Enhancer-independent promoter activity of the mouse αB-crystallin/small heat shock protein gene in the lens and cornea of transgenic mice

Mechanisms of Development

Volumn 92, Issue 2, 2000, Pages 125-134

  Gopal Srivastava, Rashmi ^a   Kays, W Todd ^a   Piatigorsky, Joram ^a  

^a NATIONAL EYE INSTITUTE   (United States)

Author keywords

Cornea; Crystallin; Enhancer; Gene expression; Lens; Promoter activity; Small heat shock protein

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; HEAT SHOCK PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CORNEA; CORNEA EPITHELIUM; ENHANCER REGION; GENE DELETION; GENE EXPRESSION; HISTOCHEMISTRY; IMMUNOHISTOCHEMISTRY; LENS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; TRANSGENE;

ANIMALS; CHLORAMPHENICOL O-ACETYLTRANSFERASE; CORNEA; CRYSTALLINS; ENHANCER ELEMENTS (GENETICS); EPITHELIUM, CORNEAL; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENES, REPORTER; HEAT-SHOCK PROTEINS; LENS, CRYSTALLINE; MICE; MICE, TRANSGENIC; PROMOTER REGIONS (GENETICS); TRANSGENES;

ANIMALIA; MUS MUSCULUS; RODENTIA;

EID: 0034176613     PISSN: 09254773     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-4773(99)00341-X     Document Type: Article

References (55)

1. Abedinia M., Pain T., Algar E.M., Holmes R.S. Bovine corneal aldehyde dehydrogenase: the major soluble corneal protein with a possible dual protective role for the eye. Exp. Eye Res. 51:1990;419-426.
2. Alexander R.J., Silverman B., Henley W.L. Isolation and characterization of BCP 54, the major soluble protein of bovine cornea. Exp. Eye Res. 32:1981;205-216.
3. Benjamin I.J., Shelton J., Garry D.J., Richardson J.A. Temporal expression of the small HSP/αB-crystallin in cardiac and skeletal muscle during mouse development. Dev. Dyn. 208:1997;75-84.
4. Bhat S.P., Nagineni C.N. αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues. Biochem. Biophys. Res. Commun. 158:1989;319-325.
5. Bloemendal H., de Jong W.W. Lens proteins and their genes. Prog. Nucleic Acid Mol. Biol. 41:1991;259-281.
6. Boesch J.S., Lee C., Lindahl R.G. Constitutive expression of class 3 aldehyde dehydrogenase in cultured rat corneal epithelium. J. Biol. Chem. 271:1996;5150-5157.
7. Cooper D.L., Baptist E.W., Enghild J.J., Isola N.R., Klintworth G.K. Bovine corneal protein 54K (BCP 54) is a homologue of the tumor-associated (class 3) rat aldehyde dehydrogenase (RATALD). Gene. 98:1991;201-207.
8. Cuthbertson R.A., Tomarev S.I., Piatigorsky J. Taxon-specific recruitment of enzymes as major soluble proteins in the corneal epithelium of three mammals, chicken, and squid. Proc. Natl. Acad. Sci. USA. 89:1992;4004-4008.
9. Cvekl A., Piatigorsky J. Lens development and crystallin gene expression: many roles for Pax-6. BioEssays. 18:1996;621-630.
10. de Jong W.W., Hendriks W., Mulders J.W.M., Bloemendal H. Evolution of eye lens crystallins: the stress connection. Trends Biochem. Sci. 14:1989;365-368.
11. de Jong W.W., Leunissen J.A.M., Voorter C.E.M. Evoultion of the α-crystallin/small heat shock protein family. Mol. Biol. Evol. 10:1993;103-126.
12. Deretic D., Aebersold R.H., Morrison H.D., Papermaster D.S. αA- and αB-crystallin in the retina. Association with the post-golgi compartment of frog retinal photoreceptors. J. Biol. Chem. 269:1994;16853-16861.
13. Donoghue M.J., Alvarez J.D., Sanes J.R. Fiber-type and position dependent expression of a myosin light chain-CAT transgene detected with a novel histochemical stain for CAT. J. Cell Biol. 115:1991;423-434.
14. Downes J., Holmes R. Development of aldehyde dehydrogenase and alcohol dehydrogenase in mouse eye: evidence for light induced changes. Biol. Neonate. 61:1992;118-123.
15. Dubin R.A., Wawrousek E.F., Piatigorsky J. Expression of the murine αB-crystallin gene is not restricted to the lens. Mol. Cell. Biol. 9:1989;1083-1091.
16. Dubin R.A., Gopal-Srivastava R., Wawrousek E.F., Piatigorsky J. Expression of the murine αB-crystallin gene in lens and skeletal muscle: identification of a muscle-preferred enhancer. Mol. Cell. Biol. 9:1991;4340-4349.
17. Flügel C., Liebe S., Voorter C., Bloemendal H., Lütjen-Drecoll E. Distribution of αB-crystallin in the anterior segment of primate and bovine eyes. Curr. Eye Res. 12:1993;871-876.
18. Gopal-Srivastava R., Piatigorsky J. The murine αB-crystallin/small heat shock protein enhancer: identification of αBE-1, αBE-2, αBE-3, and MRF control elements. Mol. Cell. Biol. 13:1993;7144-7152.
19. Gopal-Srivastava R., Piatigorsky J. Identification of a lens-specific regulatory region (LSR) of the murine αB-crystallin gene. Nucleic Acids Res. 22:1994;1281-1286.
20. Gopal-Srivastava R., Haynes J.I. II, Piatigorsky J. Regulation of the murine αB-crystallin/small heat shock protein gene in cardiac muscle. Mol. Cell. Biol. 15:1995;7081-7090.
21. Gopal-Srivastava R., Cvekl A., Piatigorsky J. Pax-6 and αB-crystallin/small heat shock protein gene regulation in the murine lens. J. Biol. Chem. 271:1996;23029-23036.
22. Gopal-Srivastava R., Cvekl A., Piatigorsky J. Involvement of retinoic acid/retinoid receptors in the regulation of murine αB-crystallin/small heat shock protein gene expression in the lens. J. Biol. Chem. 273:1998;17954-17961.
23. Haynes J.I. II, Gopal-Srivastava R., Frederikse P., Piatigorsky J. Differential use of the regulatory elements of the αB-crystallin enhancer in cultured murine lung (MLg), lens (αTN4-1) and muscle (C2C12) cells. Gene. 155:1995;151-158.
24. Haynes J.I. II, Duncan M.K., Piatigorsky J. Spatial and temporal activity of the αB-crystallin/small heat shock protein gene promoter in transgenic mice. Dev. Dyn. 207:1996;75-88.
25. Hogan B., Costantini F., Lacey E. Manipulating the Mouse Embryo. 1986;174-176 Cold Spring Harbor Laboratories, Cold Spring Harbor, NY.
26. Horwitz J. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA. 89:1992;10449-10453.
27. Horwitz J., Huang Q.-L., Ding L., Bova M.P. Lens α-crystallin: chaperone-like properties. Methods Enzymol. 290:1998;365-383.
28. Ingolia T.D., Craig E.A. Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc. Natl. Acad. Sci. USA. 79:1982;2360-2364.
29. Iwaki T., Kume-Iwaki A., Liem R.K.H., Goldman J.E. αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell. 57:1989;71-78.
30. Iwaki T., Kume-Iwaki A., Goldman J.E. Cellular distribution of αB-crystallin in non-lenticular tissues. J. Histochem. Cytochem. 38:1990;31-39.
31. Jester J.V., Moller-Pederson T., Huang J., Sax C.M., Kays W.T., Cavangh H.D., Petroll W.P., Piatigorsky J. The cellular basis of corneal transparency: evidence for 'corneal crystallins'. J. Cell Sci. 112:1999;613-622.
32. Kammandel B., Chowdhury K., Stoykova A., Aparicio S., Brenner S., Gruss P. Distinct cis-essential modules direct the time-space pattern of the Pax6 gene activity. Dev. Biol. 205:1999;79-97.
33. Klemenz R., Frohli E., Steiger R.H., Schafer R., Aoyama A. αB-crystallin is a small heat shock protein. Proc. Natl. Acad. Sci. USA. 88:1991;3652-3656.
34. Koroma B.M., Yang J.-M., Sundin O.H. The Pax-6 homeobox gene is expressed throughout the corneal and conjunctival epithelia. Invest. Ophthalmol. Vis. Sci. 38:1997;108-120.
35. Land M.F. The optics of animal eyes. Contemp. Phys. 29:1988;435-455.
36. Li H.-S., Yang J.-M., Jacobson R.D., Pasko D., Sundin O. Pax-6 is first expressed in a region of ectoderm anterior to the early neural palte: implications for stepwise determination of the lens. Dev. Biol. 162:1994;181-194.
37. Maniatis T., Fritsch E.F., Sambrook J. Molecular Cloning. 1989;1-34 Cold Spring Harbor Laboratories, Cold Spring Harbor, NY.
38. Maurice D.M. The structure and transparency of the cornea. J. Physiol. 136:1957;263-286.
39. Mitchell J., Cenedella R.J. Quantitation of ultraviolet light-absorbing fractions of the cornea. Cornea. 14:1995;266-272.
40. Neumann J.R., Morency C.A., Russian K.O. A novel and rapid assay for chloramphenicol acetyltransferase gene expression. BioTechniques. 5:1987;444-447.
41. Piatigorsky J. Lens differentiation in vertebrates. A review of cellular and molecular features. Differentiation. 19:1981;134-152.
42. Piatigorsky J. Gene sharing in lens and cornea: facts and implications. Prog. Retinal Eye Res. 17:1998;145-174.
43. Piatigorsky J., Wistow G.J. Enzyme-crystallins: gene sharing and evolutionary strategy. Cell. 57:1989;197-199.
44. Robinson M.L., Overbeek P.A. Differential expression of αA- and αB-crystallin during murine ocular development. Invest. Ophthalmol. Vis. Sci. 37:1996;2276-2284.
45. Salamon C., Chervenak M., Piatigorsky J., Sax C.M. The mouse transketolase (TKT) gene: cloning, characterization, and functional promoter analysis. Genomics. 48:1998;209-220.
46. Sax C.M., Piatigorsky J. Expression of the α-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues. Adv. Enzymol. Rel. Areas Mol. Biol. 69:1994;155-201.
47. Sax C.M., Salamon C., Kays W.T., Guo J., Yu F.X., Cuthbertson R.A., Piatigorsky J. Transketolase is a major protein in the mouse cornea. J. Biol. Chem. 271:1996;33568-33574.
48. Silverman B., Alexander R.J., Henley W.L. Tissue and species specificity of BCP 54, the major soluble protein of bovine cornea. Exp. Eye Res. 33:1981;19-29.
49. Sorger P.K. Heat shock factor and the heat shock response. Cell. 65:1991;363-366.
50. Tamm E.R., Russell P., Johnson D.H., Piatigorsky J. Human and monkey trabecular meshwork accumulate αB-crystallin in response to heat shock and oxidative stress. Invest. Ophthalmol. Vis. Sci. 37:1996;2402-2413.
51. Verhagen C., Hoekzema R., Verjans G.M.G.M., Kijlstra A. Identification of bovine corneal protein 54 (BCP 54) as an aldehyde dehydrogenase. Exp. Eye Res. 53:1991;283-284.
52. Wawrousek E.F., Brady J.P. αB-Crystallin gene knockout mice develop a severe, fatal phenotype late in life. Invest. Ophthalmol. Vis. Sci. 39:(4, suppl.):1998;S523.
53. Weintraub H., Davis R., Lockshon D., Lassar A. MyoD binds cooperatively in two sites in a target enhancer sequence: occupancy of two sites is required for activation. Proc. Natl. Acad. Sci. USA. 87:1991;5623-5627.
54. Williams S.C., Altmann C.R., Chow R.L., Hemmati-Brivanlou A., Lang R.A. A highly conserved lens transcriptional control element from the Pax-6 gene. Mech. Dev. 73:1998;225-229.
55. Wistow G., Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu. Rev. Biochem. 57:1988;479-504.