The binding of VIP36 and alpha-amylase in the secretory vesicles via high-mannose type glycans |
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Authors: | Hara-Kuge Sayuri Seko Akira Shimada Osamu Tosaka-Shimada Hisami Yamashita Katsuko |
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Affiliation: | Department of Biochemistry, Sasaki Institute, 2-2 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan. |
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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 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. |
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Keywords: | /math/alpha.gif" ALT=" {alpha}" BORDER=" 0" >-amylase / high mannose / salivary glands / secretion / VIP36 |
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