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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present study examined the effects of aging and cataractogenesis on the biochemical properties of the uniquely heat-stable lens crystallin, beta basic principle polypeptide (beta Bp). Using the techniques of SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Western-blot immunoassay, we analyzed cortical and nuclear lens sections from normal lenses of individuals aged 0 to 91 years for beta Bp content in the soluble fraction, and retention of heat stability with aging. In addition, we compared the characteristics of beta Bp in cataractous lenses with those of normal lenses of approximately the same age. While beta Bp is synthesized in new cortical cells throughout life, the beta Bp of the nucleus, which had been laid down early in life, decreased significantly in both absolute concentration and in its proportion of the total soluble protein fraction during the normal aging process. In addition, posttranslational changes in the nuclear soluble beta Bp result in a gradual loss of approximately 3000 d in the apparent mass of the beta Bp molecule; i.e., as a result of the aging process, the single heat-stable band of an apparent mass of 26 kd on SDS-PAGE of the young lens nucleus becomes two heat-stable bands, one at 26 kd and one at 23 kd. Normal lenses up to 91 years of age always retain some of the 26 kd subunit, whereas lenses with severe nuclear cataracts had only the 23 kd subunit in the soluble fraction.
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PMID:Age-dependent changes in the heat-stable crystallin, beta Bp, of the human lens. 372 Mar 46

Three classes of monomeric crystallins separable by SDS gel electrophoresis or by gel filtration have been demonstrated in human lens. In previous studies we have concluded from physico-chemical and immunological data that all three polypeptides are related and should be classified as gamma-crystallins. The present paper presents further evidence supporting this conclusion, but also demonstrates that the 24,000 dalton (24kD) polypeptide corresponds to the beta s-crystallin. beta s-crystallin was purified by classical techniques from bovine lens and was shown to cross-react with a monoclonal antibody specific for the human 24kD polypeptide. This antibody exhibited no reactivity to other crystallin fractions from either bovine or human lenses. The identification of the 24kD polypeptide as beta s was further supported by analysis of the tertiary structures of the molecules by near UV-circular dichroism and by the finding of a blocked amino terminus on the 24kD polypeptide. Our finding that the human beta s (24kD polypeptide) should actually be classified as a gamma-crystallin is fully consistent with recently reported sequence data on bovine beta s-crystallin.
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PMID:Further studies on low molecular weight crystallins: relationship between the bovine beta s, the human 24kD protein and the gamma-crystallins. 372 Mar 47

The 11-day embryonic chicken lens displays a rapid and vigorous response to a heat shock. Exposure of the lens to elevated temperature (45 degrees C) dramatically increased the synthesis of three proteins with subunit molecular weights of 89,000, 70,000 and 24,000. These lens heat-shock proteins are identical to the heat-shock proteins of cultured chicken embryo fibroblasts in electrophoretic mobility and immunological cross-reactivity. Maximum induction of lens heat-shock protein synthesis occurred upon incubation at 45 degrees C for about 1-1.5 hr and was blocked in the presence of actinomycin D. The functional half-lives at 37 degrees C of the mRNAs encoding the lens heat-shock proteins were about 3-5 hr. Synthesis of normal lens proteins continued throughout the heat shock, but delta-crystallin was unusual in that its synthesis initially rose upon heat shock, a behavior similar to that of a heat-shock protein. Proteins which co-migrated with each of the major lens heat-shock proteins were detected immunologically in non-stressed lens extracts. The endogenous lens protein, p24, which cross-reacted with antibodies raised against the small heat-shock protein (hsp 24) from chicken-embryo fibroblasts and co-migrated in one dimensional SDS gels with a major beta-crystallin was shown to be structurally similar to the chicken small heat shock protein but was distinct from the beta-crystallins.
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PMID:Induction of heat-shock proteins in the embryonic chicken lens. 373 14

Intumescent cataractous lenses were investigated as to their water content and protein composition. Nuclei were separated from cortices. Water-soluble, water-insoluble, urea-soluble and urea-insoluble portions were quantified and the subunit composition of the water-soluble crystallin fraction was looked at on SDS-gel electrophoresis. Compared to normal lenses it is observed that the water content in intumescent cataract is increased, water-soluble and urea-soluble fractions are diminished, whereas the urea-insoluble portions are augmented. No major changes are noted in the subunit composition of the soluble protein fractions. Particularly, the relative amount of gamma-crystallins is diminished in intumescent cataractous lenses.
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PMID:Lens proteins in intumescent cataract. 373 13

Previous studies have shown that there are 2 similar delta-crystallin genes (delta 1 and delta 2) and at least 2 delta-crystallin polypeptides in the chicken eye lens. We show here that both delta-crystallin polypeptides can be synthesized from mRNA transcribed in vitro from a cloned delta 1-crystallin cDNA. Both polypeptides co-migrate in SDS-urea-polyacrylamide electrophoresis with their authentic counterparts isolated from 15-day-old embryonic chicken lenses, and both react with sheep anti-chicken delta-crystallin serum. Screening nearly 900 delta-crystallin cDNA clones from a 15-day-old embryonic lens library with an oligonucleotide probe specific for exon 2 of the delta 2-crystallin gene failed to detect any delta 2 cDNA clones, indicating that the delta 2 gene produces little or no mRNA in the lens at this stage of development. Our results suggest that both of the observed delta-crystallin polypeptides are derived from mRNA transcribed from the delta 1 gene, with heterogeneity arising at the translational or co-translational level.
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PMID:Two delta-crystallin polypeptides are derived from a cloned delta 1-crystallin cDNA. 375 87

The epsilon-crystallin polypeptide is a recently described protein in the eye lens of the peking duck, Anas platyrhynchos. It does not cross react with alpha-, beta-, delta-, and gamma-crystallins. It has a molecular weight of 120K and consists of 3 identical 38K polypeptides. It is found in some reptiles and birds. The ontogeny of this polypeptide has been investigated in the developing A. platyrhynchos lens via the indirect immunofluorescence staining using a homologous antibody. The 38K polypeptide was extracted from 13% Tris-SDS acrylamide gels, lyophilized and injected into a young rabbit to raise an antibody. The purity of the isolated 38K polypeptide and and the specificity of the antibody were checked by Tris-SDS gel electrophoresis and immunoblotting, respectively. The first positive reaction is detected at 80 h (stage 18) incubated lens. It is confined to a few elongating early primary fibres. Until the 9th day of development the reaction is confined to the primary and secondary lens fibres. The first positive reaction in the annular pad area is observed in the "day 10" lens. In the anterior epithelium the first positive reaction is detectable in the "day 12" lens. At the beginning it is confined to a few cells in the center of the epithelium and gradually the reaction spreads to other cells. A strong and uniform reaction in the entire epithelium is noted for the first time in the lens of a just-hatched duckling. The 38K epsilon-polypeptide is detectable after the alpha-, beta-, and delta-crystallins, which, in the duck, appear simultaneously from 66 h (stage 15/16).
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PMID:Ontogeny of the 38K epsilon-polypeptide during lens development of the duck Anas platyrhynchos. 389 55

The proteins of the Rhesus monkey (Macaca mulatta) lens were studied and characterized. In general, there is a similarity of the monkey lens to the human lens particularly in the alpha- and beta-crystallins and the membrane proteins, although the amount of beta 1-crystallin may be greater in the monkey. There is immunological cross-reactivity in the crystallins between monkey and human lenses including the monkey low molecular weight proteins and the human low molecular weight proteins. The monkey lens low molecular weight material showed three differently sized proteins by gel exclusion chromatography. In this respect, the monkey lens proteins are similar to the human. However, the monkey lens low molecular weight proteins differ from the human low molecular weight proteins in charge as well as molecular weight determined by SDS-PAGE. One of the monkey low molecular weight proteins is more prevalent in the nucleus than in the cortex suggesting that this protein may be more important to the embryonic lens that to the adult lens.
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PMID:Analysis of the proteins in the rhesus monkey lens. 393 94

Developmental regulation of crystallin protein synthesis was observed in rat lenses between embryonic day 19 and postnatal day 21. Studies on lenses incubated in [35S]-methionine and on lens messenger RNAs translated in a reticulocyte lysate showed that several new polypeptides were synthesized in the lens beginning approximately 1 week after birth. One new polypeptide which had a molecular weight of 27 000 comigrated with the beta crystallins on SDS-PAGE and became a predominant component in older lenses. By crossed rocket immunoelectrophoresis and isoelectric focusing, synthesis of several native beta crystallins and one gamma crystallin was detected only in the postnatal lens. Many crystallin proteins were synthesized in the embryonic and the postnatal lens and did not change during the time period studied. These data suggest a differential regulation of the crystallin proteins during development. It appears that the lens undergoes a transition from embryonic to adult crystallin expression during the first weeks after birth. Factors such as maturation of the retina may be necessary for this transition.
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PMID:Differential synthesis of rat lens proteins during development. 397 59

The lens proteins from three lines of congenic mice which are homozygous for the gene retinal degeneration (rd) or retinal degeneration slow (rds) or carrying the normal alleles (normal) were analyzed by SDS-PAGE and by immunological reactivity to specific monoclonal antibodies. The lens proteins of normal, rd, and rds mice showed a similar developmental pattern between postnatal day 0 and postnatal day 30. The expression of the 25000 molecular weight (MW) beta-crystallin polypeptide which appears postnatally in the normal lens was not affected by retinal abnormalities in the mutant mice. It is concluded that the regulation of the 25000 MW beta-crystallin polypeptide is not dependent upon differentiation or maintenance of the photoreceptor outer segments or continued presence of the photoreceptor cells.
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PMID:Comparison of the lens crystallin proteins from normal, rd, and rds mutant mice utilizing specific monoclonal antibodies. 400 83

The soluble proteins from prenatal and neonatal human lenses were fractionated by gel filtration into four distinct size classes viz. high molecular weight alpha-crystallin (HM-alpha), alpha-crystallin, intermediate molecular weight (IMW) proteins and low molecular weight (LMW) proteins. Extinction coefficients of the isolated proteins were determined and used to calculate the proportions of each fraction on a weight basis. The distributions of polypeptides within each of these fractions were analyzed by SDS gel electrophoresis and isoelectric focussing, followed by densitometric scanning of the gels. HM-alpha is detectable as early as the 14th week of gestation and its proportions increase rapidly, to about 9% of the total protein in the 1 year postnatal lens. The alpha-crystallin, IMW and LMW fractions show concomitant decreases and by 1 year they represent about 34, 35 and 18%, respectively. However, the proportions of IMW and LMW proteins do not accurately reflect those of the beta- and gamma-crystallins, as is often assumed. Substantial levels of non-crystallin polypeptides were found in the IMW protein fractions, including a group of very basic polypeptides (VBP) which comprised up to one-third of this material in the youngest lenses. Moreover, in postnatal lenses beta s-crystallin accounted for almost half of the LMW proteins. These points considered, alpha-crystallin is the major protein in the neonatal lens (approximately 42%, including HM-alpha), followed by the beta-crystallin (approximately 36% at most and probably less), the gamma-crystallins (approximately 11%) and beta s-crystallin (approximately 9%). Substantial changes in the proportions of specific polypeptides were observed throughout early development. These appear to result from changes at the level of protein synthesis and from postsynthetic modification. The A:B subunit ratio of alpha-crystallin drops from about 12 to below 3 during early development. This coincides with increasing levels of various deamidated and degraded subunits. The major beta-crystallin polypeptide also undergoes rapid deamidation and evidence is presented suggesting that the gamma-crystallins are subject to similar modification. The most dramatic changes were observed in the constituents of the LMW proteins. The synthesis of gamma-crystallins virtually ceases at some time around birth. At the same time, the levels of beta s-crystallin undergo an explosive increase. These and other changes are discussed in terms of their possible functional significance. They are also related to the complex protein status found in old lenses.
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PMID:Ontogeny of human lens crystallins. 406 34


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