Glycobiology Advance Access originally published online on November 3, 2004
Glycobiology 2005 15(4):383-392; doi:10.1093/glycob/cwi012
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Glycobiology vol. 15 no. 4 © Oxford University Press 2004; all rights reserved.
Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats
2 Department of Biochemistry and Molecular Biology in Disease, Atomic Bomb Disease Institute, Nagasaki University Graduate School of Biomedical Sciences, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan; 3 CREST, JST Kawaguchi 332-1102, Japan; 4 RIKEN (Institute of Physical and Chemical Research), Saitama 351-0198, Japan; 5 Third Department of Internal Medicine, Nagasaki University Graduate School of Biomedical Sciences, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan; 6 Department of Molecular Pathology, Atomic Bomb Disease Institute, Nagasaki University Graduate School of Biomedical Sciences, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan
1 To whom correspondence should be addressed; e-mail: y-ihara{at}net.nagasaki-u.ac.jp
Received on October 20, 2004; revised on November 1, 2004; accepted on November 2, 2004
C-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications.
Key words: C-mannosylation / diabetes / hyperglycemia / mannosyltransferase / thrombospondin
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