The relationship between the ontogeny of antigens and of the polypeptide chains of the crystallins during chick lens development

Truman, D. E. S.; Brown, Gene M.; Campbell, John C.

doi:10.1016/0014-4835(72)90125-x

Cited by 28 publications

(6 citation statements)

References 23 publications

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“…The major proteins of the lens are the crystallins (Clayton, 1974;Bloemendal & de Jong, 1979), which appear, on the basis of immunological evidence, to belong to four families of lens-specific proteins, of which the a, ,f and y are found in mammals and amphibians, and the a, ,B and are found in birds and at least some reptiles (Clayton, 1974). In chick lens, the first crystallin to appear in abundance in development is the (Rabaey, 1962;Truman et al, 1972;Piatigorsky et al, 1976), and in the day-old chick, b-crystallin mRNA comprises about 20% of the total poly(A)-containing RNA in the lens (Jackson et al, 1978;Thomson et al, 1978b). Chick b-crystallin cDNA and genomic clones have already been constructed by other workers (Bhat & Piatigorsky, 1979;Bhat et al, 1980), and partly characterized by restriction enzyme analysis and genomic DNA blots; it has been shown that there are probably only two, non-allelic, c-crystallin genes.…”

mentioning

confidence: 99%

Cytoplasmic RNA sequences complementary to cloned chick δ-crystallin cDNA show size heterogeneity.

Bower¹,

Errington²,

Wainwright³

et al. 1982

Biochemical Journal

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Double-stranded complementary DNA (cDNA) sequences were prepared from day-old chick lens total polysomal RNA and inserted into the unique PstI restriction site of the plasmid pBR322. Colonies containing sequences complementary to abundant lens poly(A)-containing RNA sequences were identified by using lens 32P-labelled cDNA. Some of these clones have been characterized as containing delta-crystallin mRNA coding sequences by genomic DNA blot hybridization and RNA blot hybridizations. Hybridization of labelled DNA from such clones to RNA blots detected four size classes of delta-crystallin RNA sequences, although Southern blots indicated that there are probably only two delta-crystallin genes.

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mentioning

confidence: 99%

Cytoplasmic RNA sequences complementary to cloned chick δ-crystallin cDNA show size heterogeneity.

Bower¹,

Errington²,

Wainwright³

et al. 1982

Biochemical Journal

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“…The presence of separate components of FISC at isofocusing should not be considered as an artifact of the method as was presumed by CRAIG & PIATIGORSKY (1973), since (1) no chemical modification of the protein or differential binding of Ampholine carrier ampholytes to proteins takes place (HAYES & WELLNER, 1969;RIGHETTI & DRYSDALE, 1971); (2) neither photopolymerization with riboflavin (WRIGLEY, 1970) nor differences in composition of the polyacrylamide gel influence the isoelectric focusing of proteins (HAGLUND, 1971); (3) denaturation is not observed with lens proteins at isofocusing and (4) gross similarity of patterns obtained by starch gel electrophoresis (TRUMAN et al, 1972) and isoelectric focusing of chick lens crystallins is observed (BRAHMA, BOURS & VAN DOORENMAALEN, 1971;BOURS, 1973a). At isofocusing of chick lens crystallins the FISC shows 7 components because of a better resolution, while starch gel electrophoresis shows the same protein as one band.…”

Section: B Fisc (First Hnportant Sohtble Ct2vstallin)mentioning

confidence: 99%

“…In fact, ~-crystallin is a better name, since these crystallins are immunologically related to bovine ~-crystallins (ZWAAN, 1966). LAURELL'S two-dimensional antigen/antibody crossed electrophoresis (BRAHMA et al, 1971 ;TRUMAN et al, 1972;]]OURS & VAN DOORENMAALEN, 1972) shows at least 3 to 4 distinct immunoprecipitin curves, thus contributing to the complexity of the pattern of the ~-crystallins. At isofocusing at least 10 ~-crystallin components can be observed.…”

Section: ~-Crystallinsmentioning

confidence: 99%

“…In early embryonic stages of lens formation FISC appears after 3 days (RAUAEY, 1962), which was later determined at 2.5 days by ZWAAN & ~KEDA (1965) and confirmed as such by BRAHMA & VAN DOORENMAALEN (1971). It appears, from the composition of the embryonic lens during development as shown by quantitative immunoelectrophoresis by TRUMAN et al (1972), that in embryonic stages younger than 4 days the proportion of FISC protein comprises more than 90 o/[, of the total crystallin content, which declined to 36 o/s at 6 weeks after hatching. , 1973).…”

Section: Changes Hi Embryonic Lens Cwstallins D Rolg Derelopmentmentioning

confidence: 99%

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Isoelectric focusing and immunochemistry of lens crystallins

Bours

1974

Doc Ophthalmol

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This is a review of 11 published articles with some conclusive results on the isoelectric focusing and immunochemistry of lens crystallins. The techniques used throughout the work are isoelectric focusing and immunological methods.The isoelectric focusing technique is performed on an analytical scale to realize the separation of proteins by isoelectric focusing in thin-layer polyacrylamide gels. The importance of carrying out all isofocusing techniques at 4 ~ C, and also of measuring the pH gradients established at the same temperature is noticed. Free isoelectric focusing is used as a preparative step to isolate uncontaminated crystallin fractions. Both analytical and preparative isoelectric focusing experiments of crystallins performed throughout the work are in absence of urea or any other dissociating medium.The purity of proteins isolated by free iseelectric focusing is examined by criteria of homogeneity which are founded on three different techniques, e.g. thin-layer isoelectric focusing, immunoelectrophoresis and antigen/antibody crossed electrophoresis.The existence of various crystallins in the chick lens, like ~z-, ~-crystallin and FISC, related to own data, is reviewed and nomenclatures of chick lens crystallins are compared with present data from literature. The antigenic properties of proteins from chick intra-ocular tissues are also discussed. Anti-total iris serum contains antibodies against crystallins and serum proteins. The presence of proteins immunologically identical to lens crystallins in chick iris is shown by indirect immunofluorescence experiments: brilliant fluorescence of the lens is observed due to the presence of crystallin antibodies in anti-total iris serum. It is concluded that proteins of all intra-ocular tissues which are immunologically identical to lens crystallins are essential structural elements. Contrary to this statement several authors support the theory that the presence of proteins immunologically identical to lens crystallins in the intra-ocular tissues is due to a post-mortem diffusion of these antigens from the lens. The presence of several erum proteins in all intra-ocular tissues excepting lens is shown. Evidence is presented that the number of serum proteins in intra-ocular tissues is restricted by the various blood/ocular barriers, and that the blood/retinal barrier is of the same nature as the blood/brain barrier.The presence ~-, ~-, ,,,-and pre-~-crystallins is shown in various stages of the bovine embryonic lens by thin-layer isoelectric focusing and various immunological methods. It is defined that the bovine -~,-crystallins have isoelectric points higher than pI --7.0. It is shown by immuno-osmophoresis that the embryonic ~-crystallins consist of two molecular forms with different electrophoretic mobilities. The ~-crystallins are forming half the total amount of the crystallins present in the embryonic lens. It is concluded that the "c-crystallins are more prominent in embryonic cow lens and in adult lens nucleus and less prominent in adult lens cortex. The...

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“…This was repeated after 3 weeks, and 10 days after the third injection serum was collected from the marginal ear vein and tested by immunoelectrophoresis (Scheidegger, 1955) and two-dimensional crossed electrophoresis (Laurell, 1965;Clarke and Freeman, 1968) with the modifications of Truman, Brown and Campbell (1972) against pigeon total lens extract.…”

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confidence: 99%

Ontogeny and localization of γ-crystallin antigen in the developing pigeon (Columba livia) lens

Brahma

Rabaey

Doorenmaalen

1972

Experimental Eye Research

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Ontogeny and localization of the lens y-crystallin antigen were investigated in the embryonic and post-embryonic pigeon lenses by the indirect immunofluorescence with antiserum from rabbit immunized with isolated pigeon lens y-crystallin. The results show that y-crystallin appears for the first time in a 4-day embryonic lens and is distributed uniformly over the entire fibre cells. In a late and also post-embryonic lens y-crystallin was also detected in the epithelium and annular pad areas and the intensities of immunofluorescent reaction gradually increased from embryonic to post-embryonic lens.

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The relationship between the ontogeny of antigens and of the polypeptide chains of the crystallins during chick lens development

Cited by 28 publications

References 23 publications

Cytoplasmic RNA sequences complementary to cloned chick δ-crystallin cDNA show size heterogeneity.

Cytoplasmic RNA sequences complementary to cloned chick δ-crystallin cDNA show size heterogeneity.

Isoelectric focusing and immunochemistry of lens crystallins

Ontogeny and localization of γ-crystallin antigen in the developing pigeon (Columba livia) lens

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