Evolution of eye lens crystallins: the stress connection

Jong, Wilfried W. de; Hendriks, Wiljan; Mulders, John W. M.; Bloemendal, H.

doi:10.1016/0968-0004(89)90009-1

Cited by 194 publications

(113 citation statements)

References 22 publications

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“…Or perhaps these enzymes have evolved other functions, like adhesion (Roseman 1970;Rauvala et al 1983;Shur 1983;Bayna et al 1988), or structure (like the enzymes that also function as lens crystallins; for review, see de Jong et al 1989), that are independent of now nonessential catalytic properties. Alternatively, it can be speculated that the catalytic activity of these enzymes is essential and that their oligosaccharide products maintain critical roles during development but are nonessential in the adult organism.…”

Section: Discussionmentioning

confidence: 99%

A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase.

Kukowska-Latallo¹,

Larsen²,

Nair³

et al. 1990

Genes Dev.

491

274

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The stage-specific embryonic antigen SSEA-I is a cell-surface oligosaccharide molecule expressed with temporal precision during the murine preimplantation period and implicated in adhesive events involving the process of compaction. We used a mammalian transient expression system to isolate a cloned human cDNA that determines expression of the SSEA-I molecule. The cDNA sequence predicts a type II transmembrane protein with a domain structure similar to mammalian glycosyltransferases, but without primary sequence similarity to these enzymes. The carboxy-terminal domain of this protein was shown to be catalytically active as a fucosyltransferase when expressed in COS-I cells as a portion of a secreted protein A fusion peptide. The enzyme is an exceptional glycosyltransferase in that it can use both type I and type II oligosaccharides as acceptor substrates to generate subterminal Fucc~(l,4)-and Fuc~(l,3)-linkages, respectively, in a manner analogous to the human Lewis blood group fucosyltransferase. Southern blot analysis shows that the cDNA corresponds to sequences syntenic to the Lewis locus on chromosome 19. These results indicate that this cDNA is the product of the human Lewis blood group locus, provide genetic confirmation of the hypothesis that this enzyme can catalyze two distinct transglycosylation reactions, and outline an approach to the isolation of other sequences that determine expression of developmentally regulated oligosaccharide antigens.

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Section: Discussionmentioning

confidence: 99%

A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase.

Kukowska-Latallo¹,

Larsen²,

Nair³

et al. 1990

Genes Dev.

491

274

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“…Finally, the recent finding that aB-crystallin confers cellular thermoresistance [22] left no doubt as to its being not only evolutionarilly, but also functionally a member of the sHSP family. The extra-lenticular expression of aAcrystallin has also been reported, but only at very low levels [23,24], and, in contrast to the aB-crystallin gene [25], no heat shock element has been identified in its promoter region, It was thus conceivable that between the two subunits, aBcrystallin had retained its function as a stress protein, whereas aA-crystallin had become adapted to function as a lens structural protein.…”

Section: Introductionmentioning

confidence: 99%

“…For the small heat shock proteins (sHSPs), which are ubiquitous and range in size from [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30], cellular thermoresistance provided by their overexpression has been reported [6][7][8]. A striking sequence similarity exists between the C-terminal parts of proteins belonging to this group of HSPs and the uA-and aB-crystallins [5,9].…”

Section: Introductionmentioning

confidence: 99%

αA‐crystallin confers cellular thermoresistance

et al. 1994

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The bovine eye lens protein aA-crystallin has been overexpressed both by stable transfection of HeLa cells and by transient transfection of NIH 3T3 cells. In both experimental systems aA-crystallin overexpression results in an increased cellular thermoresistance as judged by different clonal survival assays. In contrast, similar overexpression of another stable lens protein,BB2-crystallin, does not confer thermoresistance. These results indicate that the structural relationship of aA-crystallin to the small heat shock proteins HSP25127 and to aB-crystallin is sufficient for the shared thermoprotective function of all of these molecules and strongly suggests that the chaperone-like properties that they have in common are responsible for the conferred cellular thermoresistance.

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“…The diverse crystallins comprise 80-90% of the soluble protein of vertebrate lenses (4)(5)(6). The ubiquitous crystallins (the ␣-and the ␤͞␥-crystallins) are represented in all vertebrate lenses whereas the taxon-specific crystallins (also called enzymecrystallins because they are identical to or derived from metabolic enzymes) are limited to selected species (4,7).…”

mentioning

confidence: 99%

Adaptive evolution of small heat shock protein/ αB-crystallin promoter activity of the blind subterranean mole rat,Spalax ehrenbergi

Hough

Avivi

Davis

et al. 2002

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

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Blind mole rats have degenerated subcutaneous eyes that are visually nonfunctional. In this investigation, we have compared the tissue specificity of the small heat shock protein (shsp)͞␣B-crystallin promoter of the mole rat superspecies, Spalax ehrenbergi, with that of the mouse. Earlier experiments showed that mouse shsp͞ ␣B-crystallin promoter͞enhancer activity is high in the lens and moderate in the heart and skeletal muscle of transgenic mice. Here, we show in transgenic mouse experiments using the firefly luciferase reporter gene that, despite relatively few changes in sequence, the mole rat shsp͞␣B-crystallin promoter͞enhancer has selectively lost lens activity after 13.5 days of embryogenesis (E13.5). The ratios of mole rat͞mouse promoter activity were 0.01 for lens, 1.7 for heart, and 13.6 for skeletal muscle in 8-wk-old transgenic mice. Our data indicate that the shsp͞␣B-crystallin promoter͞enhancer has undergone adaptive changes corresponding to the subterranean evolution of the blind mole rat. We speculate that selective pressures on metabolic economy may have contributed to these tissue-specific modifications of promoter͞ enhancer function during adaptation to life underground.

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Evolution of eye lens crystallins: the stress connection

Cited by 194 publications

References 22 publications

A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase.

A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase.

αA‐crystallin confers cellular thermoresistance

Adaptive evolution of small heat shock protein/ αB-crystallin promoter activity of the blind subterranean mole rat,Spalax ehrenbergi

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