Temperature Induced Structural Changes ofβ-Crystallin and Sphingomyelin Binding

Tang, Dong; Borchman, Douglas

doi:10.1006/exer.1998.0497

Cited by 21 publications

(20 citation statements)

References 35 publications

(41 reference statements)

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“…In a previous study, we used the fluorescence probe, N-(7-nitrobenz-2-oxa-1,3-diazol4yl)-1,2-dihexa-decanoyl-sn-glycero-3 phosphoethanolamine, to monitor ·-crystallin binding to sphingomyelin/cholesterol vesicles [13][14][15]. Similarly, in this experiment we preincorporated 0.5% (wt/wt) dansyl DHPE into cortex lipid vesicles, then added ·-crystallin from 0 to 60% (wt/wt).…”

Section: Resultsmentioning

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%

“…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. Hydrophobic interactions near the head group region of the bilayer membranes may define the binding site for the hydrophobic surface of ·-crystallin.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Alpha-Crystallin/Lens Lipid Interactions Using Resonance Energy Transfer

Tang¹,

Borchman²,

Yappert³

1999

Ophthalmic Res

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“…␣ -Crystallin is the only crystallin that binds noncovalently to bovine lens lipid membranes (128)(129)(130)(131)(132)(133)(134)(135)(136)(137)(138)(139)(140) that are devoid of protein and synthetic lipid membranes ( 43,(129)(130)(131). Lens membranes have both a high-affi nity saturable and a low-affi nity nonsaturable ␣ -crystallin binding site (135)(136)(137).…”

Section: ␣ -Crystallin Lipid Bindingmentioning

confidence: 99%

“…It may be relevant to cataractogenesis that as ␣ -crystallin becomes denatured, it binds more deeply into the membrane ( 128,134 ). The association of ␣ -crystallin with the membrane increases with age and cataract, as does light scattering ( 130,140,141 ). The increased association is thought not to be due to posttranslational modifi cations of ␣ -crystallin.…”

Section: ␣ -Crystallin Lipid Bindingmentioning

confidence: 99%

Lipids and the ocular lens

Borchman

Yappert

2010

Journal of Lipid Research

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139

133

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Lipid composition, membrane structure relationships in lens and muscle sarcoplasmic reticulum membranes

1999

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Membrane lipid composition varies in different tissues and species. Since a defined lipid composition is essential to the function of many membranes, the relationship between membrane lipid composition and structure was determined using infrared and Raman spectroscopy in four membranes containing a calcium pump: rabbit fast and slow twitch muscle sarcoplasmic reticulum and human and bovine lens fiber cell membranes. We found that membrane sphingolipid and phosphatidylcholine content were correlated to a decrease and increase, respectively, in the infrared lipid CH2 symmetric stretching band frequency. We interpret the change in frequency as a change in lipid hydrocarbon chain structural order. This was confirmed by Raman order parameters. The high degree of hydrocarbon chain saturation found in the variable amide chains of sphingolipids is likely to account for this correlation. Lipid phase transition temperature and cooperativity also correlated to sphingolipid and phosphatidylcholine content, and are the forces defining the order in at physiological temperature in the samples studied. Ca2+‐ATPase caused an increase in the CH2 symmetric stretching frequency in fast twitch muscle sarcoplasmic reticulum (interpreted as an increase in hydrocarbon chain disorder), but had no effect on slow twitch muscle sarcoplasmic reticulum lipid hydrocarbon chain structure. In the natural systems studied, we find that it is the lipid hydrocarbon chain saturation that defines lipid hydrocarbon chain order. © 1999 John Wiley & Sons, Inc. Biospectroscopy 5: 151–167, 1999

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Temperature Induced Structural Changes ofβ-Crystallin and Sphingomyelin Binding

Cited by 21 publications

References 35 publications

Alpha-Crystallin/Lens Lipid Interactions Using Resonance Energy Transfer

Alpha-Crystallin/Lens Lipid Interactions Using Resonance Energy Transfer

Lipids and the ocular lens

Lipid composition, membrane structure relationships in lens and muscle sarcoplasmic reticulum membranes

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