Vascular Cell Responses to TGF-β₃ Mimic Those of TGF-β₁in vitro

References

• Antonelli‐Orlidge A., Saunders K. B., Smith S. R., D'Amore P. A. An activated form of transforming growth factor‐beta is produced by co‐cultures of endothelial cells and pericytes. Proc. Natl. Acad. Sci 1989; 86: 4544–4548
   PubMed Web of Science ®Google Scholar
• Assoian R. K., Komoriya A., Meyers C. A., Miller D. M., Sporn M. B. Transforming growth factor‐beta in human platelets: identification of a major storage site, purification‐ and characterization. J. Biol. Chem 1983; 258(11)7155–7160
   PubMed Web of Science ®Google Scholar
• Barton D. E., Foellmer B. E., Du J., Tamm J., Derynck R., Francke U. Chromosomal mapping of genes for TGF‐β2 and TGF‐β3 in man and mouse: Dispersion of TGF‐P gene family. Oncogene Res 1988; 3: 323–331
   PubMedGoogle Scholar
• Bascom C. C., Wolfshohl J. R., Coffey R. J., Madisen L., Webb N. R., Purchio A. R., Derynck R., Moses H. L. Complex regulation of transforming growth factor betal, beta2 and beta3 mRNA expression in mouse fibro‐blasts and keratinocytes by transforming growth factors beta, and beta2. Mol. Cell. Bd. (USA) 1989; 9(12)5508–5515
   PubMedGoogle Scholar
• Bell L., Madri J. A. Effects of platelet factors on migration of cultured bovine aortic endothelial and smooth muscle cells. Circulation Res 1989; 65: 1057–1065
   PubMed Web of Science ®Google Scholar
• Brown P. D., Wakefield L. M., Levinson A. D., Sporn M. B. Physiochemical activation of recombinant latent transforming growth factor‐beta's 1, 2, and 3. Growth Factors 1990; 3: 35–43
   PubMed Web of Science ®Google Scholar
• Cheiftez S., Weatherbee J. A., Tsang M. L. ‐S., Anderson J. K., Mole J. E., Lucas R., Massague J. The transforming growth factor‐beta system, a complex pattern of cross‐reactive ligands and receptors. Cell 1987; 48(3)409–415
   PubMedGoogle Scholar
• Cheifetz S., Hernandez H., Laiho M., ten Dijke P., Iwata K. K., Massague J. Distinct transforming growth factor P (TGF‐β) receptor subsets as determinants of cellular responsiveness to three TGF‐P isoforms. J. Biol. Chem 1990; 265(33)20533–20538
   PubMed Web of Science ®Google Scholar
• Collins T., Pober J. S., Gimbrone M. A., Hammacher A., Betsholtz C., Westermark B., Heldin C. ‐H. Cultured human endothelial cells express platelet‐derived growth factor A chain. Am. J. Path 1987; 126: 7–12
   PubMedGoogle Scholar
• Danielpour D., Dart L. L., Flanders K. C., Roberts A. B., Sporn M. B. Immunodetection and quantitation of the two forms of transforming growth factor‐beta (TGF‐β, and TGF‐P2) secreted by cells in culture. J. Cell. Physiol 1989; 138: 79–86
   PubMed Web of Science ®Google Scholar
• Denhez F., Lafyatis R., Kondaiah P., Roberts A. B., Sporn M. B. Cloning by Polymerase Chain Reaction of a New Mouse TGF‐β, TGF‐P3. Growth Factors 1990; 3: 139–146
   PubMed Web of Science ®Google Scholar
• Derynck R., Lindquist P. B., Lee A., Wen D., Tamm J., Graycar J. L., Rhee L., Mason A. J., Miller D. A., Coffey R. J. A new type of transforming growth factor‐beta, TGF‐beta3. EMBO J 1988; 7(12)3737–3743
   PubMedGoogle Scholar
• DiCorleto P. E., Bowen‐Pope D. F. Cultured endothelial cells produce a platelet‐derived growth factor‐like protein. Proc. Natl. Acad. Sci 1983; 80: 1919–1923
   PubMed Web of Science ®Google Scholar
• Ding A., Nathan C. F., Graycar J., Derynck R., Stuehr D. J., Srimal S. Macrophage deactivating factor and TGF‐β1, TGF‐β2 and TGF‐β3 inhibit induction of macrophage nitrogen oxide synthesis by IFN‐γ. J. Immunol 1990; 145(3)940–944
   PubMedGoogle Scholar
• Fitzpatrick D. R., Denhez F., Kondaiah P., Akhurst R. J. Differential expression of TGF‐beta isoforms in murine palatogenesis. Devel 1990; 109: 585–595
   PubMedGoogle Scholar
• Flanders K. C., Roberts A. B., Ling N., Fleurdelys B. E., Sporn M. B. Antibodies to peptide determinants in transforming growth factor‐beta and their applications. Biochem 1988; 27: 739–746
   PubMed Web of Science ®Google Scholar
• Form D. M., Pratt B. M., Madri J. A. Endothelial cell proliferation during angiogenesis: in vitro modulation by basement membrane components. Lab. Invest 1986; 55: 521–530
   PubMed Web of Science ®Google Scholar
• Frolik C. A., Wakefield L. M., Smith D. M., Sporn M. B. Characterization of a membrane receptor for transforming growth factor‐beta in normal rat kidney fibro‐blasts. J. Biol. Chem 1984; 259(17)10995–11000
   PubMed Web of Science ®Google Scholar
• Fujii D., Brissenden J. E., Derynck R., Francke U. Transforming growth factor beta gene maps to human chromosome 19 long arm and to mouse chromosome. J. Somatic Cell Mol. Genet 1986; 12: 281–288
   PubMedGoogle Scholar
• Gatherer D., ten Dijke P., Baird D. T., Akhurst R. J. Expression of TGF‐P isoforms during first trimester human embryogenesis. Devel 1990; 110: 445–460
   PubMed Web of Science ®Google Scholar
• Glick A. B., Flanders K. C., Danielpour D., Yuspa S. H., Sporn M. B. Retinoic acid induces transforming growth factor‐beta2 in cultured keratinocytes and mouse epidermis. Cell Regul 1989; 1: 87–97
   PubMedGoogle Scholar
• Gospodarowicz D., Hirabayashi K., Giguere L., Tauber J. P. Factors controlling the proliferative rate, final cell density, and life span of bovine vascular smooth muscle cells in culture. J. Cell Biol 1981; 89: 568–578
   PubMed Web of Science ®Google Scholar
• Graycar J. L., Miller D. A., Arrick B. A., Lyons R. M., Moses H. L., Derynck R. Human transforming growth factor‐beta3: recombinant expression, purification, and biological activities in comparison with transforming growth factors‐beta1 and beta2. Mol. Endocrinol. (USA) 1989; 3(12)1977–1986
   PubMedGoogle Scholar
• Ikeda T., Lioubin M. N., Marquardt H. Human transforming growth factor‐beta2: production by a prostatic adenocarcinoma cell line, purification and initial characterization. Biochem 1987; 26: 2406–2410
   PubMed Web of Science ®Google Scholar
• Jakowlew S. B., Dillard P. J., Kohdaiah P., Sporn M. B., Roberts A. B. Complementary deoxyribonucleic acid cloning of a novel transforming growth factor‐β messenger ribonucleic acid from chick embryo chondrocytes. Molec. Endocrinol 1988; 2: 747–755
   PubMed Web of Science ®Google Scholar
• Jennings J. C., Mohan S., Linkhart T. A., Widstrom R., Baylink D. J. Comparison of biological actions of transforming growth factor‐beta, and transforming growth factor‐beta2: differential activity in endothelial cells. J. Cell. Physiol 1988; 137: 167–172
   PubMed Web of Science ®Google Scholar
• Karnovsky M. J. Endothelium‐vascular smooth muscle cell interactions. Am. J. Path 1981; 105: 200–206
   PubMedGoogle Scholar
• Kim S. ‐J., Angel P., Lafyatis R., Hattori K., Kim K. Y., Sporn M. B., Karin M., Roberts A. B. Autoinduction of transforming growth factor β1 is mediated by the AP‐1 complex. Molec. and Cell. Biol 1990; 10(4)1492–1497
   Google Scholar
• Kocher O., Madri J. A. Modulation of actin mRNAs in cultured vascular cells by matrix components and TGF‐β1. In Vitro Cell., & Dev. Biol 1989; 25(5)424–434
   PubMedGoogle Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Lafyatis R., Lechleider R., Kin S. ‐J., Jakowlew S., Roberts A. B., Sporn M. B. Structural and functional characterization of the transforming growth factorβ3 promoter. J. Biol. Chem 1990; 265(31)19128–19136
   PubMedGoogle Scholar
• Longenecker J. P., Kilty L. A., Johnson L. K. Glucocorticoid inhibition of vascular smooth muscle cell proliferation: influence of homologous extracellular matrix and serum mitogens. J. Cell Biol 1984; 98: 534–540
   PubMed Web of Science ®Google Scholar
• Lyons R. M., Moses H. L. Review: Transforming growth factors and the regulation of cell proliferation. Eur. J. Biochem 1990; 187: 467–473
   PubMedGoogle Scholar
• Madri J. A. The extracellular matrix as a modulator of angiogenesis. Cardiovascular Disease, L. L. Gallo. GWUMC Dept of Biochem Annual Spring Symposia, Plenum Press, NY 1987; 177–183
   Google Scholar
• Madri J. A., Dreyer F. A., Pitlick F. A., Furthmayr H. The collagenous components of the subendothelium correlation of structure and function. Lab. Invest 1980; 43: 305–315
   Google Scholar
• Madri J. A., Furthmayr H. Isolation and localization of AB2 collagen in the lung. Am. J. Path 1979; 94: 179–187
   Google Scholar
• Madri J. A., Furthmayr H. Collagen polymorphism in the lung: an immunochemical study of pulmonary fibrosis. Hum. Path 1980; 11: 353–366
   PubMed Web of Science ®Google Scholar
• Madri J. A., Pratt B. M., Tucker A. M. Phenotypic modulation of endothelial cells by transforming growth factor‐beta depends upon the composition and organization of the extracellular matrix. J. Cell Biol 1988a; 106: 1375–1384
   PubMed Web of Science ®Google Scholar
• Madri J. A., Pratt B. M., Yannariello‐Brown J. Endothelial cell‐extracellular matrix interactions: matrix as a modulator of cell function. Endothelial Cell Biology, N. Simionescu, M. Simionescu. Plenum Publishing Corp., NY 1988b; 167–188
   Google Scholar
• Madri J. A., Williams S. K. Capillary endothelial cell cultures: phenotypic modulation by matrix components. J. Cell Biol 1983; 97: 153–165
   PubMed Web of Science ®Google Scholar
• Merwin J. R., Anderson J. M., Kocher O., Van Itallie C. M., Madri J. A. Transforming growth factor‐beta, modulates extracellular matrix organization and cell‐cell junctional complex formation during in vitro angiogenesis. J. Cell. Physiol 1990; 142: 117–129
   PubMed Web of Science ®Google Scholar
• Merwin J. R., Newman W., Beall L. D., Tucker A., Madri J. A. Vascular cells respond differentially to transforming growth factors‐beta, and beta2, in vitro. Am. J. Path 1991; 138: 37–51
   PubMed Web of Science ®Google Scholar
• Miller D. A., Lee A., Matsui Y., Chen E. Y., Moses H. L., Derynck R. Complementary DNA cloning of the murine transforming growth factor‐beta3 (TGF‐beta3) precursor and the comparative expression of TGF‐beta, and TGF‐beta, messenger RNA in murine embryos and adult tissues. Mol. Endocrinol. (USA) 1989; 3(12)1926–1934
   PubMedGoogle Scholar
• Noma R., Glick A. B., Geiser A. G., O'Reilly M. A., Miller J., Roberts A. B., Sporn M. B. Molecular cloning and structure of the human transforming growth factor‐β2 gene promoter. Growth Factors 1981, in Press
   Google Scholar
• Ohta M., Greenberger J. S., Anklesaria R., Bassols A., Massague J. Two forms of transforming growth factor‐beta distinguished by multipotential haematopoietic progenitor cells. Nature 1987; 329: 539–541
   PubMed Web of Science ®Google Scholar
• Pelton R. W., Hogan R. L., Miller D. A., Moses H. L. Differential expression of genes encoding TGFs β1, β2, and β3 during murine palate formation. Devel 1990a; 141: 456–460
   Google Scholar
• Pelton R. W., Dickinson M. E., Moses H. L., Hogan B. L. M. In situ hybridization analysis of TGF‐β3 RNA expression during mouse development: comparative studies with TGF‐β1 and β2. Devel 1990b; 110: 609–620
   PubMed Web of Science ®Google Scholar
• Pratt B. M., Harris A. S., Morrow J. S., Madri J. A. Mechanisms of cytoskeletal regulation: modulation of aortic endothelial cell spectrin by the extracellular matrix. Am. J. Path 1984; 117: 349–354
   PubMed Web of Science ®Google Scholar
• Ranchalis J. E., Gentry L., Ogawa Y., Seyedin S. M., McPherson J., Purchio A., Twardzik D. R. Bone‐derived and recombinant transforming growth factor‐betas are potent inhibitors of tumor cell growth. Biochem. and Biophys. Res. Comm 1987; 148(2)783–789
   PubMedGoogle Scholar
• Rizzino A. Review: Transforming growth factor‐beta: multiple effects on cell differentiation and extracellular matrices. Devel. Biol 1988; 130: 411–422
   PubMed Web of Science ®Google Scholar
• Roberts A. B., Sporn M. B. Transforming growth factor‐beta. Adv. Cancer Res 1988; 51: 107–145
   PubMed Web of Science ®Google Scholar
• Roberts A. B., Sporn M. B. The transforming growth factor‐betas. Peptide Growth Factors and Their Receptors, M. B. Sporn, A. B. Roberts. Handbook of Experimental Pharmacology, Springer‐Verlag, Heidelberg 1990; Vol. 95: 419–472
   Google Scholar
• Roll F. J., Madri J. A., Albert J., Furthmayr H. Co‐distribution of collagen types IV and AB2 in basement membranes and mesangium of the kidney. J. Cell Biol 1980; 85: 597–616
   PubMed Web of Science ®Google Scholar
• Rosa F., Roberts A. B., Danielpour D., Dart L. L., Sporn M. B., Dawid I. B. Mesoderm induction in amphibians: the role of transforming growth factor‐beta2‐like factors. Science 1988; 239: 783–785
   PubMed Web of Science ®Google Scholar
• Sato Y., Rifkin D. B. Inhibition of endothelial cell movements by pericytes and smooth muscle cells; activation of a latent transforming growth factor‐beta1‐like molecule by plasma during co‐culture. J. Cell Biol 1989; 109: 309–315
   PubMed Web of Science ®Google Scholar
• Segarini P. R., Roberts A. B., Rosen D. M., Seyedin S. M. Membrane binding characteristics of two forms of transforming growth factor‐beta. J. Biol. Chem 1987; 262(30)14655–14662
   PubMedGoogle Scholar
• Seyedin S. M., Segarini P. R., Rosen D. M., Thompson A. Y., Bentz H., Graycar J. Cartilage‐inducing factor‐β is a unique protein structurally and functionally related to transforming growth factor‐beta. J. Biol. Chem 1987; 262(5)1946–1949
   PubMed Web of Science ®Google Scholar
• Simionescu N., Simionescu M. Endothelial Cell Biology. Plenum Publishing Corp., NY 1988
   Google Scholar
• Sporn M. B., Roberts A. B. TGF‐β: problems and prospects. Cell Reg 1990; 1: 875–882
   PubMedGoogle Scholar
• ten Dijke P., Geurts van Kessel A. H. M., Foulkes J. G., LeBeau M. M. TGF‐β3 maps to human chromosome 14, region q23‐q24. Oncogene 1988a; 3: 721–724
   PubMed Web of Science ®Google Scholar
• ten Dijke P., Hanson P., Iwata K. K., Pieler C., Foulkes J. G. Identification of a new member of the transforming growth factor‐p gene family. Proc. Natl. Acad. Sci. (USA) 1988b; 85: 4715–4719
   PubMed Web of Science ®Google Scholar
• ten Dijke P., Iwata K. K., Goddard C., Pieler C., Canalis E., McCarthy T. L., Centrella M. Recombinant TGF‐type β3: biological activities and receptor binding properties in isolated bone cells. Mol. Cell. Biol. (USA) 1990; 10(9)4473–4479
   PubMedGoogle Scholar
• Wakefield L. M., Smith D. M., Broz S., Jackson M., Levin‐son A. D., Sporn M. B. Recombinant TGF‐β1 is synthesized as a two‐component latent complex that shares some structural features with the native platelet latent TGF‐PI complex. Growth Factors 1989; 1: 203–218
   PubMed Web of Science ®Google Scholar