Extralenticular expression of Xenopus laevis α-, β-, and γ-crystallin genes

Investigative Ophthalmology and Visual Science

Volumn 38, Issue 13, 1997, Pages 2764-2771

  Brunekreef, Gerd A ^a   Van Genesen, Siebe T ^a   Destrée, Olivier H J ^b   Lubsen, Nicolette H ^a  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^b HUBRECHT INSTITUTE   (Netherlands)

Author keywords

Crystallins; Gastrula; Lens development; Xenopus laevis

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; ECTODERM; EMBRYO; EPITHELIUM CELL; GASTRULA; GENE EXPRESSION; LENS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; CRYSTALLINS; DNA, COMPLEMENTARY; EMBRYO, NONMAMMALIAN; GENE EXPRESSION; GENE LIBRARY; IN SITU HYBRIDIZATION; LENS, CRYSTALLINE; MOLECULAR SEQUENCE DATA; RNA, MESSENGER; SEQUENCE HOMOLOGY, AMINO ACID; XENOPUS LAEVIS;

EID: 0031444640     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (49)

1. Delaye M, Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature. 1983;302:415-417.
2. Wistow G, Piatigorsky J. Lens crystallins: The evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem, 1988;57:479-504.
3. Bloemendal H, De Jong WW. Lens proteins and their genes. Prog Nucl Acid Res Molec Biol. 1991;41:259-281.
4. Piatigorsky J, Wistow G. The recruitment of crystallins: New functions precede gene duplication. Science. 1991;25:1078-1079.
5. Ignolia TD, Graig EA. Four small heat shock proteins are related to each other and to mammalian α-crystallin. Proc Natl Acad Sci U S A. 1982;79:2360-2364.
6. Horwitz J. Alpha-crystallin can function as a molecular chaperon. Proc Natl Acad Sci U S A. 1992;89:10449-10453.
7. Jakob U, Gaestel M, Engek K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem. 1993;268:1517-1520.
8. Klementz R, Frohli E, Steiger RH, Schafer R, Aoyama A. αB-crystallin is a small heat shock protein. Proc Natl Acad Sci U S A. 1991;88:9292-9296.
9. Kato K, Shinohara H, Kurobe N, Goto S, Inaguma Y, Ohshima K. Immunoreactive αA-crystallin in rat nonlenticular tissues detected with a sensitive immunoassay method. Biochim Biophys Acta. 1991; 1080:173-180.
10. Bhat SP, Nagineni CN. αB subunit of lens-specific protein α-crystallin is present in other ocular and nonocular tissues. Biochem Biophys Res Commun. 1989; 158:319-325.
11. Piatigorsky J. Lens crystallins: Innovation associated with changes in gene regulation. J Biol Chem. 1992;267:4277-4280.
12. Kraft HJ, Voorter CEM, Wintjes L, Lubsen NH, Schoenmakers JGG. The developmental expression of taxon-specific crystallins in the duck lens. Exp Eye Res. 1994;58:389-395.
13. Head MW, Peter A, Clayton RM. Evidence for the extra lenticular expression of members of the β-crystallin gene family in the chick and comparison with δ-crystallin during differentiation and transdifferentiation. Differentiation. 1991;48:147-156.
14. Head MW, Sedowofia K, Clayton RM. βB2-crystallin in the mammalian retina. Exp Eye Res. 1995;61:423-428.
15. Smolich BD, Tarkington SK, Saha MS, Grainger RM. Xenopus γ-crystallin gene expression: Evidence that the γ-crystallin gene family is transcribed in lens and non-lens tissues. Mol Cell Biol. 1994;14:1355-1363.
16. McAvoy JW. Cell division, cell elongation and distribution of α-, β-, γ-crystallins in the rat lens. J Embryol Exp Morphol. 1978;44:140-165.
17. McAvoy JW. Cell division, cell elongation and the coordination of crystallin gene expression during lens morphogenesis in the rat. J Embryol Exp Morphol. 1978;45:271-281.
18. Van Leen RW, Van Roozendaal KEP, Lubsen NH, Schoenmakers JGG. Differential expression of crystallin genes during development of the rat eye lens. Dev Biol. 1987;120:457-464.
19. Hejtmancik JF, Beebe DC, Ostrer H, Piatigorsky J. δ-and β-crystallin mRNA levels in the embryonic and post-hatched chicken lens: Temporal and spatial changes during development. Dev Biol. 1985;109:72-81.
20. Brahma SK, Defize LHK. Ontogeny of the 38K ε-polypeptide during lens development of the duck Anas platyrhynchos. Curr Eye Res. 1985;4:679-684.
21. McDevitt DS, Brahma SK. Ontogeny and localization of the crystallins during embryonic lens development in Xenopus laevis. J Exp Zool. 1973;186:127-140.
22. Grainger RM. Embryonic lens induction: Shedding light on vertebrate tissue determination. Trends Genet. 1992;8:349-355.
23. Henry JJ, Grainger RM. Inductive interactions in the spatial and temporal restriction of lens forming potential in embryonic ectoderm of Xenopus laevis. Dev Biol. 1987;124:200-214.
24. Servetnick M, Grainger RM. Changes in neural and lens competence in Xenopus ectoderm: Evidence for an autonomous developmental timer. Development. 1991;112:177-188.
25. Nieuwkoop PD, Faber J. Normal Table of Xenopus laevis. Amsterdam: North-Holland; 1956.
26. Sambrook J, Fritsch EF, Maniatis T. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor: Cold Spring Harbor Laboratory. 1989.
27. Ausubel FM, Brent R, Kingston, et al, eds. Current Protocols in Molecular Biology. John Wiley & Sons, 1993.
28. Harland RM. In situ hybridization: An improved whole mount method for Xenopus embryos. Methods Cell Biol. 1991;36:685-695.
29. Barth J, Ivarie R. Polyvinyl alcohol enhances detection of low abundance transcripts in early stage quail embryos in a radioactive whole mount in situ hybridization technique. Biotechniques. 1994;17:324-327.
30. De Block M, Debrouwer D. RNA-RNA in situ hybridization using digoxigenin-labelled probes: The use of high-molecular-weight polyvinyl alcohol in the alkaline phosphatase indolyl-nitroblue tetrazolium reaction. Anal Biochem. 1993;215:86-89.
31. Van Rens GLM, Driessen HPC, Nalini V, Slingsby C, De Jong WW, Bloemendal H. Isolation and characterization of cDNAs encoding βA2- and βA4-crystallins: Heterologous interactions in the predicted βA4-βA2 heterodimer. Gene. 1991;102:179-188.
32. Duncan MK, Haynes JI, Piatigorsky J. The chicken βA4- and βB1-crystallin encoding genes are tightly linked. Gene. 1995;162:189-196.
33. Bijlsma EK, Delattre O, Juyn JA, et al. The regional fine mapping of the β-crystallin genes on chromosome 22 excludes these genes as physically linked markers for neurofibromatosis type 2. Genes Chrom Cancer. 1993;8:112-118.
34. De Jong WW, Terwindt EC. The amino-acid sequence of the alpha-crystallin A chains of red kangaroo and Virginia opossum. Eur J Biochem. 29;67:503-510.
35. Tomarev SI, Zinovieva RD, Dolgilevich SM, Krayev AS, Skryabin KG, Gause GG Jr. The absence of the long 3′ non-translated region in mRNA coding for eye lens αA2-crystallin of the frog (Rana temporaria) FEBS Lett. 1983;162:47-51.
36. Hendriks W, Weetink H, Voorter CEM, Sander J, Bloemendal H, De Jong WW. The alternative splicing product αAins-crystallin is structural equivalent to the αA and αB subunits in the rat α-crystallin aggregate. Biochim Biophys Acta. 1990;1037:58-65.
37. De Jong WW, Terwindt EC, Bloemendal H. The amino acid sequence of the A chain of human alpha crystallin. FEBS Lett. 1975;58:310-313.
38. Smolich BD, Tarkington SK, Saha MS, Stahakis DG, Grainger RM. Characterization of Xenopus laevis γ-crystallin encoding genes. Gene. 1993;128:189-195.
39. Van Rens GLM, Hol FA, De Jong WW, Bloemendal H. Presence of hybridizing DNA sequences homologous to bovine acidic and basic β-crystallins in all classes of vertebrates. J Mol Evol. 1991;33:457-463.
40. Shastry BS. Immunological studies on gamma crystallins from Xenopus: Localization, tissue specificity and developmental expression of proteins. Exp Eye Res. 1989;49:361-369.
41. Aarts HJM, Lubsen NH, Schoenmakers JGG. Crystallin gene expression during rat lens development. Eur J Biochem. 1989;183:31-36.
42. McAvoy JW. Induction of the eye lens. Differentiation. 1981;17:137-149.
43. Henry JJ, Grainger RM. Early tissue interactions leading to embryonic lens formation in Xenopus laevis. Dev Biol. 1990;141:149-163.
44. Henry JJ, Mittleman JM. The matured eye of Xenopus laevis tadpoles produces factors that elicit a lens forming response in embryonic ectoderm. Dev Biol. 1995; 171:39-50.
45. Saha MS, Spann CL, Grainger RM. Embryonic lens induction: More than meets the optic vesicle. Cell Diff. Dev 1989:28;153-172.
46. Moscona AA. Conversion of retina glia cells into lens like phenotype following disruption of normal cell contacts. Curr Top Dev Biol. 1986;20:1-19.
47. Eguchi G. Instability in cell commitment of vertebrate pigmented epithelial cells and their transdifferentiation into lens cells. Curr Top Dev Biol. 1986;20:21-37.
48. Clayton RM, Jeanny J-C, Bower DJ, Errington LH. The presence of extralenticular crystallins and its relationship with transdifferentiation to lens. Curr Top Dev Biol. 1986;20:137-151.
49. Freeman G. Lens regeneration from the cornea in Xenopus laevis. J Exp Zool. 1963;154:39-66.