Interaction of lens crystallins with lipid vesicles

Ifeanyi, F.; Takemoto, L.

doi:10.1016/0014-4835(91)90054-i

Cited by 31 publications

(30 citation statements)

References 17 publications

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“…Mulders et al (1985) and Liang and Li (1992) proposed that the binding of α-crystallin to lens membranes is mediated through the main intrinsic protein of the membrane (MIP 26), which may contain a recognition site for the α-crystallin molecule. Lens lipids alone also have a high capacity to bind α-crystallin (Ifeanyi and Takemoto, 1991 ;Ward et al, 1996 ;Borchman and Tang, 1996). As mentioned before, the ratio of cholesterol to the phospholipid in lens membranes can reach 4 to 1, the highest in nature.…”

Section: Discussionmentioning

confidence: 94%

“…α-Crystallin could bind to lens membrane through interactions with the polar-nonpolar interface of the membrane's main intrinsic protein, MIP 26, (Mulders et al, 1985 ;Liang and Li, 1992) or with the membrane's lipid, since α-crystallin was shown to bind with protein-free liposomes (Ifeanyi and Takemoto, 1991 ;Borchman and Tang, 1996 ;Ward et al, 1996). α-Crystallin is composed of 20 kDa A and B monomers which non-covalently associate into aggregates of about 800 kDa (Groth-Vasselli, Kumosinksi and Farnsworth, 1995).…”

Section: Introductionmentioning

confidence: 95%

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Influence of Cholesterol on the Interaction of α-Crystallin with Phospholipids

Tang

Borchman

Yappert

et al. 1998

Experimental Eye Research

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Section: Discussionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 95%

Influence of Cholesterol on the Interaction of α-Crystallin with Phospholipids

Tang

Borchman

Yappert

et al. 1998

Experimental Eye Research

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“…As membrane proteins in lens fiber cells are thought to contribute a large percentage of the lens membrane mass, we consider it likely that the apparent increase in binding capacity of trypsinized compared with untreated membranes reflects enhanced access of ␣-crystallin complexes to the lipid bilayer, although we cannot rule out the possibility that trypsinization creates damaged proteins to which ␣-crystallin could potentially bind. Given the insensitivity of ␣-crystallin binding to increased ionic strength at physiologic pH, the apparent enhancement of binding capacity following trypsinization of membranes, and the published reports on the saturable association of ␣-crystallin with protein-free synthetic phospholipid vesicles, we postulate that ␣-crystallin binding to the membrane occurs predominantly through hydrophobic interactions rather than through protein-protein interactions as proposed previously (22,(31)(32)(33)47).…”

mentioning

confidence: 89%

“…In a previous study, the interaction of native ␣-crystallin with membranes was shown to be markedly sensitive to ionic strength while reaching an optimum at 37°C and a pH of 7.5 (22). In addition, saturable binding to protein-free phospholipid vesicles has been observed, but the measured capacity is reduced dramatically upon incorporation of cholesterol (31)(32)(33). Finally, it has been postulated that ␣B-crystallin is largely unable to bind membranes in the absence of ␣A-crystallin (20,23).…”

mentioning

confidence: 99%

Characterization of α-Crystallin-Plasma Membrane Binding

Cobb¹,

Petrash²

2000

Journal of Biological Chemistry

113

115

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␣-Crystallin, a large lenticular protein complex made up of two related subunits (␣A-and ␣B-crystallin), is known to associate increasingly with fiber cell plasma membranes with age and/or the onset of cataract. To understand better the binding mechanism, we developed a sensitive membrane binding assay using lens plasma membranes and recombinant human ␣A-and ␣B-crystallins conjugated to a small fluorescent tag (Alexa350 ® ). Both ␣A and ␣B homopolymer complexes, as well as a reconstituted 3:1 heteromeric complex, bind to lens membranes in a specific, saturable, and partially irreversible manner that is sensitive to both time and temperature. The amount of ␣-crystallin that binds to the membrane increases under acidic pH conditions and upon removal of exposed intrinsic membrane protein domains but is not affected at high ionic strength, suggesting that ␣-crystallin binds to the fiber cell plasma membranes mainly through hydrophobic interactions. The binding capacity and affinity for the reconstituted 3:1 heteromeric complex were measured to be 3.45 ؎ 0.11 ng/g of membrane and 4.57 ؎ 0.50 ؋ 10 ؊4 g ؊1 of membrane, respectively. The present membrane binding data support the hypothesis that the physical properties of a mixed ␣-crystallin complex may hold particular relevance for the function of ␣-crystallin within the lens.

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“…The binding property of ·-crystallin has been studied extensively by Ifeanyi and Takemoto [4][5][6][7]. ·-Crystallin binding may be mediated by the intrinsic protein MP26 [8][9][10].…”

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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Interaction of lens crystallins with lipid vesicles

Cited by 31 publications

References 17 publications

Influence of Cholesterol on the Interaction of α-Crystallin with Phospholipids

Influence of Cholesterol on the Interaction of α-Crystallin with Phospholipids

Characterization of α-Crystallin-Plasma Membrane Binding

Alpha-Crystallin/Lens Lipid Interactions Using Resonance Energy Transfer

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