Initiation of mammalian liver development from endoderm by fibroblast growth factors

Science

Volumn 284, Issue 5422, 1999, Pages 1998-2003

  Jung, Joonil ^a   Zheng, Minghua ^a   Goldfarb, Mitchell ^b   Zaret, Kenneth S ^a  

^a BROWN UNIVERSITY   (United States)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR; FIBROBLAST GROWTH FACTOR 1; FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR 4; FIBROBLAST GROWTH FACTOR RECEPTOR;

ANIMAL CELL; ARTICLE; CHICK EMBRYO; EMBRYO; EMBRYO INDUCTION; ENDODERM; GENE EXPRESSION; LIVER DEVELOPMENT; MESODERM; MOUSE; NONHUMAN; ORGANOGENESIS; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION;

ALPHA-FETOPROTEINS; ANIMALS; CULTURE TECHNIQUES; DIGESTIVE SYSTEM; EMBRYONIC INDUCTION; ENDODERM; FIBROBLAST GROWTH FACTOR 1; FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR 8; FIBROBLAST GROWTH FACTORS; GENE EXPRESSION; HEART; HEPARITIN SULFATE; LIVER; MESODERM; MICE; MICE, INBRED C3H; MORPHOGENESIS; ORGAN SPECIFICITY; PREALBUMIN; RECEPTORS, FIBROBLAST GROWTH FACTOR; RECOMBINANT FUSION PROTEINS; SERUM ALBUMIN; SIGNAL TRANSDUCTION;

ANIMALIA; MAMMALIA;

EID: 0033580985     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.284.5422.1998     Document Type: Article

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56. T. P. Yamaguchi et al., Genes Dev. 8, 3032 (1994); C. X. Deng et al., ibid., p. 3045; E. N. Meyers, M. Lewandoski, G. R. Martin, Nature Genet. 18, 136 (1998).
57. S. Ortega et al., Proc. Natl. Acad. Sci. U.S.A. 95, 5672 (1998); R. Dono et al., EMBO J. 17, 4213 (1998); M. Weinstein, X. Xu, K. Ohyama, C. X. Deng, Development 125, 3615 (1998).
58. S. Ortega et al., Proc. Natl. Acad. Sci. U.S.A. 95, 5672 (1998); R. Dono et al., EMBO J. 17, 4213 (1998); M. Weinstein, X. Xu, K. Ohyama, C. X. Deng, Development 125, 3615 (1998).
59. S. Ortega et al., Proc. Natl. Acad. Sci. U.S.A. 95, 5672 (1998); R. Dono et al., EMBO J. 17, 4213 (1998); M. Weinstein, X. Xu, K. Ohyama, C. X. Deng, Development 125, 3615 (1998).
60. Whole-mount in situ hybridization was performed as described [H. Sasaki and B. L. M. Hogan, Development 118, 47 (1993)]. Full-length Fgfl, FgfZ cDNAs (provided by Gail Martin) and a 400-nucleotide Fgf8 cDNA (10) were used to generate digoxigenin-labeled antisense probes.
61. Antibody staining was performed as reported [T. Ohta et al., Br. J. Cancer 72, 824 (1995)] with modifications. Embryos were fixed in 70% EtOH overnight at 4°C, embedded in a paraffin block, and sectioned 5 μm thick. For FGF1 and FGF2 localization, sections were treated with 0.25% trypsin in phosphate-buffered saline (PBS) for 5 min at room temperature. Mouse monoclonal antibodies against FGF1 were obtained from Sigma, and monoclonal antibody against FGF2, bFM-2, has been described [K. Matsuzaki et al., 86, 9911 (1989); provided by K. Matsumoto]. For FGF8 localization, sections were microwaved in 10 mM sodium citrate buffer to unmask antigens. Mouse monoclonal antibody against FGF8 was obtained from R&D systems. Normal mouse IgG was used as a control For the staining of FGFR-1 and -4, we used rabbit polydonal antibodies from Santa Cruz and normal rabbit IgG. In all cases, we used alkaline phosphatase-conjugated secondary antibodies (Sigma). We counterstained some sections with eosin Y.
62. Antibody staining was performed as reported [T. Ohta et al., Br. J. Cancer 72, 824 (1995)] with modifications. Embryos were fixed in 70% EtOH overnight at 4°C, embedded in a paraffin block, and sectioned 5 μm thick. For FGF1 and FGF2 localization, sections were treated with 0.25% trypsin in phosphate-buffered saline (PBS) for 5 min at room temperature. Mouse monoclonal antibodies against FGF1 were obtained from Sigma, and monoclonal antibody against FGF2, bFM-2, has been described [K. Matsuzaki et al., 86, 9911 (1989); provided by K. Matsumoto]. For FGF8 localization, sections were microwaved in 10 mM sodium citrate buffer to unmask antigens. Mouse monoclonal antibody against FGF8 was obtained from R&D systems. Normal mouse IgG was used as a control For the staining of FGFR-1 and -4, we used rabbit polydonal antibodies from Santa Cruz and normal rabbit IgG. In all cases, we used alkaline phosphatase-conjugated secondary antibodies (Sigma). We counterstained some sections with eosin Y.
63. J. Jung, M. Zheng, K. Zaret, unpublished observations.
64. The dissection, culture, and analysis of C3H mouse embryo tissues was as described (2). About one-half the embryos at 8 to 8.5 days of gestation contained two to six somites, one-half of those yielded successful endoderm isolations, and two-thirds of those yielded sufficient cells in explants for RNA isolation. Enzymatic digestion [E. Houssaint, Cell Differ. 9, 269 (1980)] was used in most cases to enhance the purity of ventral endoderm tissue; the enzyme treatment had no effect on hepatic induction. Anterior portions of the embryos were isolated and incubated in a solution of 0.025% trypsin, 0.125% pancreatin, 0.025% polyvinylpyrrolidone-40, 20 mM Hepes (pH 7.4) in PBS at 4°C for 3 to 5 min. The tissues were transferred to Dulbecco's modified Eagle's medium (DMEM) containing 10% calf serum at 37°C for 1 min to stop the digestion. The tissue was then transferred to PBS on a dissecting dish and the ventral foregut endoderm was separated from cardiac mesoderm with tungsten needles under a dissecting microscope at X60 magnification. Tissues were cultured on collagen-coated slide microwells (2) in DMEM containing 10% calf serum (Hyclone). Cells were cultivated for 2 days at 37°C before analysis.
65. -1) [L. Niswander and G. R. Martin, Nature 367, 68 (1993)] and 0.1% bovine serum albumin with the designated concentrations of recombinant human FGF1 or FGF2 (Boehringer Mannheim) or recombinant mouse FGF8b (R&D systems).
66. RNA was isolated from individual colonies and subjected to RT-PCR analysis as described (7), except that the sequence of the β-actin mRN A sense-strand oligonucleotide was 5′-AAAGACCTGTACGCCAACACAGTG-3′. The oligonucleotide sequences for analysis of TTR mRNA were 5′-CTTCCCTTCGACTCTTCCTCCT-3′ (sense strand) and 5′-GCCACGTCTACAGCAGGGCTGC-3′ (antisense strand). Actin primers were added after seven cycle steps with the liver-specific primers. Reaction products were tested from different cycle steps and only those samples within the exponential range of the PCR were used for the analysis.
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68. J. B. A. Green, H. V. New, J. C. Smith, Cell 71, 731 (1992).
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70. A. S. Tucker et al., Eur. J. Oral Sci. 106 (Suppl. 1), 122 (1998); G. Celli et al., CMBO J. 17, 1642 (1998).
71. A. S. Tucker et al., Eur. J. Oral Sci. 106 (Suppl. 1), 122 (1998); G. Celli et al., CMBO J. 17, 1642 (1998).
72. Plasmid DNAs encoding FR-IgG fusion proteins were transiently transfected into COS-7 cells and secreted proteins were purified with protein A - Sepharose beads. Proteins were quantitated by dot immunoblot analysis by using conjugated antibody to human IgG - horseradish peroxidase (Jackson ImmunoResearch Lab). Protein purity was analyzed by SDS - polyacrylamide gel electrophoresis (PACE) and silver staining. Ligand binding specificity of the proteins was assessed with NIH 3T3 cells. Briefly, serum-starved cells were stimulated with FGFs in the presence of either FR1-IgG or FR4-IgC for 5 hours. Total cell lysates were prepared and the changes in the protein phosphorylation profile were determined by immunoblot analysis with an antibody to phospho-tyrosine (Santa Cruz).
73. D. M. Omitz et al., J. Biol. Chem. 271, 15292 (1996); C. A. Dionne et al., EMBO J. 9, 2685 (1990).
74. D. M. Omitz et al., J. Biol. Chem. 271, 15292 (1996); C. A. Dionne et al., EMBO J. 9, 2685 (1990).
75. Data not shown for FCF2.
76. S. Sell, M. A. Longley, J. Boulter, Dev. Br. Res. 22, 49 (1985); A. Poliard, G. Feldman, D. Bernau, Differentiation 39, 59 (1988); J. Nahon et al., J. Biol. Chem. 263, 11436 (1988).
77. S. Sell, M. A. Longley, J. Boulter, Dev. Br. Res. 22, 49 (1985); A. Poliard, G. Feldman, D. Bernau, Differentiation 39, 59 (1988); J. Nahon et al., J. Biol. Chem. 263, 11436 (1988).
78. S. Sell, M. A. Longley, J. Boulter, Dev. Br. Res. 22, 49 (1985); A. Poliard, G. Feldman, D. Bernau, Differentiation 39, 59 (1988); J. Nahon et al., J. Biol. Chem. 263, 11436 (1988).
79. Supported by National Institutes of Health grant GM36477 to K.S.Z. We thank G. Martin for the FGF cDNAs; K. Matsumoto for FGF2 monoclonal antibody; and J. Coleman, P. Bossard, and J. Lora for comments on the manuscript.