancer Biomark, 2014
This precursor is generated in the Golgi apparatus on newly synthesized glycoproteins by a family of polypeptide α-N-acetylgalactosaminyltransferases (ppGalNAcTs) and then extended to the common core 1 O-glycan Galβ1-3GalNAcα1-O-Ser/Thr (T antigen) by a single enzyme termed the T-synthase (core 1 β3-galactosyltransferase or C1GalT).
Tn and sialyl-Tn antigens, aberrant O-glycomics as human disease markers.
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.
Pathogenetic significance of aberrant glycosylation of IgA1 in IgA nephropathy.
Niigata, Japan. In Clin Exp Nephrol, 2008
Although genes encoding enzymes involved in the O-glycosylation process, such as C1GALT1, have been reported to be responsible for susceptibility to IgAN, recent evidence suggests that the abnormality is restricted to a small fraction of B cell populations and arises from dysregulated IgA1 production and secretion in mucosal immune system.
Protein glycosylation: chaperone mutation in Tn syndrome.
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
Pathogenesis of IgA nephropathy.
Leicester, United Kingdom. In Ann Med Interne (paris), 1999
This reduced galactosylation may be due to a functional defect in plasma cell beta 1,3-galactosyltransferase. Altered hinge region glycosylation may alter IgA1 structure, modifying interactions with matrix proteins, IgA receptors and complement, and therefore influence mesangial deposition and subsequent injury through mechanisms other than classical antigen-antibody reactions.