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Glycobiology Advance Access published online on April 7, 2004
Glycobiology, doi:10.1093/glycob/cwh082
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Received January 27, 2004
Revised March 14, 2004
Accepted March 17, 2004

ORIGINAL ARTICLES

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

Sayuri Hara-Kuge 1, Akira Seko 1, Osamu Shimada 2, Hisami Tosaka-Shimada 2, Katsuko Yamashita 1*

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

* To whom correspondence should be addressed. E-mail: yamashita{at}sasaki.or.jp.


  Abstract

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 co-precipitated 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.

Key words: VIP36, {alpha}-amylase, salivary glands, high mannose, secretion


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