Cyclosporine A Inhibits Induction of DNA Synthesis by PDGF and Other Peptide Mitogens in Cultured Rat Aortic Smooth Muscle Cells and Dermal Fibroblasts

References

• Barrett T. B., Benditt E. P. Platelet-derived growth factor gene expression in human atherosclerotic plaques and normal artery wall. Proc. Natl. Acad. Sri. USA 1988; 85: 2810–2814
   PubMed Web of Science ®Google Scholar
• Bijsterbosch M. K., Klaus G. G. B. Cyclosporine does not inhibit mitogen-induced inositol phospolipid degradation in mouse lymphocytes. Immunology 1985; 56: 435–440
   PubMed Web of Science ®Google Scholar
• Borel J. F., Ryffel B. The mechanism of action of ciclosporin: a continuing puzzle. Ciclosporin in Autoimmune Diseases, R. Schindler. Springer, Berlin 1985; 24–32
   Google Scholar
• Bottger B. A., Sjolund M., Thyberg J. Chloroquine and monensin inhibit induction of DNA synthesis in rat arterial smooth muscle cells stimulated with platelet-derived growth factor. Cell Tissue Res. 1988; 252: 275–285
   PubMed Web of Science ®Google Scholar
• Bottger B. A., Hedin U., Johansson S., Thyberg J. Integrin-type receptors of rat arterial smooth muscle cells: isolation, partial characterization and role in cytoskeletal organization and control of differentiated properties. Differentiation 1989; 41: 158–167
   PubMedGoogle Scholar
• Bravo R., Zerial M., Toschi L., Schurmann M., Müller R., Hirai S. I., Yaniv M., Almendral J. M., Ryseck R.-P. Identification of growth-factor-inducible genes in mouse fibroblasts. Cold Spring Harbor Symp. 1988; 53: 901–905
   PubMedGoogle Scholar
• Burgess W. H., Maciag T. The heparin-binding (fibroblast) growth factor family of proteins. Annu. Rev. Biochem. 1989; 58: 575–606
   PubMed Web of Science ®Google Scholar
• Castellot J. J., Jr., Pukac L. A., Caleb B. L., Wright T. C., Jr., Karnovsky M. J. Heparin selectively inhibits a protein kinase C-dependent mechanism of cell cycle progression in calf aortic smooth muscle cells. J. Cell Biol. 1989; 109: 3147–3155
   PubMed Web of Science ®Google Scholar
• Chabannes D., Moreau J.-F., Soulillou J.-P. Effect of cyclosporine, cyclosporine metabolite 17, and other cyclo-sporine-related compounds on T lymphocyte clones derived from rejected human kidney grafts. Transplantation 1987; 44: 813–817
   Google Scholar
• Chamley-Campbell J., Campbell G. R., Ross R. The smooth muscle cell in culture. Physiol. Rev. 1979; 59: 1–61
   PubMed Web of Science ®Google Scholar
• Chamley-Campbell J. H., Campbell G. R., Ross R. Phenotype-dependent response of cultured aortic smooth muscle to serum mitogens. J. Cell Biol. 1981; 89: 379–383
   PubMed Web of Science ®Google Scholar
• Chiara M. D., Bedoya F., Sobrino F. Cyclosporin A inhibits phorbol ester-induced activation of superoxide production in resident mouse peritoneal macrophages. Biochem. J. 1989; 264: 21–26
   Google Scholar
• Czech M. P. Signal transmission by the insulin-like growth factors. Cell 1989; 59: 235–238
   PubMedGoogle Scholar
• Deuel T. F. Polypeptide growth factors: roles in normal and abnormal cell growth. Annu. Rev. Cell Biol. 1987; 3: 443–492
   PubMedGoogle Scholar
• Emmel E. A., Verweij C. L., Durand D. B., Higgins K. M., Lacy E., Crabtree G. R. Cyclosporin A specifically inhibits function of nuclear proteins involved in T cell activation. Science 1989; 246: 1617–1620
   PubMed Web of Science ®Google Scholar
• Fischer G., Wittmann-Liebold B., Lang K., Kiefhaber T., Schmid F. X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 1989; 337: 476–478
   PubMed Web of Science ®Google Scholar
• Foxwell B. M. J., Mackie A., Ling V., Ryffel B. Identification of the multidrug resistance-related P-glycoprotein as a cyclosporine binding protein. Mot. Pharmacol. 1989; 36: 543–546
   PubMed Web of Science ®Google Scholar
• Gown A. M., Tsukada T., Ross R. Human atherosclerosis. II. Immunocytochemical analysis of the cellular composition of human atherosclerotic lesions. Amer. J. Pathol. 1986; 125: 191–207
   PubMed Web of Science ®Google Scholar
• Hanks S. K., Quinn A. M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988; 241: 42–52
   PubMed Web of Science ®Google Scholar
• Hannink M., Donoghue D. J. Structure and function of platelet-derived growth factor (PDGF) and related proteins. Biochim. Biophys. Acta 1989; 989: 1–10
   PubMed Web of Science ®Google Scholar
• Hansson G. K., Jonasson L., Holm J., Clowes M. M., Clowes A. W. γ-Interferon regulates vascular smooth muscle proliferation and la antigen expression in vivo and in vitro. Ore. Res. 1988; 63: 712–719
   Google Scholar
• Hansson G. K., Hellstrand M., Rymo L., Rubbia L., Gabbiani G. Interferon γ inhibits both proliferation and expression of differentiation-specific a-smooth muscle actin in arterial smooth muscle cells. J. Exp. Med. 1989; 170: 1595–1608
   PubMed Web of Science ®Google Scholar
• Hansson G. K., Jonasson L., Seifert P. S., Stemme S. Immune mechanisms in atherosclerosis. Arteriosclerosis 1989; 9: 567–578
   PubMedGoogle Scholar
• Hedin U., Thyberg J. Plasma fibronectin promotes modulation of arterial smooth muscle cells from contractile to synthetic phenotype. Differentiation 1987; 33: 239–246
   PubMedGoogle Scholar
• Hedin U., Bottger B. A., Forsberg E., Johansson S., Thyberg J. Diverse effects of fibronectin and laminin on phenotypic properties of cultured arterial smooth muscle cells. J. Cell Biol. 1988; 107: 307–319
   PubMed Web of Science ®Google Scholar
• Hedin U., Bottger B. A., Luthman J., Johansson S., Thyberg J. A substrate of the cell-attachment sequence of fibronectin (Arg-Gly-Asp-Ser) is sufficient to promote transition of arterial smooth muscle cells from a contractile to a synthetic phenotype. Dev. Biol. 1989; 133: 489–501
   PubMedGoogle Scholar
• Hedin U., Sjölund M., Hultgårdh-Nilsson A., Thyberg J. Changes in expression and organization of smooth muscle-specific a-actin during fibronectin-mediated modulation of arterial smooth muscle cell phenotype. Differentiation. 1990; 44: 222–231
   PubMedGoogle Scholar
• Heldin C.-H., Westermark B. Platelet-derived growth factor: three isoforms and two receptor types. Trends Genet. 1989; 5: 108–111
   PubMedGoogle Scholar
• Hess A. D., Colombani P. M. Mechanism of action: in vitro studies. Progr. Allergy 1986; 38: 198–221
   PubMedGoogle Scholar
• Isakov N., Mally M. I., Scholz W., Altman A. T-lymphocyte activation: the role of protein kinase C and the bifurcating inositol phospholipid signal transduction pathway. Immunol. Rev. 1987; 95: 89–111
   PubMed Web of Science ®Google Scholar
• Jonasson L., Holm J., Skalli O., Gabbiani G., Hansson G. K. Expression of class II transplantation antigen on vascular smooth muscle cells in human atherosclerosis. J. Clin. Invest. 1985; 76: 125–131
   PubMed Web of Science ®Google Scholar
• Jonasson L., Holm J., Skalli O., Bondjers G., Hansson G. K. Regional accumulations of T cells, macrophages, and smooth muscle cells in the human atherosclerotic plaque. Arteriosclerosis 1986; 6: 131–138
   PubMedGoogle Scholar
• Jonasson L., Holm J., Hansson G. K. Smooth muscle cells express la antigens during arterial response to injury. Lab. Invest. 1988a; 58: 310–315
   PubMed Web of Science ®Google Scholar
• Jonasson L., Holm J., Hansson G. K. Cyclosporin A inhibits smooth muscle proliferation in the vascular response to injury. Proc. Natl. Acad. Sci. USA 1988b; 85: 2303–2306
   PubMed Web of Science ®Google Scholar
• Klagsbrun M., Edelman E. R. Biological and biochemical properties of fibroblast growth factors. Implications for the pathogenesis of atherosclerosis. Arteriosclerosis 1989; 9: 269–278
   PubMedGoogle Scholar
• Libby P., Warner S. J. C., Salomon R. N., Birinyi L. K. Production of platelet-derived growth factor-like mitogen by smooth-muscle cells from human atheroma. N. Engl. J. Med. 1988; 318: 1493–1498
   PubMed Web of Science ®Google Scholar
• Martin M., Krichbaum M., Kaever V., Goppelt-Striibe M., Resch K. Cyclosporin A suppresses proliferation of renal mesangial cells in culture. Biochem. Pharmacol. 1988; 37: 1083–1088
   PubMed Web of Science ®Google Scholar
• Meyer-Lehnert H., Schrier R. W. Potential mechanism of cyclosporine A-induced vascular smooth muscle contraction. Hypertension 1989; 13: 352–360
   PubMed Web of Science ®Google Scholar
• Ostman A., Backstrom G., Fong N., Betsholtz C., Wernstedt C., Hellman U., Westermark B., Valenzuela P., Heldin C.-H. Expression of three recombinant homodimeric isoforms of PDGF in Saccharomyces cerevisiae: evidence for difference in receptor binding and functional activities. Growth Factors 1989; 1: 271–281
   PubMed Web of Science ®Google Scholar
• Pardee A. B. G, events and regulation of cell proliferation. Science 1989; 246: 603–608
   PubMed Web of Science ®Google Scholar
• Pomerantz K. B., Hajjar D. P. Eicosanoids in regulation of arterial smooth muscle cell phenotype, proliferative capacity, and cholesterol metabolism. Arteriosclerosis 1989; 9: 413–429
   PubMedGoogle Scholar
• Ross R. The pathogenesis of atherosclerosis–an update. N. Engl. J. Med. 1986; 314: 488–500
   PubMed Web of Science ®Google Scholar
• Ross R., Raines E. W., Bowen-Pope D. F. The biology of platelet-derived growth factor. Cell 1986; 46: 155–169
   PubMed Web of Science ®Google Scholar
• Ruoslahti E., Hayman E. G., Pierschbacher M., Engvall E. Fibronectin: purification, immunochemical properties, and biological activities. Methods Enzymol. 1982; 82: 803–831
   PubMed Web of Science ®Google Scholar
• Sachinidis A., Locher R., Vetter W., Tatje D., Hoppe J. Different effects of platelet-derived growth factor isoforms on rat vascular smooth muscle cells. J. Biol. Chem. 1990; 265: 10238–10243
   PubMed Web of Science ®Google Scholar
• Schlessinger J. The epidermal growth factor receptor as a multifunctional allosteric protein. Biochemistry 1988; 27: 3119–3123
   PubMed Web of Science ®Google Scholar
• Schwartz S. M., Campbell G. R., Campbell J. H. Replication of smooth muscle cells in vascular disease. Circ. Res. 1986; 58: 427–444
   PubMed Web of Science ®Google Scholar
• Seifert R. A., Schwartz S. M., Bowen-Pope D. F. Developmentally regulated production of platelet-derived growth factor-like molecules. Nature 1984; 311: 669–671
   PubMed Web of Science ®Google Scholar
• Shevach E. M. The effects of cyclosporin A on the immune system. Annu. Rev. Immunol. 1985; 3: 397–423
   PubMed Web of Science ®Google Scholar
• Sjolund M., Rahm M., Claesson-Welsh L., Sejersen T., Heldin C.-H., Thyberg J. Expression of PDGF-α and β-receptors in rat arterial smooth muscle cells is phenotype and growth state dependent. Growth Factors. 1990; 3: 191–203
   PubMedGoogle Scholar
• Skalli O., Gabbiani G. The biology of the myofibroblast. Relationship to wound contraction and fibrocontractive diseases. The Molecular and Cellular Biology of Wound Repair, R. A, F. Clark, P. M. Henson. Plenum, New York 1988; 373–402
   Google Scholar
• Soltoff S. P., Cantley L. C. Mitogens and ion fluxes. Annu. Rev. Physiol. 1988; 50: 207–223
   PubMedGoogle Scholar
• Sraer J., Bens M., Ardaillou R. Dual effects of cyclosporine A on arachidonate metabolism by peritoneal macrophages. Phospholipase activation and partial thromboxane-synthase blockage. Biochem. Pharmacol. 1989; 38: 1947–1954
   Google Scholar
• Takahashi N., Hayano T., Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporine A-binding protein cyclo-philin. Nature 1989; 337: 473–475
   PubMed Web of Science ®Google Scholar
• Thyberg J., Palmberg L., Nilsson J., Ksiazek T., Sjolund M. Phenotype modulation in primary cultures of arterial smooth muscle cells. On the role of platelet-derived growth factor. Differentiation 1983; 25: 156–167
   PubMedGoogle Scholar
• Thyberg J., Hedin U., Bottger B. A. Attachment substrates for smooth muscle cells. Cell Culture Techniques in Heart and Vessel Research, H. M. Piper. Springer Verlag, Berlin 1990a; 315–333
   Google Scholar
• Thyberg J., Hedin U., Sjölund M., Palmberg L., Bottger B. A. Regulation of differentiated properties and proliferation of arterial smooth muscle cells. Arteriosclerosis. 1990b; 10: 966–990, in press
   PubMedGoogle Scholar
• Warner S. J. C., Friedman G. B., Libby P. Regulation of major histocompatibility gene expression in human vascular smooth muscle cells. Arteriosclerosis 1989; 9: 279–288
   PubMedGoogle Scholar
• Wenger R. M. Pharmacology of cyclosporin (Sandimmune). II. Chemistry. Pharmacol. Rev. 1989; 41: 243–247
   Google Scholar
• Westermark B., Heldin C.-H. Similar action of platelet-derived growth factor and epidermal growth factor in the prereplicative phase of human fibroblasts suggests a common intracellular pathway. J. Cell. Physiol. 1985; 124: 43–48
   PubMed Web of Science ®Google Scholar
• Whitman M., Cantley L. Phosphoinositide metabolism and the control of cell proliferation. Biochim. Biophys. Acta 1988; 948: 327–344
   Web of Science ®Google Scholar
• Wickremasinghe R. G. The role of prostaglandins in the regulation of cell proliferation. Prostagland. Leuk. Essent. Fatty Acids 1988; 31: 171–179
   PubMed Web of Science ®Google Scholar
• Wilcox J. N., Smith K. M., Williams L. T., Schwartz S. M., Gordon D. Platelet-derived growth factor mRNA detection in human atherosclerotic plaques by in situ hybridization. J. Clin. Invest. 1988; 82: 1134–1143
   PubMed Web of Science ®Google Scholar
• Williams L. T. Signal transduction by the platelet-derived growth factor receptor. Science 1989; 243: 1564–1570
   PubMed Web of Science ®Google Scholar
• Wiskocil R., Weiss A., Imboden J., Kamin-Lewis R., Stobo J. Activation of a human T cell line: a two-stimulus requirement in the pretranslational events involved in the coordinate expression of interleukin 2 and γ-interferon genes. J. Immunol. 1985; 134: 1599–1603
   PubMedGoogle Scholar
• Yarden Y., Ullrich A. Molecular analysis of signal transduction by growth factors. Biochemistry 1988; 27: 3113–3119
   PubMed Web of Science ®Google Scholar