Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.

Aquaporin 0 (AQP0) formerly known as membrane intrinsic protein (MIP), is expressed exclusively in the lens during terminal differentiation of fiber cells. AQP0 plays an important role not only in the regulation of water content but also in cell-to-cell adhesion of the lens fiber cells. We have inve...

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Autores principales:	Satyanarayana Swamy-Mruthinti, Volety Srinivas, John E Hansen, Ch Mohan Rao
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/98fb3059a13249b29ed52f22d57591dc
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spelling	oai:doaj.org-article:98fb3059a13249b29ed52f22d57591dc2021-11-18T08:44:27ZThermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.1932-620310.1371/journal.pone.0080404https://doaj.org/article/98fb3059a13249b29ed52f22d57591dc2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24312215/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Aquaporin 0 (AQP0) formerly known as membrane intrinsic protein (MIP), is expressed exclusively in the lens during terminal differentiation of fiber cells. AQP0 plays an important role not only in the regulation of water content but also in cell-to-cell adhesion of the lens fiber cells. We have investigated the thermal stress-induced structural alterations of detergent (octyl glucoside)-solubilized calf lens AQP0. The results show an increase in the amount of AQP0 that aggregated as the temperature increased from 40°C to 65°C. α-Crystallin, molecular chaperone abundantly present in the eye lens, completely prevented the AQP0 aggregation at a 1∶1 (weight/weight) ratio. Since α-crystallin consists of two gene products namely αA- and αB-crystallins, we have tested the recombinant proteins on their ability to prevent thermal-stress induced AQP0 aggregation. In contrast to the general observation made with other target proteins, αA-crystallin exhibited better chaperone-like activity towards AQP0 compared to αB-crystallin. Neither post-translational modifications (glycation) nor C-terminus truncation of AQP0 have any appreciable effect on its thermal aggregation properties. α-Crystallin offers similar protection against thermal aggregation as in the case of the unmodified AQP0, suggesting that αcrystallin may bind to either intracellular loops or other residues of AQP0 that become exposed during thermal stress. Far-UV circular dichroism studies indicated a loss of αhelical structures when AQP0 was subjected to temperatures above 45°C, and the presence of α-crystallin stabilized these secondary structures. We report here, for the first time, that α-crystallin protects AQP0 from thermal aggregation. Since stress-induced structural perturbations of AQP0 may affect the integrity of the lens, presence of the molecular chaperone, α-crystallin (particularly αA-crystallin) in close proximity to the lens membrane is physiologically relevant.Satyanarayana Swamy-MruthintiVolety SrinivasJohn E HansenCh Mohan RaoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e80404 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Satyanarayana Swamy-Mruthinti Volety Srinivas John E Hansen Ch Mohan Rao Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.
description	Aquaporin 0 (AQP0) formerly known as membrane intrinsic protein (MIP), is expressed exclusively in the lens during terminal differentiation of fiber cells. AQP0 plays an important role not only in the regulation of water content but also in cell-to-cell adhesion of the lens fiber cells. We have investigated the thermal stress-induced structural alterations of detergent (octyl glucoside)-solubilized calf lens AQP0. The results show an increase in the amount of AQP0 that aggregated as the temperature increased from 40°C to 65°C. α-Crystallin, molecular chaperone abundantly present in the eye lens, completely prevented the AQP0 aggregation at a 1∶1 (weight/weight) ratio. Since α-crystallin consists of two gene products namely αA- and αB-crystallins, we have tested the recombinant proteins on their ability to prevent thermal-stress induced AQP0 aggregation. In contrast to the general observation made with other target proteins, αA-crystallin exhibited better chaperone-like activity towards AQP0 compared to αB-crystallin. Neither post-translational modifications (glycation) nor C-terminus truncation of AQP0 have any appreciable effect on its thermal aggregation properties. α-Crystallin offers similar protection against thermal aggregation as in the case of the unmodified AQP0, suggesting that αcrystallin may bind to either intracellular loops or other residues of AQP0 that become exposed during thermal stress. Far-UV circular dichroism studies indicated a loss of αhelical structures when AQP0 was subjected to temperatures above 45°C, and the presence of α-crystallin stabilized these secondary structures. We report here, for the first time, that α-crystallin protects AQP0 from thermal aggregation. Since stress-induced structural perturbations of AQP0 may affect the integrity of the lens, presence of the molecular chaperone, α-crystallin (particularly αA-crystallin) in close proximity to the lens membrane is physiologically relevant.
format	article
author	Satyanarayana Swamy-Mruthinti Volety Srinivas John E Hansen Ch Mohan Rao
author_facet	Satyanarayana Swamy-Mruthinti Volety Srinivas John E Hansen Ch Mohan Rao
author_sort	Satyanarayana Swamy-Mruthinti
title	Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.
title_short	Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.
title_full	Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.
title_fullStr	Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.
title_full_unstemmed	Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.
title_sort	thermal stress induced aggregation of aquaporin 0 (aqp0) and protection by α-crystallin via its chaperone function.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/98fb3059a13249b29ed52f22d57591dc
work_keys_str_mv	AT satyanarayanaswamymruthinti thermalstressinducedaggregationofaquaporin0aqp0andprotectionbyacrystallinviaitschaperonefunction AT voletysrinivas thermalstressinducedaggregationofaquaporin0aqp0andprotectionbyacrystallinviaitschaperonefunction AT johnehansen thermalstressinducedaggregationofaquaporin0aqp0andprotectionbyacrystallinviaitschaperonefunction AT chmohanrao thermalstressinducedaggregationofaquaporin0aqp0andprotectionbyacrystallinviaitschaperonefunction
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Thermal stress induced aggregation of aquaporin 0 (AQP0) and protection by α-crystallin via its chaperone function.

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