期刊
FEBS LETTERS
卷 582, 期 3, 页码 439-444出版社
WILEY
DOI: 10.1016/j.febslet.2008.01.006
关键词
dystroglycan; muscular dystrophy; processing of protein; glycosylation; proprotein convertase
alpha-Dystroglycan (alpha-DG) plays a crucial role in maintaining the stability of muscle cell membrane. Although it has been shown that the N-terminal domain of alpha-DG (alpha-DG-N) is cleaved by a proprotein convertase,its physiological significance remains unclear. We show here that native alpha-DG-N is secreted by a wide variety of cultured cells into the culture media. The secreted alpha-DG-N was both N- and O-glycosylated. Finally, a small amount of alpha-DG-N was detectable in the normal human serum. These observations indicate that the cleavage of alpha-DG-N is a widespread event and suggest that the secreted alpha-DG-N might be transported via systemic circulation in vivo. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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