Molecular characterization of human Aquaporin-7 gene and its chromosomal mapping

Ishibashi, Keiichiro; Yamauchi, Kozue; Kageyama, Yukio; Saito-Ohara, Fumiko; Ikeuchi, Tatsro; Marumo, Fumiaki; Sasaki, Sei

doi:10.1016/s0167-4781(98)00094-3

Cited by 64 publications

(53 citation statements)

References 13 publications

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“…Although Northern blot analysis of cardiac AQP expression was not performed in this study, others have reported Northern blot data consistent with the RT-PCR data here. This includes the presence of AQP-1 in human and rat hearts (9), AQP-4 in human (51) and mouse (27) hearts, AQP-7 in both human and rat hearts (11,13,20), and AQP-11 in mouse hearts (33). The species difference in AQP-8 transcript expression described here is supported by separate studies that show the presence of mRNA in mouse hearts (26) and the absence in human (17) and rat (12,18) hearts.…”

Section: Discussionsupporting

confidence: 61%

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Cardiac aquaporin expression in humans, rats, and mice

Butler¹,

Au²,

Yang³

et al. 2006

American Journal of Physiology-Heart and Circulatory Physiology

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Water accumulation in the heart is important in ischemia-reperfusion injury and operations performed by using cardiopulmonary bypass, with cardiac dysfunction associated with myocardial edema being the principal determinant of clinical outcome. As an initial step in determining the role of aquaporin (AQP) water channels in myocardial edema, we have assessed the myocardial expression of AQPs in humans, rats, and mice. RT-PCR revealed expression of AQP-1, -4, -6, -7, -8, and -11 transcripts in the mouse heart. AQP-1, -6, -7, and -11 mRNAs were found in the rat heart as well as low levels of AQP-4 and -9. Human hearts contained AQP-1, -3, -4, -5, -7, -9, -10, and -11 mRNAs. AQP-1 protein expression was confirmed by Western blot analysis in all three species. AQP-4 protein was detected in the mouse heart but not in the rat or human heart. To determine the potential functional consequences of myocardial AQP expression, water permeability was measured in plasma membrane vesicles from myocardial cells of wild-type versus various AQP knockout mice. Water permeability was reduced by AQP-1 knockout but not by AQP-4 or AQP-8 knockout. With the use of a model of isolated rat heart perfusion, it was found that osmotic and ischemic stresses are not associated with changes in AQP-1 or AQP-4 expression. These studies support a possible functional role of AQP-1 in myocardium but indicate that early adaptations to osmotic and ischemic stress do not involve transcriptional or posttranslational AQP-1 regulation. aquaporin knockout; cardiac myocyte; cardiopulmonary bypass OUR INTEREST IN CARDIAC AQUAPORINS (AQPs) stems from the recognition that myocardial edema is associated with a significant reduction in cardiac performance in a number of clinically important situations. Ischemia and reperfusion are associated with the development of myocardial edema, with expansion of both interstitial and cellular compartments. The resulting systolic and diastolic dysfunctions are the most important prognostic factors in patient survival after an acute ischemic event or "planned" ischemia, as occurs during cardiac surgery. Procedures involving cardiopulmonary bypass bring additional osmotic stress due to hemodilution and increased vascular permeability (32,40,42

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Section: Discussionsupporting

confidence: 61%

“…5), including AQP-1 expression in endothelium (9,35) and myocytes (1,38) of cardiac tissue. Human (20), rat (11,13), and mouse (34) hearts all contain AQP-7 transcript. Low levels of AQP-11 expression were seen by Western blot analysis in the mouse heart (33).…”

mentioning

confidence: 99%

Cardiac aquaporin expression in humans, rats, and mice

Butler¹,

Au²,

Yang³

et al. 2006

American Journal of Physiology-Heart and Circulatory Physiology

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“…D9S165 has been mapped between the markers D9S1788 and WI-5340, both of which reside in chromosome 9p13.3-p21.1 in the Whitehead YAC map. Thus the AQPap gene was assigned to chromosome 9p13.3-p21.1, close, but not identical, to the region described previously [26]. Computer analysis revealed both the AQPap and AQP3 genes were colocalized in a BAC clone (RP11-115015) found by a BLAST search, indicating their close localization to Chr9p13.3-p21.1.…”

Section: Chromosome Localization Of the Aqpap Genesupporting

confidence: 60%

Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation

Kondo¹,

Shimomura²,

Kishida³

et al. 2002

Eur J Biochem

104

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Aquaporin adipose (AQPap), which we identified from human adipose tissue, is a glycerol channel in adipocyte [Kishida et al. (2000) J. Biol. Chem. 275, 20896-20902]. In the current study, we determined the genomic structure of the human AQPap gene, and identified three AQPap-like genes that resembled ( 95%) AQPap, with little expression in human tissues. The AQPap promoter contained a putative peroxisome proliferator response element (PPRE) at )46 to )62, and a putative insulin response element (IRE) at )542/)536. Deletion of the PPRE abolished the pioglitazone-mediated induction of AQPap promoter activity in 3T3-L1 adipocytes. Deletion and single base pair substitution analysis of the IRE abolished the insulin-mediated suppression of the human AQPap gene. Analysis of AQPap sequence in human subjects revealed three missense mutations (R12C, V59L and G264V), and two silent mutations (A103A and G250G). The cRNA injection of the missense mutants into Xenopus oocytes revealed the absence of the activity to transport glycerol and water in the AQPap-G264V protein. In the subject homozygous for AQPap-G264V, exercise-induced increase in plasma glycerol was not observed in spite of the increased plasma noradrenaline. We suggest that AQPap is responsible for the increase of plasma glycerol during exercise in humans.

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“…12 Subsequently, other researchers found AQP7 expression in testis and renal proximal tubule cells. 13,14 The various AQP7 mouse models that were developed (for a phenotype overview, see Supplementary Table S1 online) showed a role for AQP7 in controlling fat and in glucose metabolism. [15][16][17] AQP7-knockout mice were shown to develop obesity and insulin resistance, with excess glycerol concentrations in the adipocytes.…”

Section: Introductionmentioning

confidence: 99%

Homozygosity for aquaporin 7 G264V in three unrelated children with hyperglyceroluria and a mild platelet secretion defect

Goubau

Jaeken

Levtchenko

et al. 2013

Genetics in Medicine

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Purpose: Aquaporin 7 (AQP7) belongs to the aquaglyceroporin family, which transports glycerol and water. AQP7-deficient mice develop obesity, insulin resistance, and hyperglyceroluria. However, AQP7's pathophysiologic role in humans is not yet known.methods: Three children with psychomotor retardation and hyperglyceroluria were screened for AQP7 mutations. The children were from unrelated families. Urine and plasma glycerol levels were measured using a three-step enzymatic approach. Platelet morphology and function were studied using electron microscopy, aggregations, and adenosine triphosphate (ATP) secretion tests. results:The index patients were homozygous for AQP7 G264V, which has previously been shown to inhibit transport of glycerol in Xenopus oocytes. We also detected a subclinical platelet secretion defect with reduced ATP secretion, and the absence of a secondary aggregation wave after epinephrine stimulation. Electron microscopy revealed round platelets with centrally located granules. Immunostaining showed AQP7 colocalization, with dense granules that seemed to be released after strong platelet activation. Healthy relatives of these patients, who were homozygous (not heterozygous) for G264V, also had hyperglyceroluria and platelet granule abnormalities. conclusion:The discovery of an association between urine glycerol loss and a platelet secretion defect is a novel one, and our findings imply the involvement of AQPs in platelet secretion. Additional studies are needed to define whether AQP7 G264V is also a risk factor for mental disability.

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Molecular characterization of human Aquaporin-7 gene and its chromosomal mapping

Cited by 64 publications

References 13 publications

Cardiac aquaporin expression in humans, rats, and mice

Cardiac aquaporin expression in humans, rats, and mice

Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation

Homozygosity for aquaporin 7 G264V in three unrelated children with hyperglyceroluria and a mild platelet secretion defect

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