| Literature DB >> 28914590 |
Hiroshi Gomi1, Hiromi Osawa1, Rie Uno1, Tadashi Yasui1, Masahiro Hosaka2, Seiji Torii3, Azuma Tsukise1.
Abstract
The comparative structure and expression of salivary components and vesicular transport proteins in the canine major salivary glands were investigated. Histochemical analysis revealed that the morphology of the five major salivary glands-parotid, submandibular, polystomatic sublingual, monostomatic sublingual, and zygomatic glands-was greatly diverse. Immunoblot analysis revealed that expression levels of α-amylase and antimicrobial proteins, such as lysozyme, lactoperoxidase, and lactoferrin, differed among the different glands. Similarly, Rab proteins (Rab3d, Rab11a, Rab11b, Rab27a, and Rab27b) and soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) proteins VAMP4, VAMP8, syntaxin-2, syntaxin-3, syntaxin-4, and syntaxin-6 were expressed at various levels in individual glands. mmunohistochemistry of Rab3d, Rab11b, Rab27b, VAMP4, VAMP8, syntaxin-4, and syntaxin-6 revealed their predominant expression in serous acinar cells, demilunes, and ductal cells. The VAMP4/syntaxin-6 SNARE complex, which is thought to be involved in the maturation of secretory granules in the Golgi field, was found more predominantly in the monostomatic sublingual gland than in the parotid gland. These results suggest that protein expression profiles in canine salivary glands differ among individual glands and reflect the properties of their specialized functions.Entities:
Keywords: Rab protein; SNARE complex; VAMP4; dog; salivary glands; secretory pathway; syntaxin-6; zymogen granules
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Year: 2017 PMID: 28914590 PMCID: PMC5665109 DOI: 10.1369/0022155417732527
Source DB: PubMed Journal: J Histochem Cytochem ISSN: 0022-1554 Impact factor: 2.479