Cytokeratin 13 Contains O-Glycosidically Linked N-Acetylglucosamine Residues
نویسندگان
چکیده
منابع مشابه
Glycan-dependent signaling: O-linked N-acetylglucosamine.
The addition of O-linked N-acetylglucosamine (O-GlcNAc) to target proteins may serve as a signaling modification analogous to protein phosphorylation. Like phosphorylation, O-GlcNAc is a dynamic modification occurring in the nucleus and cytoplasm. Various analytical methods have been developed to detect O-GlcNAc and distinguish it from glycosylation in the endomembrane system. Many target molec...
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The complete structures of the oligosaccharides in a human X-type immunoglobulin light chain have been determined. Four glycopeptides were isolated by chromatography on Bio-Gel P-6 columns following digestion of the glycoprotein with pronase. The 0-glycosidically linked chains were also isolated as reduced oligosaccharides by treating the glycoprotein with alkaline borohydride. Analysis of the ...
متن کاملRole of O-linked N-acetylglucosamine modification in diabetic nephropathy.
Increased O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) is a known contributor to diabetes; however, its relevance in diabetic nephropathy (DN) is poorly elucidated. Here, we studied the process and enzymes of O-GlcNAcylation with a special emphasis on Akt-endothelial nitric oxide synthase (eNOS) and heat shock protein (HSP)72 signaling. Since tubular injury is the prominent si...
متن کاملAltering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function.
Mitochondrial impairment is commonly found in many diseases such as diabetes, cancer, and Alzheimer disease. We demonstrate that the enzymes responsible for the addition or removal of the O-GlcNAc modification, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), respectively, are critical regulators of mitochondrial function. Using a SILAC (stable isotope labeling of amino acids in cell culture)-...
متن کاملO-Linked N-Acetylglucosamine Cycling Regulates Mitotic Spindle Organization*
Any defects in the correct formation of the mitotic spindle will lead to chromosomal segregation errors, mitotic arrest, or aneuploidy. We demonstrate that O-linked N-acetylglucosamine (O-GlcNAc), a post-translational modification of serine and threonine residues in nuclear and cytoplasmic proteins, regulates spindle function. In O-GlcNAc transferase or O-GlcNAcase gain of function cells, the m...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)71636-0