Loss of high-affinity membrane binding of bovine nuclear α-crystallin

Mulders, John W. M.; Wojcik, E. G. C.; Bloemendal, H.; Jong, Wilfried W. de

doi:10.1016/0014-4835(89)90083-3

Cited by 31 publications

(15 citation statements)

References 15 publications

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“…The increased association is thought not to be due to posttranslational modifi cations of ␣ -crystallin. Indeed, in vitro studies have shown that ␣ -crystallins from older ( 129,139,142 ) or cataractous lenses ( 143 ) that have undergone posttranslational modifi cations do not bind effectively to lens membranes. In vitro binding studies show that the binding capacity of ␣ -crystallin to lipids from older lenses increases with age and decreases in diabetic donors who were treated with insulin ( 144 ).…”

Section: ␣ -Crystallin Lipid Bindingmentioning

confidence: 99%

Lipids and the ocular lens

Borchman

Yappert

2010

Journal of Lipid Research

139

133

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Section: ␣ -Crystallin Lipid Bindingmentioning

confidence: 99%

Lipids and the ocular lens

Borchman

Yappert

2010

Journal of Lipid Research

139

133

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Section: Introductionmentioning

confidence: 99%

“…·-Crystallin binding may be mediated by the intrinsic protein MP26 [8][9][10]. Ionic interaction between phospholipid and ·-crystallin [8,9] and the hydrophobic surface of ·-crystallin also influence binding [11][12][13][14]. We studied the binding of ·-crystallin to the lens membrane [15], phospholipid vesicles [13] and the influence of temperature on binding [14] using fluorescence spectroscopy and centrifugation methods.…”

Section: Introductionmentioning

confidence: 99%

Alpha-Crystallin/Lens Lipid Interactions Using Resonance Energy Transfer

Tang¹,

Borchman²,

Yappert³

1999

Ophthalmic Res

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Resonance energy transfer was used to study the interaction of α-crystallin with lens cortex lipid vesicles. The binding of α-crystallin to cortex lipid vesicles and the preincubation temperature dependence of the binding were confirmed. In this study, the tryptophan of α-crystallin was used as the energy donor, and the fluorescence probe N-(5-dimethylaminonaphthalene-1-sulfonyl)-1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine triethylammonium salt (dansyl DHPE) was chosen as the energy acceptor. Lens cortex lipid vesicles were preincorporated with dansyl DHPE. Energy transfer from the tryptophan of α-crystallin to dansyl DHPE was found and the energy transfer efficiency was calculated. There was a higher energy transfer efficiency between α-crystallin and dansyl DHPE when α-crystallin was preincubated at 65°C compared to 22°C. Data confirmed the binding of α-crystallin to lens cortex lipid and showed that α-crystallin bound more closely to the surface of cortex vesicles when it was preincubated at a higher temperature. This is probably due to the exposure of hydrophobic surfaces when α-crystallin is preincubated at a higher temperature.

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“…Mulders et al (1985Mulders et al ( , 1989 found that α-crystallin binding to lens plasma membranes is dependent on salt, temperature, pH and the involvement of transmembrane protein MIP 26. Ifeanyi and Takemoto (1989, 1990a, 1990b found that αcrystallin binds to cortical lens membranes, but not to nuclear membranes, and showed that α-crystallin from human cataractous lenses binds less to lens membranes in vitro.…”

Section: Introductionmentioning

confidence: 99%