Induction of lens differentiation by activation of a bZIP transcription factor, L-Maf

Science

Volumn 280, Issue 5360, 1998, Pages 115-118

  Ogino, Hajime ^a   Yasuda, Kunio ^a  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BINDING PROTEIN; GENE PRODUCT; LENS PROTEIN; TRANSCRIPTION FACTOR;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CHICK EMBRYO; CONTROLLED STUDY; ECTODERM; EMBRYO; GENE EXPRESSION; LENS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ISOLATION; TRANSCRIPTION REGULATION; VERTEBRATE;

AMINO ACID SEQUENCE; ANIMALS; BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS; CELL DIFFERENTIATION; CELLS, CULTURED; CHICK EMBRYO; CRYSTALLINS; DNA, COMPLEMENTARY; DNA-BINDING PROTEINS; ECTODERM; ENHANCER ELEMENTS (GENETICS); EYE PROTEINS; G-BOX BINDING FACTORS; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENES, REPORTER; INTERMEDIATE FILAMENT PROTEINS; LENS, CRYSTALLINE; MAF TRANSCRIPTION FACTORS; MOLECULAR SEQUENCE DATA; PROMOTER REGIONS (GENETICS); RECOMBINANT FUSION PROTEINS; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC; TRANSFECTION;

ANIMALIA; MAMMALIA; VERTEBRATA;

EID: 0032478785     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5360.115     Document Type: Article

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25. Culturing of lens, neural retina, and lung tissues was performed as described (4). For virus experiments, specific pathogen-free white Leghorn eggs were used (line M, supplied by Nisseiken Ltd.).
26. L-maf cDNA or the Hind III-Bam HI fragment of pCHIIO (Pharmacia) encoding β-galactosidase were inserted into pEFX, resulting in pEFX-L-Maf and pEFX-β-gal, respectively. Cotransfection was carried out using a calcium phosphate method with 0.3 μg of luciferase reporter plasmid, 0.25 μg of pEFX-β-gal, 0.45 μg of pUC119 (carrier), and 20 ng of effector plasmid (pEFX or pEFX-L-Maf) in 22-mm dishes. Cell extracts were prepared 48 hours after transfection for assay of luciferase activities. β-Ga-lactosidase was used to determine relative transfection efficiencies and to normalize luciferase activity. For forced expression experiments, 2 μg of pEFX-β-gal or pEFX-L-Maf was transfected into a 35-mm dish.
27. L-maf cDNA containing the open reading frame was inserted into the Eco RI site of pMAL-cRI vector (New England Biolabs). MBP-L-Maf fusion protein was purified by amylose resin affinity-column chromatography as recommended by the supplier (New England Biolabs); 250 ng of MBP-L-Maf or MBP (control) was incubated with the following end-labeled oligonucleotides and analyzed by polyacrylamide gel electrophoresis (3, 4): cαA, chick αA-crystallin (base pairs -114 to -90, 5′-CATTTCTGCTGACCACGT-TGCCTTC-3′); mt-cαA, a mutated version of cαA (5′-CATTTCTCAGGACCACGTTGCCTTC-3′); cβB1, chick βB1-crystallin (base pairs -93 to -69, 5′-AGACACTGATGAGCTGGCACTTCCA-3′); cδ1, chick δ1 -crystallin (base pairs 2200 to 2224, 5′-CAG-GACTGCAGGATCAGCATGATC-3′); mαA, mouse αA-crystallin (base pairs -116 to -92, 5′-TC-CAGCTGCTGACGGTGCAGCCTCT-3′); and mγF, mouse γF-crystallin (base pairs -53 to -29, 5′-TGTTCCTGCCAACACAGCAGACCTC-3′).
28. L-Maf antiserum was generated by immunizing a rabbit with MBP-L-Maf. The crystallin mAbs were provided by K. Sawada and G. Eguchi [K. Sawada, K. Agata, A. Yoshiki, G. Eguchi, Jpn. J. Ophthalmol. 37, 355 (1993)]. L-Maf and β-gal immune complexes were detected with antibodies to rabbit immunoglobulin G (IgG) conjugated to tetramethyl rhodamine isothiocyanate (DAKO); crystallin immune complexes were detected with antibody to mouse IgG conjugated to fluorescein isothiocyanate (DAKO).
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30. In ovo electroporation was basically performed as described [T. Muramatsu, Y. Mizutani, J. Okumura, Anim. Sci. Technol. 67, 906 (1996)]. Plasmid pCAGGS-L-Maf, containing an L-maf cDNA fused to a plasmid pCAGGS bearing a CMV-β-actin promoter [M. Tokui et al., Biochem. Biophys. Res. Commun. 233, 527 (1997)], was electroporated into chick embryos at stage 9 to 10 together with plasmid pCAGGS-GFP to monitor incorporation of DNA into embryos. Whole mount immunostaining was performed as described [Y. M. Lee et al., Development 121, 825 (1995)]. We have found that not all tissues are equally sensitive to uptake of DNA delivered by this method. In particular, the branchial arch region appears less sensitive than the surrounding ectoderm for induction of L-Maf expression.
31. In ovo electroporation was basically performed as described [T. Muramatsu, Y. Mizutani, J. Okumura, Anim. Sci. Technol. 67, 906 (1996)]. Plasmid pCAGGS-L-Maf, containing an L-maf cDNA fused to a plasmid pCAGGS bearing a CMV-β-actin promoter [M. Tokui et al., Biochem. Biophys. Res. Commun. 233, 527 (1997)], was electroporated into chick embryos at stage 9 to 10 together with plasmid pCAGGS-GFP to monitor incorporation of DNA into embryos. Whole mount immunostaining was performed as described [Y. M. Lee et al., Development 121, 825 (1995)]. We have found that not all tissues are equally sensitive to uptake of DNA delivered by this method. In particular, the branchial arch region appears less sensitive than the surrounding ectoderm for induction of L-Maf expression.
32. In ovo electroporation was basically performed as described [T. Muramatsu, Y. Mizutani, J. Okumura, Anim. Sci. Technol. 67, 906 (1996)]. Plasmid pCAGGS-L-Maf, containing an L-maf cDNA fused to a plasmid pCAGGS bearing a CMV-β-actin promoter [M. Tokui et al., Biochem. Biophys. Res. Commun. 233, 527 (1997)], was electroporated into chick embryos at stage 9 to 10 together with plasmid pCAGGS-GFP to monitor incorporation of DNA into embryos. Whole mount immunostaining was performed as described [Y. M. Lee et al., Development 121, 825 (1995)]. We have found that not all tissues are equally sensitive to uptake of DNA delivered by this method. In particular, the branchial arch region appears less sensitive than the surrounding ectoderm for induction of L-Maf expression.
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46. We thank K. Umesono, R. Yu, K. Shimamoto, M. Nakafuku, J. Kato, and M. Takeichi for critical reading and comments on the manuscript; T. Momose and K. Ono for help with whole mount in situ hybridization; K. Umesono, H. Ogawa, and J. Miyazaki for plasmids; and K. Sawada and G. Eguchi for mAbs. Supported in part by grants-in-aid for scientific research from the Ministry of Education, Science, and Culture of Japan and by a grant from the Human Frontier Science Program. The GenBank accession number for L-maf is AF034570.