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

被引:21
作者
Hara-Kuge, S
Seko, A
Shimada, O
Tosaka-Shimada, H
Yamashita, K
机构
[1] Sasaki Inst, Dept Biochem, Chiyoda Ku, Tokyo 1010062, Japan
[2] Yamanashi Univ, Sch Med, Dept Anat, Yamanashi, Japan
关键词
alpha-amylase; high mannose; salivary glands; secretion; VIP36;
D O I
10.1093/glycob/cwh082
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:739 / 744
页数:6
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