The presence of lens antigens in the intra-ocular tissues of the chick eye

Bours, J.; Doorenmaalen, W.J. van

doi:10.1016/0014-4835(72)90105-4

Cited by 27 publications

(6 citation statements)

References 31 publications

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“…The modern concept that lens antigens, which were once believed to be organ-specific are neither tissue-nor species-specific (Perkins and Wood, 1963;Clayton et al, 1968;Bours and Doorenmaalen, 1972) is compatible with the findings presented in this paper, which provide for the first time a rational explanation, at least in part, for the cross-reactivity of antilens sera. Almost every tissue in the body contains mitochondria, endoplasmic reticulum (i.e., the microsomes of the cell biochemist), nuclei, and contractile filaments and would be expected to cross-react with potent antisera produced against the lens homogenates, which for developmental reasons contain all these structures entrapped among the specific lens crystallins.…”

supporting

confidence: 88%

“…A number of investigators have reported that the lens antigens are present not only in other ocular structures (e.g., the iris, the retina, the cornea, the vitreous, and the aqueous humour) but also in extraocular tissues such as the brain, the skin, the 164 skeletal muscles, the liver, and the renal glomeruli (Hektoen, 1922;Rao et al, 1955;Maisel and Harmison, 1963a, b;Nozaki et al, 1963a, b;Perkins and Wood, 1963;Zwaan, 1963;Cate, 1964;Mehta et al, 1964;Rathburn et al, 1971;Bours and Doorenmaalen, 1972). It is not surprising, therefore, that Campbell et al (1968) found about 2 dozen electrophoretically distinct antigenic components within the lens, that all other tissues examined contained some antigenic determinants similar to those found in lens proteins, and that all of the major classes of lens proteins contained cross-reacting groups.…”

mentioning

confidence: 99%

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Immunopathology of the lens. I. Humoral and cellular immune responses to heterologous lens antigens and their roles in ocular inflammation.

Rahi¹,

Misra²,

Morgan³

1977

British Journal of Ophthalmology

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SUMMARY In experimental rabbits heterologous soluble lens proteins consisting of a-, 3-, and y-crystallins were found to be antigenic; they stimulated a marked antibody response compared to a rather weak T-cell response. The serum antibodies to ac-crystallins appeared first, to be followed by antibodies to 13-and y-crystallins in that order. The rabbits did not respond to heterologous y-crystallins unless these were injected with Freund's adjuvant containing mycobacteria. Incomplete Freund's adjuvant (i.e., without mycobacteria) was found to be an inferior immunoaccelerator so far as lens antigens are concerned. The response to lenticular antigens in both magnitude and duration varied in different rabbits, which suggested to us the important role played by a central control mechanism involving the immune response (Ir) genes.Some of the antibodies in potent lens antisera cross-reacted with mitochondria, endoplasmic reticulum (i.e., microsomes), contractile organelles, and cell nuclei. This explains for the first time at least in part the reasons for the widely observed phenomenon of the reactivity of lens antisera with ocular and extraocular structures. Antibodies to soluble lens proteins as detected by immunofluorescence and immunoperoxidase techniques were shown to be of the IgG class. Systemic heterologous immunisation followed by discission of the lens does not lead to the typical changes of phakoallergic endophthalmitis in the rabbit.

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supporting

confidence: 88%

mentioning

confidence: 99%

Immunopathology of the lens. I. Humoral and cellular immune responses to heterologous lens antigens and their roles in ocular inflammation.

Rahi¹,

Misra²,

Morgan³

1977

British Journal of Ophthalmology

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“…Although a direct comparison between the relative abundance levels of different crystallin polypeptides would depend on the relative titres and avidities of the antiserum for each polypeptide, the sequence of changes in relative amounts is clear (Figs. 8,9). During normal lens development, the anti-total crystallin antiserum detects a high level of &crystallin, and both a Aand a B-crystallin polypeptides but only trace levels of /?-crystallins at the 4 and 8 day stages.…”

Section: Resultsmentioning

confidence: 99%

Evidence for the extralenticular expression of members of the β-crystallin gene family in the chick and a comparison with δ-crystallin during differentiation and transdifferentiation

1991

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“…3). 3-Crystallin has been detected by immunological criteria in the chicken cornea (24,25). We show here by peptide sequencing the presence of the 81 polypeptide in the embryonic chicken cornea (Fig.…”

Section: Resultsmentioning

confidence: 99%

Taxon-specific recruitment of enzymes as major soluble proteins in the corneal epithelium of three mammals, chicken, and squid.

Cuthbertson

Tomarev

Piatigorsky

1992

Proc. Natl. Acad. Sci. U.S.A.

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Studies of others have shown that class 3 aldehyde dehydrogenase is a major component of the epithelial cells of the mammalian cornea. Here we demonstrate by peptide sequencing that other major proteins of the corneal epithelium are also identical or related to enzymes in the human, mouse, kangaroo, chicken, and squid. Aldehyde dehydrogenase class 3 was found to be the major protein of human, mouse, and kangaroo corneal epithelial cells. Peptidyl prolyl cis-trans isomerase (cyclophilin) or a homologue thereof is strikingly abundant in the corneal epithelial cells of chicken, but not mammals, and appears to be absent from the cornea of squid. By contrast, enolase or its homologue is relatively abundant in both the mammalian and chicken corneal epithelial cells. In some instances, abundant enzymes are common to cornea and lens in the same species-for example, arininosuccinate lyase/81-crystallin in the chicken and glutathione S-transferase-like protein in the squid; in other cases, the abundant proteins in the cornea have not been found as lens crystallins in any species-for example, aldehyde dehydrogenase class 3 and cyclophilin. These data suggest that enzymes and certain enzyme-crystallins have been recruited as major corneal proteins in a taxon-specific manner and may serve structural rather than, or as well as, enzymatic roles in corneal epithelial cells.

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The presence of lens antigens in the intra-ocular tissues of the chick eye

Cited by 27 publications

References 31 publications

Immunopathology of the lens. I. Humoral and cellular immune responses to heterologous lens antigens and their roles in ocular inflammation.

Immunopathology of the lens. I. Humoral and cellular immune responses to heterologous lens antigens and their roles in ocular inflammation.

Evidence for the extralenticular expression of members of the β-crystallin gene family in the chick and a comparison with δ-crystallin during differentiation and transdifferentiation

Taxon-specific recruitment of enzymes as major soluble proteins in the corneal epithelium of three mammals, chicken, and squid.

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