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

Tang, Dong; Borchman, Douglas; Yappert, Marta C.; Cenedella, Richard J.

doi:10.1006/exer.1997.0467

Cited by 49 publications

(55 citation statements)

References 41 publications

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“…When the cholesterol content is analyzed, the smallest relative quantities were in the eye lens of a duck (about one third of the average relative cholesterol content of bovine and horse eye lens) and in the eye lens of fish (about one sixth of the relative cholesterol content in the eye lens content of lipids derived from the eye lens of mammals). Cholesterol might affect the interaction of lens membranes with alpha-crystallin, regarded as the key protein engaged in the protection of the vital lens fiber proteins [19].…”

Section: R R R R Results Esults Esults Esults Esultsmentioning

confidence: 99%

Comparing the content of lipids derived from the eye lenses of various species

Panz

Lepiarczyk²,

Zuber³

2011

Folia Histochem Cytobiol.

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Abstract:Abstract: Abstract: Abstract: Abstract: The lipid content in the eye lens was analyzed and compared among various species in this study. The eye lens lipids of the following species were investigated: cow, horse, duck, and freshwater trout. Additionally, the lipids derived from cataractous bovine lens and from cataractous human eye lens lipoprotein complexes were analyzed. The following lipid classes were detected in clear lenses: cholesterol, sphingomyelin, phosphatidylcholine, phosphatidyletanolamine, and phosphatidylserine. In cataractous bovine lens and in lipoprotein complexes from human nuclear cataract, phosphatidyloinositol and phosphatidyloglycerol were detected. Cholesterol and sphingomyelin, essential for hypothetical formation of cholesterol-rich domains, were the most abundant lipids in the lenses of all investigated species. These two components of eye lens lipid fraction were analyzed quantitatively using thin layer chromatography and spectrophotometric assay; the other lipids were identified qualitatively using thin layer chromatography.

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Section: R R R R Results Esults Esults Esults Esultsmentioning

confidence: 99%

Comparing the content of lipids derived from the eye lenses of various species

Panz

Lepiarczyk²,

Zuber³

2011

Folia Histochem Cytobiol.

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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%

Lipids and the ocular lens

Borchman

Yappert

2010

Journal of Lipid Research

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133

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“…This association may be promoted by reductions in membrane cholesterol as the inhibition of cholesterol biosynthesis in the lens has been shown to induce the development of cataracts in rats (42), dogs (43), and humans (44,45). Maintenance of high membrane concentrations of cholesterol may attenuate the interaction of ␣-crystallin with the lens fiber cell membrane (46), but the mechanism is not understood. Based on the findings from this study, it is proposed that the formation of separate sterol-rich and -poor domains may interfere with the ability of extrinsic proteins to aggregate at the membrane surface.…”

Section: Figmentioning

confidence: 99%

Direct Evidence for Immiscible Cholesterol Domains in Human Ocular Lens Fiber Cell Plasma Membranes

Jacob¹,

Cenedella

Mason³

1999

Journal of Biological Chemistry

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The molecular structure of human ocular lens fiber cell plasma membranes was examined directly using small angle x-ray diffraction approaches. A distinct biochemical feature of these membranes is their high relative levels of free cholesterol; the mole ratio of cholesterol to phospholipid (C/P) measured in these membranes ranges from 1 to 4. The organization of cholesterol in this membrane system is not well understood, however. In this study, the structure of plasma membrane samples isolated from nuclear (3.3 C/P) and cortical (2.4 C/P) regions of human lenses was evaluated with x-ray diffraction approaches. Meridional diffraction patterns obtained from the oriented membrane samples demonstrated the presence of an immiscible cholesterol domain with a unit cell periodicity of 34.0 Å, consistent with a cholesterol monohydrate bilayer. The dimensions of the sterol-rich domains remained constant over a broad range of temperatures (5-20°C) and relative humidity levels (31-97%). In contrast, dimensions of the surrounding sterol-poor phase were significantly affected by experimental conditions. Similar structural features were observed in membranes reconstituted from fiber cell plasma membrane lipid extracts. The results of this study indicate that the lens fiber cell plasma membrane is a complex structure consisting of separate sterol-rich and -poor domains. Maintenance of these separate domains may be required for the normal function of lens fiber cell plasma membrane and may interfere with the cataractogenic aggregation of soluble lens proteins at the membrane surface.

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

Cited by 49 publications

References 41 publications

Comparing the content of lipids derived from the eye lenses of various species

Comparing the content of lipids derived from the eye lenses of various species

Lipids and the ocular lens

Direct Evidence for Immiscible Cholesterol Domains in Human Ocular Lens Fiber Cell Plasma Membranes

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