Effect of Plasma Fibronectin, Macrophages, and Glycosaminoglycans on Tumor Cell Growth

References

• Mosher D F. Fibronectin. Prog Hemostasis Thrombosis 1980; 5: 111–151
   PubMedGoogle Scholar
• Mosher D F, Furcht L T. Fibronectin: Review of its structure and possible functions. J Invest Dermatol 1981; 77: 175–180
   PubMed Web of Science ®Google Scholar
• Robbins A B, Doran J E, Reese A C. Effect of cholecystectomy on cold insoluble globulin. Arch Surg 1980; 115: 1207–1209
   PubMed Web of Science ®Google Scholar
• Robbins A B, Doran J E, Reese A C. Cold insoluble globulin levels in operative trauma: Serum depletion, wound sequestration, and biological activity: An experimental and clinical study. Am Surgeon 1980; 46: 663–672
   PubMed Web of Science ®Google Scholar
• Saba T M, Scovill W A. Effect of surgical trauma on host defense. Surg Annu 1975; 7: 71–102
   PubMedGoogle Scholar
• Cho E, Saba T M. Effect of bilateral nephrectomy on plasma fibronectin levels-Its influence on acute fibronectin response to trauma and RE blockade. Adv Shock Res 1982; 8: 99–110
   PubMedGoogle Scholar
• Lanser M E, Saba T M. Opsonic glycoprotein (plasma fibronectin) enhances bacterial phagocytosis by neutrophils. J Reticuloendothel Soc 1980; 28: 21a
   Google Scholar
• Grossman J E, Demling R H, Duy N D. Response of plasma fibronectin to major body bum. J Trauma 1980; 20: 967–970
   PubMed Web of Science ®Google Scholar
• Saba T M, Blumenstock F A, Scovill W A. Cryoprecipitate reversal of opsonic alpha-2-surface binding glycoprotein deficiencies in septic surgical and trauma patients. Science 1978; 201: 622–624
   PubMed Web of Science ®Google Scholar
• Pisano J C, Di Luzio N R, Salky N K. Absence of macrophage humoral recognition factor (s) in patients with carcinoma. J Lab Clin Med 1970; 76: 141–150
   PubMedGoogle Scholar
• Pisano J C, Jackson J P, Di Luzio N R. Dimensions of humoral recognition factor depletion in carcinomatous patients. Cancer Res 1972; 32: 11–15
   PubMed Web of Science ®Google Scholar
• Hynes R O. Alteration of cell-surface proteins by viral transformation and by proteolysis. Proc Natl Acad Sci USA 1973; 70: 3170–3174
   PubMed Web of Science ®Google Scholar
• Saba T M, Antikatzides T G. Decreased resistance to intravenous tumor-cell challenge during reticuloendothelial depression following surgery. Br J Cancer 1976; 34: 381–389
   PubMed Web of Science ®Google Scholar
• Roberts S, Long D, Jonassen O. The isolation of cancer cells from the blood streams during uterine curettage. Surg Gynecol Obstet 1960; 111: 3–11
   PubMedGoogle Scholar
• El Rifi K, Bacon B, Methigan J. Increased incidence of pulmonary metastases after celiotomy: Counteraction by heparin. Arch Surg 1965; 91: 625–629
   PubMed Web of Science ®Google Scholar
• Saba T M, Cho E. Alteration of tumor growth by a purified alpha-2-glycoprotein. J Reticuloendothel Soc 1977; 22: 583–596
   PubMedGoogle Scholar
• Keller R. Cytostatic elimination of syngeneic rat tumor cells in vitro by nonspecifically activated macrophages. J Exp Med 1973; 138: 625–644
   PubMed Web of Science ®Google Scholar
• Keller R. Cytostatic and cytocidal effects of activated macrophages. Immunobiology of the Macrophage, D S Nelson. Academic Press, Inc, New York 1976
   Google Scholar
• Kranbuhl J L. Effects of activated macrophages on tumor target cells in discrete phases of the cell cycle. Cancer Res 1980; 40: 4622–4627
   PubMed Web of Science ®Google Scholar
• Mantovani A, Sessa C, Peri G. Intraperitoneal administration of Corynebacterium parvum in patients with ascitic ovarian tumors resistant to chemotherapy: Effects on cytotoxicity of tumor-associated macrophages and NK cells. Int J Cancer 1981; 27: 437–446
   PubMed Web of Science ®Google Scholar
• Schultz R N, Chirigos M A. Macrophage activation for nonspecific tumor cytotoxicity. Adv Pharmacol Chemother 1980; 17: 157–193
   PubMedGoogle Scholar
• Doran J E, Mansberger A R, Reese A C. Cold insoluble globulin enhanced phagocytosis of gelatinized targets by macrophage monolayers: A model system. J Reticuloendothel Soc 1980; 27: 471–483
   PubMedGoogle Scholar
• Doran J E, Mansberger A R, Edmondson H T. Cold insoluble globulin and heparin interactions in phagocytosis by macrophage monolayers: Lack of heparin requirement. J Reticuloendothel Soc 1981; 29: 275–284
   PubMedGoogle Scholar
• Doran J E, Mansberger A R, Edmondson H T. Cold insoluble globuline and heparin interactions in phagocytosis by macrophage monolayers: Mechanism of heparin enhancement. J Reticuloendothel Soc 1981; 29: 285–294
   PubMedGoogle Scholar
• Gudewicz P W, Molnar J, Lai M. Fibronectin mediated uptake of gelatin-coated latex particles by peritoneal macrophages. J Cell Biol 1981; 87: 427–433
   Web of Science ®Google Scholar
• Bevilacqua M P, Amrani D, Mosesson M W. Receptors for cold-insoluble globulin (plasma fibronectin) on human monocytes. J Exp Med 1981; 153: 42–60
   PubMed Web of Science ®Google Scholar
• Perri R T, Kay N E, McCarthy J. Fibronectin enhances in vitro monocytemacrophage-mediated tumoricidal activity. Blood 1982; 60: 430–435
   PubMed Web of Science ®Google Scholar
• Jilek F, Horman H. Fibronectin (cold-insoluble globulin). VI. Influence of heparin and hyaluronic acid on the binding of native collagen. Hoppe-Seyler Z Physiol Chem 1979; 360: 597–603
   PubMedGoogle Scholar
• Johansson S, Hook M. Heparin enhances the rate of binding of fibronectin to collagen. J Biochem 1980; 187: 521–524
   Google Scholar
• Ruoslahti E, Pierschbacher M, Hayman E G. Fibronectin: A molecule with remarkable structural and functional diversity. Trends Biochem Sci 1982; 7: 188–190
   Web of Science ®Google Scholar
• Hormann H, Jelinic V. Regulation by heparin and hyaluronic acid of the fibronectin-dependent association of collagen, type III, with macrophages. Hoppe-Seyler Z Physiol Chem 1981; 362: 87–94
   PubMedGoogle Scholar
• Saba T M, Filkins J P, Di Luzio N R. Properties of the opsonic system regulating in vitro hepatic phagocytosis. J Reticuloendothel Soc 1966; 3: 398–414
   Google Scholar
• Van De Water L, III, Schroeder S, Crenshaw E B. Phagocytosis of gelatin-latex particles by a murine macrophage line is dependent on fibronectin and heparin. J Cell Biol 1981; 90: 32–39
   PubMed Web of Science ®Google Scholar
• Yamada K M, Kennedy D W, Kimata K. Characterization of fibronectin interactions with glycosaminoglycans and identification of active propteolytic fragments. J Biol Chem 1980; 255: 6055–6063
   PubMed Web of Science ®Google Scholar
• Howard E F, Scott D F, Bennett C E. Stimulation of thymidine uptake and cell proliferation in mouse embryo fibroblasts by conditioned medium from mammary cells in culture. Cancer Res 1976; 36: 4543–4551
   PubMed Web of Science ®Google Scholar
• Engvall E, Ruoslahti E. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer 1977; 20: 1–5
   PubMed Web of Science ®Google Scholar
• Porath J, Aspberg K, Drevin H. Preparation of cyanogen bromideactivated agarose gels. J Chromatogr 1973; 86: 53–56
   Web of Science ®Google Scholar
• Check I J, Wolfman H C, Coley T B. Agglutination assay for human opsonic factor using gelatin-coated latex particles. J Reticuloendothel Soc 1979; 25: 351–362
   PubMedGoogle Scholar
• Steele R GD, Torrie J H. Principles and Procedures of Statistics, 2nd ed. McGraw-Hill, New York 1980
   Google Scholar
• Newman D. The distribution of range in samples from a normal population, expressed in terms of an independent estimate of standard deviation. Biometrika 1939; 31: 20–30
   Google Scholar
• Keuls M. The use of the “standardized range” in connection with an analysis of variance. Euphytica 1952; 1: 112–122
   Google Scholar
• Young D C, Doran J E, Mansberger A R. Effect of cold insoluble globulin on carcinoma cell growth in vitro. Oncology 1981; 38: 295–300
   PubMed Web of Science ®Google Scholar
• Chapes S K, Haskill S. Role of Corynebacterium parvum in the activation of peritoneal macrophages. I. Association between intracellular C. parvum and cytotoxic macrophages. Cell Immunol 1982; 70: 65–75
   PubMed Web of Science ®Google Scholar
• Olivotto M, Bomford R. In vitro inhibition of tumour cell growth and DNA synthesis by peritoneal and lung macrophages from mice injected with Corynebacterium parvum. Int J Cancer 1974; 13: 478–488
   PubMed Web of Science ®Google Scholar
• Keller R. Major changes in lymphocyte proliferation evoked by activated macrophages. Cell Immunol 1975; 17: 542–551
   PubMed Web of Science ®Google Scholar
• Alitalo K, Hovi T, Vaheri A. Fibronectin is produced by human macrophages. J Exp Med 1980; 151: 602–613
   PubMed Web of Science ®Google Scholar
• Rennard S I, Hunninghake G W, Bitterman P B. Production of fibronectin by the human alveolar macrophage: Mechanism for the recruitment of fibroblasts to sites of tissue injury in interstitial lung diseases. Proc Natl Acad Sci USA 1981; 78: 7147–7151
   PubMed Web of Science ®Google Scholar
• Opitz H G, Niethammer D, Lemke H. Inhibition of 3H-thymidine incorporation of lymphocytes by a soluble factor from macrophages. Cell Immunol 1975; 16: 379–388
   PubMed Web of Science ®Google Scholar
• Stathakis N E, Mosesson M W. Interactions among heparin, cold insoluble globulin and fibrinogen in formatin of the heparin percipitable fraction of plasma. J Clin Invest 1977; 60: 855–865
   PubMed Web of Science ®Google Scholar
• Bleiberg I, Macgregor I, Aronson M. Heparin receptors on mouse macrophages. Thrombosis 1983; 29: 53–61
   PubMed Web of Science ®Google Scholar
• Mosesson M W, Amrani D L. Review: The structure and biologic activities of plasma fibronectin. Blood 1980; 56: 145–158
   PubMed Web of Science ®Google Scholar
• Ruoslahti E, Engvall E, Hayman E G. Fibronectin: Current concepts of its structure and function. Coll Res 1981; 1: 95–128
   Web of Science ®Google Scholar
• Smith D E, Furcht L T. Localization of two unique heparin binding domains of human fibronectin with monoclonal antibodies. J Biol Chem 1982; 257: 6518–6523
   PubMed Web of Science ®Google Scholar
• Akiyama S K, Yamada K M, Hayashi M. The structure of fronectin and its role in cellular adhesion. J Supramol Struc Cell Biochem 1981; 16: 345–358
   PubMedGoogle Scholar