Cloning and characterization of porcine aquaporin 1 water channel expressed extensively in gastrointestinal system

World Journal of Gastroenterology : WJG
Shun-Ying JinTong-Hui Ma

Abstract

To clone and characterize the porcine aquaporins (AQPs) in the gastrointestinal system. A PCR-based cloning strategy and RACE were used to clone full-length AQP coding sequence from reversely transcribed pig liver cDNA. Stopped-flow light scattering and a YFP-based fluorescence method were used to measure the osmotic water permeability of erythrocytes and the stably transfected CHO cells. RT-PCR, Northern blot, and immunohistochemistry were used to determine the gastrointestinal expression and localization of cloned AQPs. Protein expression in transfected cells and red blood cells was analyzed by Western blot. An 813 bp cDNA encoding a 271 amino acid porcine aquaporin (designated pAQP1) was cloned from liver mRNA (pAQP1 has a 93% identity with human AQP1 and contains two NPA motifs conserved in AQP family, one consensus sequence for N-linked glycosylation, and one mercury-sensitive site at cysteine 191). RT-PCR analysis revealed extensive expression of pAQP1 mRNA in porcine digestive glands and gut. Northern blot showed a single 3.0 kb transcript in selected digestive organs. pAQP1 protein was localized at central lacteals of the small intestine, microvessles of salivary glands, as well as epithelium of intrahepatic bile ducts ...Continue Reading

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Citations

Feb 20, 2008·Expert Review of Proteomics·Fulvio MagniMarina Pitto
Jan 4, 2008·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Demetrio RaldúaJoan Cerdà
Sep 3, 2016·International Journal of Molecular Sciences·Cui ZhuZongyong Jiang
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Jul 30, 2016·International Journal of Molecular Sciences·Alessandra PelagalliRosaria Meli
Apr 4, 2021·Journal of Animal Physiology and Animal Nutrition·Hao LvAnshan Shan
Feb 6, 2008·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Xiaofeng LiZaiqing Yang

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