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Glycobiology Advance Access originally published online on April 7, 2004
Glycobiology 2004 14(8):739-744; doi:10.1093/glycob/cwh082
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Glycobiology vol. 14 no. 8 © Oxford University Press 2004; all rights reserved.

The binding of VIP36 and {alpha}-amylase in the secretory vesicles via high-mannose type glycans

Sayuri Hara-Kuge2, Akira Seko2, Osamu Shimada3, Hisami Tosaka-Shimada3 and Katsuko Yamashita1,2

2 Department of Biochemistry, Sasaki Institute, 2-2 Kanda–Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan; and 3 Department of Anatomy, Yamanashi University School of Medicine, Yamanashi, Japan

Received on January 27, 2004; revised on March 14, 2004; accepted on March 17, 2004

Vesicular integral protein of 36 kDa (VIP36) is an intracellular lectin recognizing high-mannose type glycans and is highly expressed in salivary glands, especially the parotid gland, which secretes {alpha}-amylase in large quantities. Here immunoelectron microscopy demonstrated that VIP36 was primarily localized to secretory vesicles in the glandula parotis of the rat, where {alpha}-amylase also resided. A secretory vesicle fraction, prepared by Percoll density gradient centrifugation, contained both VIP36 and {alpha}-amylase. Moreover, {alpha}-amylase that was localized to these secretory vesicles contained high-mannose type glycans. In addition, VIP36 coprecipitated with {alpha}-amylase in an endo H treatment–sensitive manner. These results suggest that VIP36 is involved in the secretion of {alpha}-amylase in the rat parotid gland.

1 To whom correspondence should be addressed; e-mail: yamashita{at}sasaki.or.jp


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