Structure and Chromosomal Localization of a Human Water Channel (AQP3) Gene

Ishibashi, Keiichiro; Sasaki, Sei; Saito, Fumiko; Ikeuchi, Tatsuro; Marumo, Fumiaki

doi:10.1006/geno.1995.1055

Cited by 65 publications

(39 citation statements)

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“…AQPs play a pivotal role for normal gastrointestinal homeostasis, all from the secretion of saliva where AQP5 plays an important role [191][192][193], through the water-tight regulated stomach where AQP1, 3 and 4 play major roles in the secretion of gastric juices [189,[194][195][196] and the small intestine, where enterocytes immense bidirectional water transport where AQP1, 3, 7, 10 and 11 are expressed [189,195,197] to the ascending colon where primarily AQP1, 3, 7, 8 and 11 are present [198][199][200]. Several studies have displayed the importance of AQPs in faecal concentration/water absorption in the colon.…”

Section: Aquaporins In Gastrointestinal Homeostasis and Diarrhoeamentioning

confidence: 99%

Aquaporins in Infection and Inflammation

Holm¹

2016

Linköping University Medical Dissertations

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About the cover:The front cover displays a human, blood-derived macrophage stained for aquaporin 9.During the course of the research underlying this thesis, Angelika Holm was enrolled in Forum Scientium, a multidisciplinary doctoral programme at Linköping University Printed by LiU-Tryck, Linköping, Sweden, 2016 "Be brave, even if you're not, pretend to be. No one can tell the difference."To that young, awkward, tall girl who dared to dream of something else, something more:You did it. SUPERVISOR Elena VikströmDepartment of Clinical and Experimental Medicine Linköping University Linköping Sweden When cells of the innate immune system encounter pathogens they need to respond and prepare for migration and phagocytosis and do so through volume regulatory processes. The Gramnegative bacterium Pseudomonas aeruginosa utilizes a small molecule-based communication system, called quorum sensing (QS) to control the production of its virulence factors and biofilms. We found that P. aeruginosa with a complete QS system elicits a stronger phagocytic response in human blood-derived macrophages compared to its lasI-/rhlI-mutant lacking the production of the QS molecules N-butyryl-L-homoserine lactone (C4-HSL) and N-3-oxododecanoyl-L-homoserine lactone (3O-C12-HSL). Infection with P. aeruginosa further increases the expression of AQP9 and induces re-localisation of AQP9 to the front and trailing ends of macrophages. Moreover, the 3O-C12-HSL alone elevates the expression of AQP9, redistribute the water channel to the front and rear ends and increases the cell area and volume of macrophages. Both infection with the wild type P. aeruginosa and the treatment with 3O-C12-HSL change the nano-structural architecture of the AQP9 distribution in macrophages. ASSISTANT SUPERVISORS Karl-Eric MagnussonViruses use the intracellular machinery of the invaded cells to produce and assemble new viral bodies. Intracellular AQPs are localised in a membranes of cellular organelles to regulate their function and morphology. C3H10T1/2 fibroblasts transiently expressing green fluorescent protein (GFP)-AQP6 show a reduced expression of AQP6 after Hazara virus infection and an increased cell area. Overexpressing AQP6 in C3H10T1/2 cells reduces the infectivity of Hazara virus indicating that AQP6 expression has a protective role in virus infections.Ion and water channels in the epithelial cell lining tightly regulate the water homeostasis. In microscopic colitis (MC), patients suffer from severe watery diarrhoeas. For the first time, we have shown that the expression of AQP1, 8 and 11 and the sodium/hydrogen exchanger NHE1 are reduced in colonic biopsies from MC patients compared to healthy control individuals. Following treatment with the glucocorticoid budesonide the patients experienced a rapid recovery and we observed a restored or increased expression of the AQPs and NHE1 during treatment, suggesting a role for AQPs in the diarrhoeal mechanisms in MC.Taken together, this thesis provides new evidence on the importance of water homeostasis regulatio...

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Section: Aquaporins In Gastrointestinal Homeostasis and Diarrhoeamentioning

confidence: 99%

Aquaporins in Infection and Inflammation

Holm¹

2016

Linköping University Medical Dissertations

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“…Ec-CLPF (Weissenborn et al, 1992), Ec-AQPZ (Calamita et al, 1995), Cm-NOD26 (Fortin et a!., 1987), Os-rMIP1 (Liu et al, 1994), Na-U20490 (Newbigin, GenBank accession no. U20490), Hs-AQP1 (Preston and Agre, 1991), Hs-AQP2 (Deen et al, 1994), Hs-AQP3 (Ishibashi et al, 1995), Hs-AQP4 (Lu et al, 1996), and Hs-AQP5 .…”

Section: Nlml 1s the First Member Of The Third Subgroup Of Aquaporinsmentioning

confidence: 99%

The Major Intrinsic Protein Family of Arabidopsis Has 23 Members That Form Three Distinct Groups with Functional Aquaporins in Each Group

1997

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Aquaporins, proteins that enhance the permeability of biological membranes to water, are widely distributed i n living organisms.They are 26-to 29-kD proteins that belong to the major intrinsic protein (MIP) family of channels. By searching the Arabidopsis fbaliana expressed sequence tag database and by using the polymerase chain reaction with oligonucleotides to conserved plant aquaporin domains, we identified 23 expressed Arabidopsis MIP genes. Eight of these had been previously identified as active aquaporins, and two additional ones are now reported to have watertransport activity i n Xenopus laevis oocytes. One of these is highly expressed in suspension-cultured cells. O n a dendrogram these 23 MIP sequences cluster into three groups: the first group has 1 1 members and contains the plasma membrane aquaporins, the second group also has 11 members and contains the tonoplast aquaporins, and the third group has only a single member. This MIP protein, provisionally called At-NLM1, is most closely related to the Cm-NOD26 protein that is found i n the bacteroid membranes of soybean (Glycine max L.) nodules; At-NLM1 is an active aquaporin when expressed in oocytes. With a semiquantitative slot-blot analysis technique, we determined the expression levels of 22 MIP genes in the various organs. The quantitative polymerase chain reaction was used t o determine the effects of various stress treatments on the expression of NLMl.

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“…This sequence showed 96% identity to rat kidney AQP3 (16,28), 98% identity to human kidney AQP3 (29) and 99% to human kidney glycerol intrinsic protein (GLIP) (30) in their respective conserved regions. Furthermore, AQP3 mRNA expression in the different gastrointestinal sections was analyzed by Northern blot using the 420-bp RT-PCR product as a probe.…”

Section: Aqp3 Mrna Expressionmentioning

confidence: 99%

Functional characterization and localization of AQP3 in the human colon

Silberstein¹,

Kierbel²,

Amodeo³

et al. 1999

Braz J Med Biol Res

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Water channels or aquaporins (AQPs) have been identified in a large variety of tissues. Nevertheless, their role in the human gastrointestinal tract, where their action is essential for the reabsorption and secretion of water and electrolytes, is still unclear. The purpose of the present study was to investigate the structure and function of water channels expressed in the human colon. A cDNA fragment of about 420 bp with a 98% identity to human AQP3 was amplified from human stomach, small intestine and colon by reverse transcription polymerase chain reaction (RT-PCR) and a transcript of 2.2 kb was expressed more abundantly in colon than in jejunum, ileum and stomach as indicated by Northern blots. Expression of mRNA from the colon of adults and children but not from other gastrointestinal regions in Xenopus oocytes enhanced the osmotic water permeability, and the urea and glycerol transport in a manner sensitive to an antisense AQP3 oligonucleotide, indicating the presence of functional AQP3. Immunocytochemistry and immunofluorescence studies in human colon revealed that the AQP3 protein is restricted to the villus epithelial cells. The immunostaining within these cells was more intense in the apical than in the basolateral membranes. The presence of AQP3 in villus epithelial cells suggests that AQP3 is implicated in water absorption across human colonic surface cells.

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Structure and Chromosomal Localization of a Human Water Channel (AQP3) Gene

Cited by 65 publications

References 0 publications

Aquaporins in Infection and Inflammation

Aquaporins in Infection and Inflammation

The Major Intrinsic Protein Family of Arabidopsis Has 23 Members That Form Three Distinct Groups with Functional Aquaporins in Each Group

Functional characterization and localization of AQP3 in the human colon

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