1990
DOI: 10.1016/0014-4835(90)90017-o
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Alpha crystallin from human cataractous vs. normal lenses: Change in binding to lens membrane

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Cited by 23 publications
(11 citation statements)
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“…The binding between human lens lipids and alpha-crystallin aggregates of high-molecular weight has been documented. These associations increase with age and opacification Petrash, 2000, 2002a,b;Duindam et al, 1998;Ifeanyi and Takemoto, 1989, 1990a,b, 1991Kodama and Takemoto, 1988;Takehana and Takemoto, 1987;Takemoto et al, 1984;Tang et al, 1998Tang et al, , 1999Zhang et al, 1999;Zigman et al, 1984). It is also possible that the unexpected absence of non-sedimenting bands in membranes from cataractous tissues may reflect an even greater enhancement in the density of the otherwise floating clusters.…”
Section: Sms Versus Dhsms: Interactions With Cholmentioning
confidence: 99%
“…The binding between human lens lipids and alpha-crystallin aggregates of high-molecular weight has been documented. These associations increase with age and opacification Petrash, 2000, 2002a,b;Duindam et al, 1998;Ifeanyi and Takemoto, 1989, 1990a,b, 1991Kodama and Takemoto, 1988;Takehana and Takemoto, 1987;Takemoto et al, 1984;Tang et al, 1998Tang et al, , 1999Zhang et al, 1999;Zigman et al, 1984). It is also possible that the unexpected absence of non-sedimenting bands in membranes from cataractous tissues may reflect an even greater enhancement in the density of the otherwise floating clusters.…”
Section: Sms Versus Dhsms: Interactions With Cholmentioning
confidence: 99%
“…Many models of cataracts involve alterations in lens cell membranes [79][80][81]. ACrystallin binds to lens cell membranes and this association is increased in lenses with cataracts.…”
Section: Functions Of -Crystallin In Cell Growth Viability and Genomentioning
confidence: 99%
“…But to date, there have been no reports of α-crystallin association with such receptors, and α-crystallin function has been attributed mostly to its actions in the cytoplasm. Significant interactions of αA-crystallin with lens membranes have been reported to occur with cataract onset, but this association results from changes in the biochemical properties of lens membranes that are acquired with aging (Ifeanyi and Takemoto, 1990b; Ifeanyi and Takemoto, 1990a; Ifeanyi and Takemoto, 1991; Cobb and Petrash, 2000; Cobb and Petrash, 2002). While αA-crystallin also has been shown to localize along cell-cell borders of normal lens epithelial cells (Wang et al, 2004), how αA-crystallin is targeted to the lens plasma membrane is not yet known, and no studies have investigated whether αA-crystallin associates with membrane receptors that regulate cell survival signaling pathways.…”
Section: Introductionmentioning
confidence: 99%