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Carbonic anhydrase 12 mutation modulates membrane stability and volume regulation of aquaporin 5

Authors
 Soyoung Hwang  ;  Jung Yun Kang  ;  Min Jae Kim  ;  Dong Min Shin  ;  Jeong Hee Hong 
Citation
 Journal of Enzyme Inhibition and Medicinal Chemistry, Vol.34(1) : 179-188, 2019 
Journal Title
 Journal of Enzyme Inhibition and Medicinal Chemistry 
ISSN
 1475-6366 
Issue Date
2019
Keywords
Carbonic anhydrase 12 ; acidosis ; aquaporin 5 ; salivary glands ; volume regulation
Abstract
Patients carrying the carbonic anhydrase12 E143K mutation showed the dry mouth phenotype. The mechanism underlying the modulation of aquaporin 5 and function in the salivary glands by carbonic anhydrase12 remains unknown. In this study, we identified the mislocalised aquaporin 5 in the salivary glands carrying the E143K. The intracellular pH of E143K cells was more acidic than that of the cells carrying wild type. To evaluate the role of carbonic anhydrase12 on the volume regulation of aquaporin 5, the submandibular gland cells were subjected to hypotonic stimuli. E143K enhanced the extent of swelling of cells on hypotonicity. Aquaporin 5 modulates water influx through ion transporters to prevent osmotic imbalance. These results suggest that the carbonic anhydrase12 E143K, including acidification or inflammation, mediates volume dysregulation by the loss of aquaporin 5. Thus, carbonic anhydrase12 may determine sensible effects on the cellular osmotic regulation by modulating aquaporin 5.
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DOI
10.1080/14756366.2018.1540475
Appears in Collections:
2. College of Dentistry (치과대학) > Dept. of Oral Biology (구강생물학교실) > 1. Journal Papers
Yonsei Authors
신동민(Shin, Dong Min) ORCID logo https://orcid.org/0000-0001-6042-0435
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URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/167311
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