Aquaporins: water channel proteins of the cell membrane

Takata, Kuniaki; Matsuzaki, Toshiyuki; Tajika, Yuki

doi:10.1016/j.proghi.2004.03.001

Cited by 361 publications

(288 citation statements)

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“…Compared with other mammalian orthodox aquaporins (namely with AQP1), AQP3 is moderately permeable to water, but highly permeable to glycerol and possibly to urea [1]. AQP3 expression has been reported in several mammalian tissues including kidney, epidermis, urinary, respiratory and digestive tracts [11] and in human erythrocytes [13].…”

Section: Introductionmentioning

confidence: 99%

Lack of Aquaporin 3 in bovine erythrocyte membranes correlates with low glycerol permeation

Campos

Moura

Oliva

et al. 2011

Biochemical and Biophysical Research Communications

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In general, erythrocytes are highly permeable to water, urea and glycerol.However, expression of aquaporin isoforms in erythrocytes appears to be species characteristic. In the present study, human (hRBC) and bovine (bRBC) erythrocytes were chosen for comparative studies due to their significant difference in membrane glycerol permeability.Osmotic water permeability (P f ) at 23 ºC was (2.89 0.37) 10 -2 and (5.12 0.61) 10 -2 cm s -1 for human and bovine cells respectively, with similar activation energies for water transport. Glycerol permeability (P gly ) for human ((1.37 0.26) 10 -5 cm s -1 ) differed in three orders of magnitude from bovine erythrocytes ((5.82 0.37) 10 -8 cm s -1 ) that also showed higher activation energy for glycerol transport.When compared to human, bovine erythrocytes showed a similar expression pattern of AQP1 glycosylated forms on immunoblot analysis, though in slight higher levels, which could be correlated with the 1.5-fold larger P f found. However, AQP3 expression was not detectable. Immunofluorescence analysis confirmed the absence of AQP3 expression in bovine erythrocyte membranes.In conclusion, lack of AQP3 in bovine erythrocytes points to the lipid pathway as responsible for glycerol permeation and explains the low glycerol permeability and high E a for transport observed in ruminants.

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Section: Introductionmentioning

confidence: 99%

Lack of Aquaporin 3 in bovine erythrocyte membranes correlates with low glycerol permeation

Campos

Moura

Oliva

et al. 2011

Biochemical and Biophysical Research Communications

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“…The other aspect is the discovery that some aquaporins are multifunctional channel proteins, allowing some small neutral solutes across cellular membranes, such as glycerol, CO 2 , ammonia (NH 3 ), urea, boron, and hydrogen peroxide [13][14][15][16][17]. The diversity of aquaporin isoforms in plants can also be explained in part by their presence in multiple subcellular compartments [7,9,18].…”

Section: Diversity Of Plant Aquaporinsmentioning

confidence: 99%

“…Studies regarding the aquaporin mRNA abundance have led to the following conclusions: (1) many aquaporins are highly expressed in the vascular tissues; (2) some tonoplast aquaporins are highly expressed in meristems, where vacuolar biogenesis takes place; (3) aquaporins are highly expressed in the tissues that can experience high water or metabolite flux [39][40][41]. It is therefore of interest to study the expression patterns of AQP isoforms in order to further elucidate their involvement in plant water transport [6,18,19].…”

Section: Aquaporin Gene Expression and Diurnal Fluctuationsmentioning

confidence: 99%

“…Regardless of whether all or only the majority of the plant MIPs are aquaporins, it is clear that a large number of aquaporins are present in plants, some localized in the tonoplast, some in the plasma membrane and some possibly localized in endomembranes [4,6,11,18,20,21,26,32,45]. MIP-B was found in fractions containing tonoplast proteins and possibly in a fraction of intermediate density, distinct from both plasma membrane and tonoplast, and also distinct from the fractions in which MIP-A was located [19,34,50].…”

Section: Aquaporin Cellular and Subcellular Localizationmentioning

confidence: 99%

“…Multiple aquaporin genes could allow for variable expression in different tissues, cells and intracellular membranes during development, under changing external conditions and in response to rapidly changing demands for water movement [4,6,11,18,20,21,26,32,45,50,52]. Höfte et al found that a presumptive tonoplast aquaporin (Phaseollus ␣-TIP) is located in multivesicular bodies in transgenic tobacco that expresses Phaseollus ␣-TIP [53].…”

Section: Aquaporin Cellular and Subcellular Localizationmentioning

confidence: 99%

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Aquaporin structure–function relationships: Water flow through plant living cells

Zhao

Shao

Chu

2008

Colloids and Surfaces B: Biointerfaces

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Plant aquaporins play an important role in water uptake and movement-an aquaporin that opens and closes a gate that regulates water movement in and out of cells. Some plant aquaporins also play an important role in response to water stress. Since their discovery, advancing knowledge of their structures and properties led to an understanding of the basic features of the water transport mechanism and increased illumination to water relations. Meanwhile, molecular and functional characterization of aquaporins has revealed the significance of their regulation in response to the adverse environments such as salinity and drought. This paper reviews the structure, species diversity, physiology function, regulation of plant aquaporins, and the relations between environmental factors and plant aquaporins. Complete understanding of aquaporin function and regulation is to integrate those mechanisms in time and space and to well regulate the permeation of water across biological membranes under changing environmental and developmental conditions.

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