The role of mammalian superaquaporins inside the cell

Ishibashi, Keiichiro; Tanaka, Yasuko; Morishita, Yoshiyuki

doi:10.1016/j.bbagen.2013.10.039

Cited by 124 publications

(76 citation statements)

References 44 publications

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“…In particular, the liver strongly expresses at least six AQPs (AQP1, 3, 7, 8, 9, and 11) [22,39,41,57]. Immunohistochemical studies revealed the expression of AQPs in different hepatic cell types, such as in cholangiocytes (AQP1 and AQP7), endothelial cells (AQP1), Kupffer cells (AQP3), and hepatocytes, (AQP7, 8, and 9) [22].…”

Section: Aqp Structure and Distribution In Gutmentioning

confidence: 99%

“…Recently, Ishibashi et al [39] reviewed mammalian superaquaporins (AQP11 and AQP12), focusing on their roles, which are only speculated by the phenotypes of their null mutants. For example, the water transport through the superaquaporin inside the cell will be important for the cell organelle function; the facilitated vesicle-to-plasma membrane fusion will be controlled by water transport through vesicular AQPs, as suggested by AQP12 null mice [40].…”

Section: Aqp Structure and Distribution In Gutmentioning

confidence: 99%

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Aquaporins in Health and Disease: An Overview Focusing on the Gut of Different Species

Pelagalli

Squillacioti

Mirabella

et al. 2016

IJMS

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Aquaporins (AQPs) play a pivotal role in gut homeostasis since their distribution and function is modulated both in physiological and in pathophysiological conditions. The transport of water and solutes through gut epithelia is essential for osmoregulation and digestive and absorptive functions. This passage is regulated by different AQP isoforms and characterized by their peculiar distribution in the gastrointestinal tract. To date, AQP localization has been identified in the gut and associated organs of several mammalian species by different techniques (immunohistochemical, western blotting, and RT-PCR). The present review describes the modulation of AQP expression, distribution, and function in gut pathophysiology. At the same time, the comparative description of AQP in animal species sheds light on the full range of AQP functions and the screening of their activity as transport modulators, diagnostic biomarkers, and drug targets. Moreover, the phenotype of knockout mice for several AQPs and their compensatory role and the use of specific AQP inhibitors have been also reviewed. The reported data could be useful to design future research in both basic and clinical fields.

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Section: Aqp Structure and Distribution In Gutmentioning

confidence: 99%

Section: Aqp Structure and Distribution In Gutmentioning

confidence: 99%

Aquaporins in Health and Disease: An Overview Focusing on the Gut of Different Species

Pelagalli

Squillacioti

Mirabella

et al. 2016

IJMS

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“…The AQP-s are divided into three families based on functionality: one family including AQP-1, -2, -4, -5 and -8, which selectively transport water; another including AQP-3, -7, -9 and -10, which transport both water and glycerol (aquaglyceroporins), and possibly other small solutes 12 and finally, the subfamily of subcellular AQPs or super-aquaporins, which includes AQP-11 and -12 13 . Aquaglyceroporins have been described in fat tissue, suggesting involvement in glycerol export during lipolysis, an important and novel function for these polypeptides 14 .…”

Section: Introductionmentioning

confidence: 99%

Membrane Stress During Thawing Elicits Redistribution of Aquaporin 7 But Not of Aquaporin 9 in Boar Spermatozoa

Vicente-Carrillo

Ekwall

Álvarez‐Rodríguez

et al. 2016

Reprod Domestic Animals

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Freezing of boar spermatozoa includes the cryoprotectant glycerol, but renders low cryosurvival, owing to major changes in osmolarity during freezing/thawing. We hypothesize that aquaglyceroporins (AQPs)-7 and -9 adapt their membrane domain location to these osmotic challenges, thus maintaining sperm homeostasis. Western blotting (WB) and immunocytochemistry (ICC) at light-and electron microscope levels with several commercial primary antibodies explored AQP-location on cauda epididymal and ejaculated spermatozoa (from different fractions of the ejaculate); un-processed, extended, chilled and frozen-thawed.Although differences in WB-and ICC-labelling were seen among antibodies, AQP-7 was conspicuously located over the entire tail and cytoplasmic droplet in caudal spermatozoa, being restricted to the mid-piece and principal piece domains in ejaculated spermatozoa.AQP-9 was mainly localized over the sperm head both in caudal and ejaculated spermatozoa.While unaffected by chilling (+5ºC), freezing and thawing of ejaculated spermatozoa clearly relocated the head labelling of AQP-7-, but not that of AQP-9. In vitro mimicking of cell membrane expansion during quick thawing maintained the localization of AQP-9 but relocated AQP-7 towards the acrosome. AQP-7 but not AQP-9 appears as a relevant marker for non-empirical studies of sperm handling.

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“…So far, thirteen AQPs have been cloned in mammals. They are classified into essentially permeable to water, permeable to water but also to glycerol, urea, and small solutes and unorthodox AQPs with highly variable NPA motifs (Ishibashi et al, 2014). Different AQPs have specific tissue distribution and execute particular physiological function.…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemical Study of Aquaporin 1 and 2 in the Hepatobiliary System of Qinghai Lizard ( Phrynocephalus vlangalii )

Zhang²

2019

Int. J. Morphol.

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AN, F. & ZHANG, Y.Immunohistochemical study of aquaporin 1 and 2 in the hepatobiliary system of Qinghai lizard (Phrynocephalus vlangalii). Int. J. Morphol., 37(2):706-711, 2019. SUMMARY:A serous membrane covering the liver and the hepatic parenchyma, consists of hepatocytes, arteries, veins, hepatic sinusoids and biliary ductuli. There are erythrocytes, thrombocytes, melanin particles and Kupffer cell in the hepatic sinusoids and the blood vessels. The gall bladder wall consists of a mucous layer a muscle layer and a serous layer. The bottom of the epithelium abounds with round or oval secretory. In liver, immunohistochemistry results show that AQP1 have intense reaction in hepatic lobule, Kupffer cells (Macrophagocytus stellatus), hepatocytes, portal tract, blood islands ,vein and artery, but almost no reaction of AQP2 was detected. In gallbladder, mucous epithelium, endothelial cells from vein and artery all have strong AQP1 expression, AQP2 showed minor diffused positive reaction in gallbladder, which suggesting that AQP1 may have the main role in the absorption and transportation of fluid in hepatobiliary system of Qinghai Lizard.

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The role of mammalian superaquaporins inside the cell

Cited by 124 publications

References 44 publications

Aquaporins in Health and Disease: An Overview Focusing on the Gut of Different Species

Aquaporins in Health and Disease: An Overview Focusing on the Gut of Different Species

Membrane Stress During Thawing Elicits Redistribution of Aquaporin 7 But Not of Aquaporin 9 in Boar Spermatozoa

Immunohistochemical Study of Aquaporin 1 and 2 in the Hepatobiliary System of Qinghai Lizard ( Phrynocephalus vlangalii )

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