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

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 prima...

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Bibliographic Details
Published in:Glycobiology (Oxford) 2004-03, Vol.14 (8), p.739-744
Main Author: Hara-Kuge, S.
Format: Article
Language:English
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Summary: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.
ISSN:1460-2423
0959-6658
1460-2423
DOI:10.1093/glycob/cwh082