ID 109816
Title Transcription
アクアポリン5 シゼン ハッセイ イデンシ ヘンイ ノ ミズ チャネル キノウ ニ オヨボス エイキョウ
Title Alternative
Effects of a Naturally Occurring Mutation in Rat Aquaporin 5 on its Water Channel Functions
Author
Hosoi, Kazuo Department of Molecular Oral Physiology, Institute of Health Biosciences Graduate School of the University of Tokushima Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Keywords
アクアポリン
水チャネル
外分泌腺
遺伝子変異
Content Type
Journal Article
Description
The aquaporin (AQP) family in mammals is composed of 13 members (AQP0-12) of
water channel proteins. One of them, AQP5, is expressed in the various exocrine glands such as the lachrymal, parotid, and submandibular gland, and also in lung. We found the presence of G>A point mutation at position 308 in the rat AQP5 mRNA as well as the genome DNA. This mutation resulted in replacement of Gly103 with Asp103 in the AQP5 protein molecule, and led to various phenotypic alterations in the salivary gland. The point mutation localized in the 3rd trans-membrane domain, which is remote site from the water pore. As expected, the water permeability of the mutant molecule was almost same as that of the wild type molecule, indicating that the mutation does not affect the water permeability. In the submandibular gland, membrane expression of the mutant molecule was extremely reduced; and the secretion of saliva in the mutant rat was reduced also as compared to the wild-type animals. By confocal immunohistochemistry, an increased association of AQP5 and lysosomal markers, Lamp2 and/or cathepsin D was observed in the cytoplasmic area of acinar cells of mutant rats, implying the accelerated metabolism of the mutant molecule by the lysosomal system.
Journal Title
四国歯学会雑誌
ISSN
09146091
NCID
AN10050046
Publisher
四国歯学会
Volume
24
Issue
2
Start Page
51
End Page
57
Sort Key
51
Published Date
2012-01-31
EDB ID
FullText File
language
jpn
TextVersion
Publisher
departments
Oral Sciences