Immunological Properties of Rat Lens Gamma-Crystallins

Vornhagen, Rolf; Bours, J.; Rink, H.

doi:10.1159/000265207

Cited by 3 publications

(5 citation statements)

References 10 publications

(10 reference statements)

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“…[6]. Microimmunoelectrophoresis (MIE) and immunodiffusion (ID) were carried out as pub lished by Bours et al [7], The antisera were from pre vious studies [7][8][9][10].…”

Section: Aterials and M Ethodsmentioning

confidence: 99%

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Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with β_s- and γ-Crystallins

Bours

1996

Ophthalmic Res

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Calf water-soluble (WS) crystallins consist of high-molecular weight (HM), α-, β_H-, β_L-, β_s- and γ-crystallins. α-Crystallin as a molecular chaperone forms a structure with a central hole, known as Carver’s model. The only crystallins fitting into this central cavity are β_s- and γ-crystallins, with native molecular weights of 28 and 18.5-21 kD, respectively. The β_s-crystallin is loosely bound to this structure, whereas with the application of 7M urea in the sample, β_s-, may be some β_L-components and all γ-crystallins emerge from the central hole. Although WS and water-insoluble (WI) crystallins display the same immunologic determinants, there is an appreciable difference in electrophoretic mobility already in the young calf lens, α-Crystallins from the WI part demonstrate a clear cathodic shift. WI β- and γ-crystallins show smaller but well perceptible cathodic shifts. The chaperone function of α-crystallin preserves the original structures of β_s- and γ-crystallins for aggregation and other influences.

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“…[6]. Microimmunoelectrophoresis (MIE) and immunodiffusion (ID) were carried out as pub lished by Bours et al [7], The antisera were from pre vious studies [7][8][9][10].…”

Section: Aterials and M Ethodsmentioning

confidence: 99%

“…e Anti bovine y-crystallin (ABGC). f Antirat yi-crystallin (ARGiC), directed against y-crystallins of lower isoelectric points (IEPs) (7.05-7.50) [9,10]. g Antirat yi-crystallin (ARG:C), directed against y-crystallins of higher IEPs (7.55-8.20) [10].…”

Section: Fig 3 Mie Of: (1) Ws Crystallins and (2) Wi Crys Tallins Omentioning

confidence: 99%

Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with β_s- and γ-Crystallins

Bours

1996

Ophthalmic Res

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“…The exact function of these proteins is unknown, although the integrity of these polypeptides is generally believed to be critical to the maintenance of lens transparency (5). Changes in lens transparency that occur with age or during cataract formation are usually accompanied by structural alterations in the -y-crystallin proteins (8-10); however, the relationship between these changes and the opacification of the lens is not yet understood.Studies on rodent y-crystallins indicate that y-crystallin gene expression is differentially regulated during development (18,(21)(22)(23). Differential accumulation of low-molecular-weight human lens proteins has also been observed, suggesting that the human y-crystallin genes may also be temporally regulated during development (15,19,26).…”

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confidence: 99%

“…Studies on rodent y-crystallins indicate that y-crystallin gene expression is differentially regulated during development (18,(21)(22)(23). Differential accumulation of low-molecular-weight human lens proteins has also been observed, suggesting that the human y-crystallin genes may also be temporally regulated during development (15,19,26).…”

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Relationship between proteins encoded by three human gamma-crystallin genes and distinct polypeptides in the eye lens.

Russell¹,

Meakin²,

Hohman³

et al. 1987

Mol. Cell. Biol.

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Although individual -y-crystallins from the human eye lens have not been successfully purffied and sequenced, most of the genes coding for these lens-specific structural proteins have been cloned and characterized. To investigate the relationship between these genes and the y-crystallins of the human lens, we made use of mouse cell lines which contain stably integrated copies of the coding sequences for three of the human -y-crystallin genes coupled to the human metallothionein IIA promoter. The proteins produced by these hybrid genes in cell culture were detected immunologically and compared by physical characteristics with the -y-crystallins from the human lens. The protein encoded by the G3 gene showed properties identical to those of the 21,000-molecular-weight y-crystallin from 11-month-old lens. The protein isolated from the cells expressing the G4 gene was similar to a 19,000-molecular-weight lens y-crystallin, while gene G5 encodes a highly basic -y-crystallin which may be synthesized in only limited amounts in the human lens. These correlations provide a basis for future investigations on the relationship between putative mutations in human -y-crystallin genes and altered proteins in hereditary lens cataracts.The human lens is a biconvex, avascular organ which contains three major immunologically and biochemically distinct classes of proteins, the oa-, P-, and -y-crystallins (1).During lens growth, undifferentiated epithelial cells migrate from the anterior surface of the lens towards the equatorial axis, where they differentiate to form elongated lens fibers. Concomitant with lens cell differentiation is the activation of -y-crystallin gene expression (1, 14). The y-crystallins account for approximately 20% of the soluble lens protein. The exact function of these proteins is unknown, although the integrity of these polypeptides is generally believed to be critical to the maintenance of lens transparency (5). Changes in lens transparency that occur with age or during cataract formation are usually accompanied by structural alterations in the -y-crystallin proteins (8-10); however, the relationship between these changes and the opacification of the lens is not yet understood.Studies on rodent y-crystallins indicate that y-crystallin gene expression is differentially regulated during development (18,(21)(22)(23). Differential accumulation of low-molecular-weight human lens proteins has also been observed, suggesting that the human y-crystallin genes may also be temporally regulated during development (15,19,26). The human -y-crystallins are encoded by seven closely related genes located on chromosome 2, region q33-36 (6,7,16,17,20,24). Detailed analysis of six of these genes has revealed that two are highly related pseudogenes and contain the same in-frame termination codon at identical positions in their coding sequence (16); the other four are potentially active and encode closely related polypeptides that show 70 to 79% homology in amino acid sequence (7,17). However, the relationship between these gen...

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“…Studies on rodent y-crystallins indicate that y-crystallin gene expression is differentially regulated during development (18, [21][22][23]. Differential accumulation of low-molecular-weight human lens proteins has also been observed, suggesting that the human y-crystallin genes may also be temporally regulated during development (15,19,26).…”

mentioning

confidence: 99%

Relationship Between Proteins Encoded by Three Human γ-Crystallin Genes and Distinct Polypeptides in the Eye Lens

Russell

Meakin

Hohman

et al. 1987

Molecular and Cellular Biology

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Although individual gamma-crystallins from the human eye lens have not been successfully purified and sequenced, most of the genes coding for these lens-specific structural proteins have been cloned and characterized. To investigate the relationship between these genes and the gamma-crystallins of the human lens, we made use of mouse cell lines which contain stably integrated copies of the coding sequences for three of the human gamma-crystallin genes coupled to the human metallothionein IIA promoter. The proteins produced by these hybrid genes in cell culture were detected immunologically and compared by physical characteristics with the gamma-crystallins from the human lens. The protein encoded by the G3 gene showed properties identical to those of the 21,000-molecular-weight gamma-crystallin from 11-month-old lens. The protein isolated from the cells expressing the G4 gene was similar to a 19,000-molecular-weight lens gamma-crystallin, while gene G5 encodes a highly basic gamma-crystallin which may be synthesized in only limited amounts in the human lens. These correlations provide a basis for future investigations on the relationship between putative mutations in human gamma-crystallin genes and altered proteins in hereditary lens cataracts.

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Immunological Properties of Rat Lens Gamma-Crystallins

Cited by 3 publications

References 10 publications

Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with β_s- and γ-Crystallins

Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with β_s- and γ-Crystallins

Relationship between proteins encoded by three human gamma-crystallin genes and distinct polypeptides in the eye lens.

Relationship Between Proteins Encoded by Three Human γ-Crystallin Genes and Distinct Polypeptides in the Eye Lens

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Immunological Properties of Rat Lens Gamma-Crystallins

Cited by 3 publications

References 10 publications

Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with βs- and γ-Crystallins

Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with βs- and γ-Crystallins

Relationship between proteins encoded by three human gamma-crystallin genes and distinct polypeptides in the eye lens.

Relationship Between Proteins Encoded by Three Human γ-Crystallin Genes and Distinct Polypeptides in the Eye Lens

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Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with β_s- and γ-Crystallins

Calf Lens α-Crystallin, a Molecular Chaperone, Builds Stable Complexes with β_s- and γ-Crystallins