Molecular physiology of water transport: Aquaporin nomenclature workshop. Mammalian aquaporins

Agre, Peter

doi:10.1016/s0248-4900(97)83377-1

Cited by 13 publications

(7 citation statements)

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“…They belong to a highly conserved membrane protein family called major intrinsic proteins (MIPs) [1,2]. In higher plants, AQPs are phylogenetically classified into seven subfamilies: plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), Nodulin 26-like intrinsic proteins (NIPs), small basic intrinsic proteins (SIPs), unrecognized X intrinsic proteins (XIPs), GlpF-like intrinsic proteins (GIPs), and hybrid intrinsic proteins (HIPs) [3][4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

A ginseng PgTIP1 gene whose protein biological activity related to Ser128 residue confers faster growth and enhanced salt stress tolerance in Arabidopsis

Cai

2015

Plant Science

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Section: Introductionmentioning

confidence: 99%

A ginseng PgTIP1 gene whose protein biological activity related to Ser128 residue confers faster growth and enhanced salt stress tolerance in Arabidopsis

Cai

2015

Plant Science

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“…Certain ion channels and organic ion transporters have been shown to mediate water flux. However, it is now realized that the kidney and many other organs contain proteins that are specialized for water transport (5). These proteins constitute the aquaporin family, which now counts as many as 11 members in mammals and more than 30 members in plants.…”

mentioning

confidence: 99%

Alpha syntrophin deletion removes the perivascular but not the endothelial pool of aquaporin‐4 at the blood‐brain barrier and delays the development of brain edema in an experimental model of acute hyponatremia

Xue²,

et al. 2004

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The formation of brain edema, commonly occurring as a potentially lethal complication of acute hyponatremia, is delayed following knockout of the water channel aquaporin-4 (AQP4). Here we show by high-resolution immunogold analysis of the blood-brain-barrier that AQP4 is expressed in brain endothelial cells as well as in the perivascular membranes of astrocyte endfeet. A selective removal of perivascular AQP4 by alpha-syntrophin deletion delays the buildup of brain edema (assessed by Diffusion-weighted MRI) following water intoxication, despite the presence of a normal complement of endothelial AQP4. This indicates that the perivascular membrane domain, which is peripheral to the endothelial blood-brain barrier, may control the rate of osmotically driven water entry. This study is also the first to demonstrate that the time course of edema development differs among brain regions, probably reflecting differences in aquaporin-4 distribution. The resolution of the molecular basis and subcellular site of osmotically driven brain water uptake should help design new therapies for acute brain edema.

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“…Aquaporin 1 (AQP1) was the first water channel to be identified following its cloning and isolation from a human bone marrow library (Preston and Agre, 1991; Agre, 1997). Since then, a number of AQP homologs with wide tissue distributions (Takata et al, 2004) have been found in all living organisms (Hohmann et al, 2001; Cerdà and Finn, 2010).…”

Section: Introductionmentioning

confidence: 99%

Expression and Localization of Aquaporin 1a in the Sea-Bass (Dicentrarchus labrax) during Ontogeny

et al. 2011

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The successful establishment of a species in a given habitat depends on the ability of each of its developing stages to adapt to the environment. In order to understand this process we have studied the adaptation of a euryhaline fish, the sea-bass Dicentrarchus labrax, to various salinities during its ontogeny. The expression and localization of Aquaporin 1a (AQP1a) mRNA and protein were determined in different osmoregulatory tissues. In larvae, the sites of AQP1a expression are variable and they shift according to age, implying functional changes. In juveniles after metamorphosis (D32–D48 post-hatch, 15–25 mm) and in pre-adults, an increase in AQP1a transcript abundance was noted in the digestive tract, and the AQP1a location was observed in the intestine. In juveniles (D87–D100 post-hatch, 38–48 mm), the transcript levels of AQP1a in the digestive tract and in the kidney were higher in sea water (SW) than at lower salinity. These observations, in agreement with existing models, suggest that in SW-acclimated fish, the imbibed water is absorbed via AQP1a through the digestive tract, particularly the intestine and the rectum. In addition, AQP1a may play a role in water reabsorption in the kidney. These mechanisms compensate dehydration in SW, and they contribute to the adaptation of juveniles to salinity changes during sea-lagoon migrations. These results contribute to the interpretation of the adaptation of populations to habitats where salinity varies.

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Molecular physiology of water transport: Aquaporin nomenclature workshop. Mammalian aquaporins

Cited by 13 publications

References 0 publications

A ginseng PgTIP1 gene whose protein biological activity related to Ser128 residue confers faster growth and enhanced salt stress tolerance in Arabidopsis

A ginseng PgTIP1 gene whose protein biological activity related to Ser128 residue confers faster growth and enhanced salt stress tolerance in Arabidopsis

Alpha syntrophin deletion removes the perivascular but not the endothelial pool of aquaporin‐4 at the blood‐brain barrier and delays the development of brain edema in an experimental model of acute hyponatremia

Expression and Localization of Aquaporin 1a in the Sea-Bass (Dicentrarchus labrax) during Ontogeny

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