Lens-preferred activity of chicken δ1- and δ2-crystallin enhancers in transgenic mice and evidence for retinoic acid-responsive regulation of the δ1-crystallin gene

Li, Xuan; Cvekl, Aleš; Bassnett, Steven; Piatigorsky, Joram

doi:10.1002/(sici)1520-6408(1997)20:3<258::aid-dvg8>3.0.co;2-6

Cited by 30 publications

(11 citation statements)

References 44 publications

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“…Transgenic mouse experiments have established that the lenspreferred activity of vertebrate crystallin promoters is transcriptionally controlled (67)(68)(69)(70)(71) and often species-independent (13)(14)(15)(16)(17)(18). Various attempts to find common cis-regulatory sequences among different crystallin promoters/enhancers accounting for their high lens expression have advanced our knowledge but have not been entirely successful (72)(73)(74).…”

Section: Discussionmentioning

confidence: 99%

“…If correct, one might expect to find similar transcription factors utilized for high expression of different crystallin genes in the lens. This idea is supported by experiments using transgenic mice showing the conservation of preferential lens activity of numerous crystallin promoters across vertebrate species (13)(14)(15)(16)(17)(18). Comparisons between regulatory sequences associated with different crystallin genes of vertebrates have revealed a group of ubiquitous transcription factors (AP-1, USF, CREB, and Sp1) as well as other more specialized factors like Pax-6, Maf, Sox, retinoic acid receptor/ RXR, and ␣ACRYBP1 (19 -23).…”

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confidence: 96%

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Structure and Expression of the Scallop Ω-Crystallin Gene

Carosa¹,

Kozmík²,

Rall³

et al. 2002

Journal of Biological Chemistry

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⍀-Crystallin of the scallop lens is an inactive aldehyde dehydrogenase (1A9). Here we have cloned the scallop ⍀-crystallin gene. Except for an extra novel first exon, its 14-exon structure agrees well with that of mammalian aldehyde dehydrogenases 1, 2, and 6. The ؊2120/ ؉63, ؊714/؉63, and ؊156/؉63 ⍀-crystallin promoter fragments drive the luciferase reporter gene in transfected ␣TN4-1 lens cells and L929 fibroblasts but not in Cos7 cells. Putative binding sequences for cAMPresponsive element-binding protein (CREB)/Jun, ␣ACRYBP1, AP-1, and PAX-6 in the ⍀-crystallin promoter are surprisingly similar to the cis-elements used for lens promoter activity of the mouse and chicken ␣A-crystallin genes, which encode proteins homologous to small heat shock proteins. Site-specific mutations in the overlapping CREB/Jun and Pax-6 sites abolished activity of the ⍀-crystallin promoter in transfected cells. Gel shift experiments utilizing extracts from the ␣TN4-1, L929, and Cos7 cells and the scallop stomach and oligonucleotides derived from the putative binding sites of the ⍀-crystallin promoter showed complex formation. Gel shift experiments showed binding of recombinant Pax-6 and CREB to their respective sites. Our data suggest convergent evolutionary adaptations that underlie the preferential expression of crystallin genes in the lens of vertebrates and invertebrates.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 96%

Structure and Expression of the Scallop Ω-Crystallin Gene

Carosa¹,

Kozmík²,

Rall³

et al. 2002

Journal of Biological Chemistry

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“…Here we report a close homologue of vertebrate RXRs that binds 9-cis-retinoic acid as a ligand and also binds a vertebrate consensus DNA response element in one of the most primitive Cnidarian jellyfish Tripedalia cystophora. We also show that this jellyfish RXR (jRXR) binds to potential regulatory element of crystallin gene expressed highly in the eye lens of T. cystophora (14), raising the possibility that retinoid signaling is used for eye development and crystallin gene expression in invertebrates as it is in vertebrates (15)(16)(17)(18)(19)(20)(21)(22).…”

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confidence: 93%

Retinoic acid X receptor in the diploblast, Tripedalia cystophora

Kostrouch

Love

Jannini

et al. 1998

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

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132

104

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Nuclear hormone receptors comprise a characteristic family of transcription factors found in vertebrates, insects and nematodes. Here we show by cDNA and gene cloning that a Cnidarian, Tripedalia cystophora, possesses a retinoid receptor (jRXR) with remarkable homology to vertebrate retinoic acid X receptors (RXRs). Like vertebrate RXRs, jRXR binds 9-cis retinoic acid (K d ‫؍‬ 4 ؋ 10 ؊10 M) and binds to the DNA sequence, PuGGTCA as a monomer in vitro. jRXR also heterodimerizes with Xenopus TR beta on a thyroid responsive element of a direct repeat separated by 4 bp. A jRXR binding half-site capable of interacting with (His 6 )jRXR fusion protein was identified in the promoters of three T. cystophora crystallin genes that are expressed highly in the eye lens of this jellyfish. Because crystallin gene expression is regulated by retionoid signaling in vertebrates, the jellyfish crystallin genes are candidate in vivo targets for jRXR. Finally, an antibody prepared against (His 6 )jRXR showed that fulllength jRXR is expressed at all developmental stages of T. cystophora except the ephydra, where a smaller form replaces is. These data show that Cnidaria, a diploblastic phylum ancestral to the triploblastic invertebrate and subsequent vertebrate lineages, already have an RXR suggesting that RXR is an early component of the regulatory mechanisms of metazoa.

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“…RA has been shown to activate the ␦1-crystallin gene in stably transformed mouse teratocarcinoma stem cells (64) and in cultured lens epithelial cells from newly hatched chickens (17). Recent cotransfection experiments using reporter genes in recombinant plasmids have provided more direct evidence implicating retinoic acid receptors in the control of the chicken ␦1-crystallin gene (14). Unlike the and pRSVRXR␤ (wild type RAR␤ and RXR␤ cDNAs, respectively) and either p11-3 (wild type Ϫ115/ϩ44 ␣B-crystallin promoter fragment fused to cat gene) or p65-7 (wild type Ϫ164/ϩ44 ␣B-crystallin promoter fragment fused to cat gene).…”

Section: Resultsmentioning

confidence: 99%

“…While no one cis-control element or transcription factor is solely responsible for the high lens expression of the crystallin genes, Pax-6 (8 -11) and retinoic acid (RA) 1 (12)(13)(14) appear to have prominent roles. This is consistent with the critical use of these transcription factors for eye and lens development (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28).…”

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confidence: 99%

Involvement of Retinoic Acid/Retinoid Receptors in the Regulation of Murine αB-crystallin/Small Heat Shock Protein Gene Expression in the Lens

Gopal-Srivastava

Cvekl

Piatigorsky

1998

Journal of Biological Chemistry

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Crystallins are a diverse group of abundant soluble proteins that are responsible for the refractive properties of the transparent eye lens. We showed previously that Pax-6 can activate the ␣B-crystallin/small heat shock protein promoter via the lens-specific regulatory regions LSR1 (؊147/؊118) and LSR2 (؊78/؊46). Here we demonstrate that retinoic acid can induce the accumulation of ␣B-crystallin in N/N1003A lens cells and that retinoic acid receptor heterodimers (retinoic acid receptor/retinoid X receptor; RAR/RXR) can transactivate LSR1 and LSR2 in cotransfection experiments. DNase I footprinting experiments demonstrated that purified RAR/RXR heterodimers will occupy sequences resembling retinoic acid response elements within LSR1 and LSR2. Electrophoretic mobility shift assays using antibodies indicated that LSR1 and LSR2 can interact with endogenous RAR/RXR complexes in extracts of cultured lens cells. Pax-6 and RAR/RXR together had an additive effect on the activation of ␣B-promoter in the transfected lens cells. Thus, the ␣B-crystallin gene is activated by Pax-6 and retinoic acid receptors, making these transcription factors examples of proteins that have critical roles in early development as well as in the expression of proteins characterizing terminal differentiation.The refractive properties of the transparent eye lens depend on a diverse group of globular proteins called crystallins that comprise approximately 90% of the water-soluble proteins of this tissue (1, 2). Despite their specialized function in the lens, crystallins are surprisingly diverse and may differ among species. Moreover, crystallins often play more than one biological role, a situation called gene sharing (3), with many being related or identical to metabolic enzymes or stress proteins (4 -6). These multifunctional crystallins are expressed very highly in the lens and to a lesser extent in other tissues, where they have nonrefractive roles.The molecular basis for the specialized expression of crystallin genes has been investigated for some time (7). While no one cis-control element or transcription factor is solely responsible for the high lens expression of the crystallin genes, Pax-6 (8 -11) and retinoic acid (RA) 1 (12-14) appear to have prominent roles. This is consistent with the critical use of these transcription factors for eye and lens development (15-28).We have been studying mouse ␣B-crystallin, a conserved small heat shock protein (29, 30) that is constitutively expressed highly in the lens and more moderately in many other tissues (31, 32). ␣B-crystallin is also induced by stress (33) and overexpressed in numerous diseases (34, 35). The differential constitutive expression of the murine ␣B-crystallin gene is developmentally and transcriptionally controlled (32, 36, 37). Transgenic mouse experiments have established that the sequences downstream of Ϫ164 are sufficient to direct lens-specific gene expression (38). This 5Ј-flanking sequence contains two lens-specific regulatory regions called LSR1 (Ϫ147/Ϫ118) and LSR2 (Ϫ78/...

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Lens-preferred activity of chicken δ1- and δ2-crystallin enhancers in transgenic mice and evidence for retinoic acid-responsive regulation of the δ1-crystallin gene

Cited by 30 publications

References 44 publications

Structure and Expression of the Scallop Ω-Crystallin Gene

Structure and Expression of the Scallop Ω-Crystallin Gene

Retinoic acid X receptor in the diploblast, Tripedalia cystophora

Involvement of Retinoic Acid/Retinoid Receptors in the Regulation of Murine αB-crystallin/Small Heat Shock Protein Gene Expression in the Lens

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