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Journal of Histochemistry and Cytochemistry, Vol. 51, 1057-1063, August 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Localization of VIP36 in the Post-Golgi Secretory Pathway Also of Rat Parotid Acinar Cells

Osamu Shimadaa, Sayuri Hara–Kugeb, Katsuko Yamashitab, Hisami Tosaka–Shimadaa, Li Yanchaoa, Li Einana, Saoko Atsumia, and Harunori Ishikawac
a Department of Anatomy, Yamanashi University School of Medicine, Yamanashi
b Department of Biochemistry, Sasaki Institute, Tokyo
c Department of Anatomy, Gunma University School of Medicine, Gunma, Japan

Correspondence to: Osamu Shimada, Dept. of Anatomy, Yamanashi U. School of Medicine, 1110 Tamaho-cho, Yamanashi 409-3898, Japan. E-mail: oshimada@swallow.res.yamanashi-med.ac.jp

VIP36 (36-kD vesicular integral membrane protein), originally purified from Madin–Darby canine kidney (MDCK) epithelial cells, belongs to a family of animal lectins and may act as a cargo receptor. To understand its role in secretory processes, we performed morphological analysis of the rat parotid gland. Immunoelectron microscopy provided evidence that endogenous VIP36 is localized in the trans-Golgi network, on immature granules, and on mature secretory granules in acinar cells. Double-staining immunofluorescence experiments confirmed that VIP36 and amylase co-localized in the apical regions of the acinar cells. This is the first study to demonstrate that endogenous VIP36 is involved in the post-Golgi secretory pathway, suggesting that VIP36 plays a role in trafficking and sorting of secretory and/or membrane proteins during granule formation.

(J Histochem Cytochem 51:1057–1063, 2003)

Key Words: VIP36, immunoelectron microscopy, parotid acinar cells, post-Golgi secretory pathway, animal lectin


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