Changes to zonular tension alters the subcellular distribution of AQP5 in regions of influx and efflux of water in the rat lens

Petrova, Rosica S.; Bavana, Nandini; Zhao, Rusin; Schey, Kevin L.; Donaldson, Paul J.

doi:10.1101/2020.06.29.178756

Cited by 4 publications

(11 citation statements)

References 57 publications

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“…Results from bafilomycin A1 treatment also provide further evidence that AQP5 functions as a regulatory water channel whose trafficking is inducible in the mammalian lens. Petrova et al has previously demonstrated dynamic AQP5 subcellular localization changes in response to changes in zonular tension via mechanosensitive TRPV1 channel agonism 17,21 . Since AQP5 plasma membrane insertion significantly increases fiber cell water permeability in both mouse and rat lenses 17 , regulation of AQP5 subcellular localization can alter lens water homeostasis.…”

Section: Discussionmentioning

confidence: 99%

“…The important role of AQP5 in maintaining lens homeostasis is implied by its expression in all mammalian lenses studied to date including human 12,[18][19][20] , bovine 12 , mouse 11,12,16,17,[19][20][21] , rat 12,17,21 , rabbit 8 , and dog 22 lenses. Functional studies demonstrate the relationship between AQP5 expression and lens osmotic homeostasis.…”

Section: Introductionmentioning

confidence: 99%

“…Immunohistochemical studies show AQP5 primarily localized to the plasma membrane in the fiber cells of the mouse lens cortex and to cytoplasmic vesicles in the rat lens cortex and the extent of fiber cell permeability correlates to plasma membrane AQP5 abundance 17 . Cytoplasmic AQP5 in rat lenses is dynamically inserted into fiber cell plasma membranes in response to changes in zonular tension and thereby increases fiber cell plasma membrane water permeability (P H2O ) 17,21 .…”

Section: Introductionmentioning

confidence: 99%

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Lens aquaporin-5 inserts into bovine fiber cell plasma membranes through mitochondria-associated lysosome secretion

Gletten

Cantrell

Schey

et al. 2022

Preprint

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PURPOSE: To spatially map aquaporin-5 (AQP5) expression in bovine lens, molecularly characterize cytoplasmic AQP5-containing vesicles in the outer cortex, and elucidate AQP5 membrane trafficking mechanisms. METHODS. Immunofluorescence was performed on bovine lens cryosections using AQP5, TOMM20, COX IV, calnexin, LC3B, LIMP-2, and connexin-50 antibodies and the fluorescent lipid membrane dye CM-DiI. AQP5 plasma membrane insertion was defined via line expression profile analysis. Transmission electron microscopy (TEM) was performed on bovine lens tissue sections to define cytoplasmic organelle identity, morphology, and subcellular localization in cortical fiber cells. Bovine lenses were treated with 10 nM bafilomycin A1 or 0.1% dimethyl sulfoxide vehicle control in ex vivo culture to determine changes in AQP5 plasma membrane expression. RESULTS. Immunofluorescence analysis revealed cytoplasmic AQP5 expression in bovine lens epithelial cells and differentiating fiber cells. In the bovine lens cortex, complete AQP5 plasma membrane insertion occurs at r/a 0.951 + 0.005. AQP5-containing cytoplasmic vesicles are spheroidal, tubular in morphology, express TOMM20, and contain LC3B and LIMP-2 as fiber cells mature. TEM analysis revealed spheroidal, tubular autophagosomes, autolysosomes, and lysosomes with degrading mitochondria. AQP5-containing cytoplasmic vesicles and autolysosomes dock and fuse with the plasma membrane. Bafiloymcin A1 treatment reduced AQP5 plasma membrane expression by 27%. CONCLUSIONS: AQP5 localizes to spheroidal, tubular cytoplasmic vesicles in the differentiating bovine lens fiber cells. During fiber cell differentiation, these vesicles incorporate LC3B and fuse with LIMP-2-positive lysosomes. AQP5 trafficking to the plasma membrane occurs through lysosome secretion as a novel mechanism of AQP5 trafficking.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Lens aquaporin-5 inserts into bovine fiber cell plasma membranes through mitochondria-associated lysosome secretion

Gletten

Cantrell

Schey

et al. 2022

Preprint

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“…It has also been reported that oral treatment with Hsd ameliorated lens fluid influx and osmotic imbalance in diabetic cataract lenses [ 25 ]. Membrane insertion of TRPV4 and AQP5 was observed in response to accommodation changes [ 10 , 11 ]. As fiber cells differentiate, they lose their cellular organelles and their ability to perform de novo protein synthesis [ 26 , 27 ].…”

Section: Discussionmentioning

confidence: 99%

“…Among the AQP family, AQP0, AQP1, and AQP5 are expressed in lens cells. It was reported that the distribution of TRPV4 in the peripheral fiber cells and AQP5 in the efflux and anterior influx zones altered their subcellular localization in response to mechanical and pharmacologically induced reductions in zonular tension [ 10 , 11 ]. These data suggest that AQPs and TRPVs could exist as a store of channels that could be recruited to the plasma membrane to control the water circulation and intracellular pressure in the lens.…”

Section: Introductionmentioning

confidence: 99%

Effect of Alpha-Glucosyl-Hesperidin Consumption on Lens Sclerosis and Presbyopia

Nakazawa

Doki

Sugiyama

et al. 2021

Cells

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Presbyopia is characterized by a decline in the ability to accommodate the lens. The most commonly accepted theory for the onset of presbyopia is an age-related increase in the stiffness of the lens. However, the cause of lens sclerosis remains unclear. With age, water microcirculation in the lens could change because of an increase in intracellular pressure. In the lens, the intracellular pressure is controlled by the Transient Receptor Potential Vanilloid (TRPV) 1 and TRPV4 feedback pathways. In this study, we tried to elucidate that administration of α-glucosyl-hesperidin (G-Hsd), previously reported to prevent nuclear cataract formation, affects lens elasticity and the distribution of TRPV channels and Aquaporin (AQP) channels to meet the requirement of intracellular pressure. As a result, the mouse control lens was significantly toughened compared to both the 1% and 2% G-Hsd mouse lens treatments. The anti-oxidant levels in the lens and plasma decreased with age; however, this decrease could be nullified with either 1% or 2% G-Hsd treatment in a concentration- and exposure time-dependent manner. Moreover, G-Hsd treatment affected the TRPV4 distribution, but not TRPV1, AQP0, and AQP5, in the peripheral area and could maintain intracellular pressure. These findings suggest that G-Hsd has great potential as a compound to prevent presbyopia and/or cataract formation.

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The importance of the epithelial fibre cell interface to lens regeneration in an in vivo rat model and in a human bag-in-the-lens (BiL) sample

Lois

Prescott

et al. 2021

Experimental Eye Research

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Changes to zonular tension alters the subcellular distribution of AQP5 in regions of influx and efflux of water in the rat lens

Cited by 4 publications

References 57 publications

Lens aquaporin-5 inserts into bovine fiber cell plasma membranes through mitochondria-associated lysosome secretion

Lens aquaporin-5 inserts into bovine fiber cell plasma membranes through mitochondria-associated lysosome secretion

Effect of Alpha-Glucosyl-Hesperidin Consumption on Lens Sclerosis and Presbyopia

The importance of the epithelial fibre cell interface to lens regeneration in an in vivo rat model and in a human bag-in-the-lens (BiL) sample

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