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FEBS Lett. 2008 Feb 6;582(3):439-44. doi: 10.1016/j.febslet.2008.01.006. Epub 2008 Jan 15.

Processing and secretion of the N-terminal domain of alpha-dystroglycan in cell culture media.

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  • 1Department of Neurology and Neuroscience, Teikyo University School of Medicine, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan.


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.

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