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Volumn 3, Issue 1-4, 2003, Pages 131-137

Crystallin genes: Specialization by changes in gene regulation may precede gene duplication

Author keywords

Crystallins; Enzyme crystallins; Gene regulation; Gene sharing; Lens evolution; Pax 6; Small heat shock proteins

Indexed keywords

ARGININOSUCCINATE LYASE; CRYSTALLIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; DELTA CRYSTALLIN; ENOLASE; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN; LACTATE DEHYDROGENASE; RETINOIC ACID RECEPTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR PAX6;

EID: 0037270166     PISSN: 1345711X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022626304097     Document Type: Article
Times cited : (68)

References (44)
  • 1
    • 0037016680 scopus 로고    scopus 로고
    • Structure and expression of the scallop Ω-crystallin gene: Evidence for convergent evolution of promoter sequences
    • Carosa, E., Kozmik, Z., Rall, J.E. and Piatigorsky, J. (2002) Structure and expression of the scallop Ω-crystallin gene: evidence for convergent evolution of promoter sequences. J. Biol. Chem., 277, 656-664.
    • (2002) J. Biol. Chem. , vol.277 , pp. 656-664
    • Carosa, E.1    Kozmik, Z.2    Rall, J.E.3    Piatigorsky, J.4
  • 2
    • 0030219742 scopus 로고    scopus 로고
    • Lens development and crystallin gene expression: Many roles for Pax-6
    • Cvekl, A. and Piatigorsky, J. (1996) Lens development and crystallin gene expression: many roles for Pax-6. BioEssays, 18, 621-630.
    • (1996) BioEssays , vol.18 , pp. 621-630
    • Cvekl, A.1    Piatigorsky, J.2
  • 4
    • 0027472047 scopus 로고
    • Evolution of the α-crystallin/small heat-shock protein family
    • de Jong, W.W., Leunissen, J.A.M. and Voorter, C.E.M. (1993) Evolution of the α-crystallin/small heat-shock protein family. Mol. Biol. Evol., 10, 103-126.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.M.2    Voorter, C.E.M.3
  • 6
    • 0029893374 scopus 로고    scopus 로고
    • Developmental regulation of the chicken βB1-crystallin promoter in transgenic mice
    • Duncan, M.K., Li, X., Ogino, H., Yasuda, K. and Piatigorsky, J. (1996) Developmental regulation of the chicken βB1-crystallin promoter in transgenic mice. Mech. Dev., 57, 79-89.
    • (1996) Mech. Dev. , vol.57 , pp. 79-89
    • Duncan, M.K.1    Li, X.2    Ogino, H.3    Yasuda, K.4    Piatigorsky, J.5
  • 7
    • 0033198374 scopus 로고    scopus 로고
    • Pax6 mastering eye morphogenesis and eye evolution
    • Gehring, W.J. and Ikeo, K. (1999) Pax6 mastering eye morphogenesis and eye evolution. Trends Genet., 15, 371-377.
    • (1999) Trends Genet. , vol.15 , pp. 371-377
    • Gehring, W.J.1    Ikeo, K.2
  • 8
    • 0024095133 scopus 로고
    • Duck lens e-crystallin and lactate dehydrogenase B4 are identical: A single-copy gene product with two distinct functions
    • Hendriks, W., Mulders, J.W.M., Bibby, M.A., Slingsby, C., Bloemendal, H. and de Jong, W.W. (1988) Duck lens e-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions. Proc. Natl. Acad. Sci. USA, 85, 7114-7118.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7114-7118
    • Hendriks, W.1    Mulders, J.W.M.2    Bibby, M.A.3    Slingsby, C.4    Bloemendal, H.5    De Jong, W.W.6
  • 9
    • 0026483279 scopus 로고
    • α-crystallin can function as a molecular chaperone
    • Horwitz, J. (1992) α-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA, 89, 10449-10453.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 10
    • 0033538341 scopus 로고    scopus 로고
    • Regulation of αA-crystallin gene expression. Lens specificity achieved through the differential placement of similar transcriptional control elements in mouse and chicken
    • Ilagan, J.G., Cvekl, A., Kantorow, M., Piatigorsky, J. and Sax, C.M. (1999) Regulation of αA-crystallin gene expression. Lens specificity achieved through the differential placement of similar transcriptional control elements in mouse and chicken. J. Biol. Chem., 274, 19973-19978.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19973-19978
    • Ilagan, J.G.1    Cvekl, A.2    Kantorow, M.3    Piatigorsky, J.4    Sax, C.M.5
  • 11
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin
    • Ingolia, T.D. and Craig, E.A. (1982) Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc. Natl. Acad. Sci. USA, 79, 2360-2364.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 15
    • 0030745384 scopus 로고    scopus 로고
    • 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, X., Cvekl, A., Bassnett, S. and Piatigorsky, J. (1997) 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. Dev. Genet., 20, 258-266.
    • (1997) Dev. Genet. , vol.20 , pp. 258-266
    • Li, X.1    Cvekl, A.2    Bassnett, S.3    Piatigorsky, J.4
  • 17
    • 0029886088 scopus 로고    scopus 로고
    • Lens-specific expression of a chicken βA3/A1-crystallin promoter fragment in transgenic mice
    • McDermott, J.B., Cvekl, A. and Piatigorsky, J. (1996) Lens-specific expression of a chicken βA3/A1-crystallin promoter fragment in transgenic mice. Biochem. Biophy. Res. Comm., 221, 559-564.
    • (1996) Biochem. Biophy. Res. Comm. , vol.221 , pp. 559-564
    • McDermott, J.B.1    Cvekl, A.2    Piatigorsky, J.3
  • 18
    • 0026705801 scopus 로고
    • The muscle-derived lens of a squid bioluminescent organ is biochemically convergent with the ocular lens. Evidence for recruitment of aldehyde dehydrogenase as a predominant structural protein
    • Montgomery, M.K. and McFall-Ngai, M.J. (1992) The muscle-derived lens of a squid bioluminescent organ is biochemically convergent with the ocular lens. Evidence for recruitment of aldehyde dehydrogenase as a predominant structural protein. J. Biol. Chem., 267, 20999-21003.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20999-21003
    • Montgomery, M.K.1    McFall-Ngai, M.J.2
  • 19
    • 0026754720 scopus 로고
    • Lens crystallins. Innovation associated with changes in gene regulation
    • Piatigorsky, J. (1992) Lens crystallins. Innovation associated with changes in gene regulation. J. Biol. Chem., 267, 4277-4280.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4277-4280
    • Piatigorsky, J.1
  • 20
    • 0027288469 scopus 로고
    • Puzzle of crystallin diversity in eye lenses
    • Piatigorsky, J. (1993) Puzzle of crystallin diversity in eye lenses. Dev. Dyn., 196, 267-272.
    • (1993) Dev. Dyn. , vol.196 , pp. 267-272
    • Piatigorsky, J.1
  • 21
    • 0032052922 scopus 로고    scopus 로고
    • Gene sharing in lens and cornea: Facts and implications
    • Piatigorsky, J. (1998) Gene sharing in lens and cornea: facts and implications. Progr. Retinal Eye Res., 17, 145-174.
    • (1998) Progr. Retinal Eye Res. , vol.17 , pp. 145-174
    • Piatigorsky, J.1
  • 22
    • 0030592171 scopus 로고    scopus 로고
    • Characterization and enzyme activity of argininosuccinate lyase/δ-crystallin of the embryonic duck lens
    • Piatigorsky, J. and Horwitz, J. (1996) Characterization and enzyme activity of argininosuccinate lyase/δ-crystallin of the embryonic duck lens. Biochim. Biophys. Acta, 1295, 158-164.
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 158-164
    • Piatigorsky, J.1    Horwitz, J.2
  • 24
    • 0027286792 scopus 로고
    • J1-crystallins of the cubomedusan jellyfish lens constitute a novel family encoded in at least three intronless genes
    • Piatigorsky, J., Horwitz, J. and Norman, B.L. (1993) J1-crystallins of the cubomedusan jellyfish lens constitute a novel family encoded in at least three intronless genes. J. Biol. Chem., 268, 11894-11901.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11894-11901
    • Piatigorsky, J.1    Horwitz, J.2    Norman, B.L.3
  • 27
    • 0023074382 scopus 로고
    • Conservation of δ-crystallin gene structure between ducks and chicken
    • Piatigorsky, J., Norman, B.L. and Jones, R.E. (1987) Conservation of δ-crystallin gene structure between ducks and chicken. J. Mol. Evol., 25, 308-317.
    • (1987) J. Mol. Evol. , vol.25 , pp. 308-317
    • Piatigorsky, J.1    Norman, B.L.2    Jones, R.E.3
  • 29
    • 0024520027 scopus 로고
    • Enzyme/crystallins: Gene sharing as an evolutionary strategy
    • Piatigorsky, J. and Wistow, G. (1989) Enzyme/crystallins: gene sharing as an evolutionary strategy. Cell, 57, 197-199.
    • (1989) Cell , vol.57 , pp. 197-199
    • Piatigorsky, J.1    Wistow, G.2
  • 30
    • 0026326815 scopus 로고
    • The recruitment of crystallins: New functions precede gene duplication
    • Piatigorsky, J. and Wistow, G. (1991) The recruitment of crystallins: new functions precede gene duplication. Science 252, 1078-1079.
    • (1991) Science , vol.252 , pp. 1078-1079
    • Piatigorsky, J.1    Wistow, G.2
  • 31
    • 0000117979 scopus 로고
    • Transcriptional regulation of crystallin genes: Cis-elements, trans-factors and signal transduction systems in the lens
    • Piatigorsky, J. and Zelenka, P.S. (1992) Transcriptional regulation of crystallin genes: cis-elements, trans-factors and signal transduction systems in the lens. Adv. Dev. Biochem., 1, 211-256.
    • (1992) Adv. Dev. Biochem. , vol.1 , pp. 211-256
    • Piatigorsky, J.1    Zelenka, P.S.2
  • 32
    • 0028254544 scopus 로고
    • Expression of the α-crystallin/small heat shock protein/molecular chaperone genes in the lens and other tissues
    • Sax, C.M. and Piatigorsky, J. (1994) Expression of the α-crystallin/small heat shock protein/molecular chaperone genes in the lens and other tissues. Adv. Enzymol. Related Areas Molec. Biol., 69, 155-201.
    • (1994) Adv. Enzymol. Related Areas Molec. Biol. , vol.69 , pp. 155-201
    • Sax, C.M.1    Piatigorsky, J.2
  • 33
    • 0029564980 scopus 로고
    • Glutathione S-transferase and S-crystallins of cephalopods: Evolution from active enzyme to lens-refractive proteins
    • Tomarev, S.I., Chung, S. and Piatigorsky, J. (1995) Glutathione S-transferase and S-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins. J. Mol. Evol., 41, 1048-1056.
    • (1995) J. Mol. Evol. , vol.41 , pp. 1048-1056
    • Tomarev, S.I.1    Chung, S.2    Piatigorsky, J.3
  • 34
    • 0028291690 scopus 로고
    • Convergent evolution of crystallin gene regulation in squid and chicken: The AP-1/ARE connection
    • Tomarev, S.I., Duncan, M.K., Roth, H.R., Cvekl, A. and Piatigorsky, J. (1994) Convergent evolution of crystallin gene regulation in squid and chicken: the AP-1/ARE connection. J. Mol. Evol., 39, 134-143.
    • (1994) J. Mol. Evol. , vol.39 , pp. 134-143
    • Tomarev, S.I.1    Duncan, M.K.2    Roth, H.R.3    Cvekl, A.4    Piatigorsky, J.5
  • 35
    • 0030032495 scopus 로고    scopus 로고
    • Lens crystallins of invertebrates. Diversity and recruitment from detoxification enzymes ana novel proteins
    • Tomarev, S.I. and Piatigorsky, J. (1996) Lens crystallins of invertebrates. Diversity and recruitment from detoxification enzymes ana novel proteins. Eur. J. Biochem., 235, 449-465.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 449-465
    • Tomarev, S.I.1    Piatigorsky, J.2
  • 36
    • 0023691542 scopus 로고
    • Squid major lens polypeptides are homologous to glutathione S-transferease subunits
    • Tomarev, S.I. and Zinovieva, R.D. (1988) Squid major lens polypeptides are homologous to glutathione S-transferease subunits. Nature, 336, 86-88.
    • (1988) Nature , vol.336 , pp. 86-88
    • Tomarev, S.I.1    Zinovieva, R.D.2
  • 37
    • 0027513157 scopus 로고
    • Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods
    • Tomarev, S.I., Zinovieva, R.D., Guo, K. and Piatigorsky, J. (1993) Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods. J. Biol. Chem., 268, 4534-4542.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4534-4542
    • Tomarev, S.I.1    Zinovieva, R.D.2    Guo, K.3    Piatigorsky, J.4
  • 38
    • 0026669302 scopus 로고
    • Characterization of squid crystallin genes. Comparison with mammalian glutathione S-transferase genes
    • Tomarev, S.I., Zinovieva, R.D. and Piatigorsky, J. (1992) Characterization of squid crystallin genes. Comparison with mammalian glutathione S-transferase genes. J. Biol. Chem., 267, 8604-8612.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8604-8612
    • Tomarev, S.I.1    Zinovieva, R.D.2    Piatigorsky, J.3
  • 41
    • 0023648790 scopus 로고
    • The enzyme lactate dehydrogenases as a structural protein in avian and crocodilian lenses
    • Wistow, G., Mulders, J.W.M. and de Jong, W.W. (1987) The enzyme lactate dehydrogenases as a structural protein in avian and crocodilian lenses. Nature, 326, 622-624.
    • (1987) Nature , vol.326 , pp. 622-624
    • Wistow, G.1    Mulders, J.W.M.2    De Jong, W.W.3
  • 42
    • 0023225865 scopus 로고
    • Recruitment of enzymes as lens structural proteins
    • Wistow, G.J. and Piatigorsky, J. (1987) Recruitment of enzymes as lens structural proteins. Science, 236, 1554-1556.
    • (1987) Science , vol.236 , pp. 1554-1556
    • Wistow, G.J.1    Piatigorsky, J.2
  • 43
    • 0023917935 scopus 로고
    • Lens crystallins: The evolution and expression of proteins for a highly specialized tissue
    • Wistow, G. and Piatigorsky, J. (1988) Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Ann. Rev. Biochem., 57, 479-504.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 479-504
    • Wistow, G.1    Piatigorsky, J.2
  • 44
    • 0027302398 scopus 로고
    • Aldehyde dehydrogenase-derived Ω-crystallin of squid and octopus. Specialization for lens expression
    • Zinovieva, R.D., Tomarev, S.I. and Piatigorsky, J. (1993) Aldehyde dehydrogenase-derived Ω-crystallin of squid and octopus. Specialization for lens expression. J. Biol. Chem., 268, 11449-11455.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11449-11455
    • Zinovieva, R.D.1    Tomarev, S.I.2    Piatigorsky, J.3


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