Advertisement

Physiology pp 331-352 | Cite as

Selected Aspects of Protein Metabolism in Relation to Reticuloendothelial System, Lymphocyte, and Fibroblast Function

  • Michael C. Powanda
  • Elizabeth D. Moyer

Abstract

For the purposes of this discussion, the reticuloendothelial or mononuclear phagocyte system will be considered to include monocytes, histiocytes, Kupffer cells, alveolar macrophages, and phagocytic cells in spleen, lymph nodes, bone marrow, the nervous system, and the pleural and peritoneal cavities (Bloom and Fawcett, 1975). Fibroblasts, which are facultative phagocytes, are not usually included in the RES, nor are lymphocytes, but both cell types interact with mononuclear cells in the performance of their functions (Pierce, 1980; Leibovich and Ross, 1975). There are a number of plasma proteins (excluding immunoglobulins) which may play roles in host defense against infection and in wound healing. Some of these are synthesized by, catabolized within, and/or adherent to RES cells, lymphocytes, and fibroblasts. The possible consequences of these protein-cell interactions are the focus of this chapter.

Keywords

Alveolar Macrophage Bullous Pemphigoid Familial Hypercholesterolemia Lecithin Cholesterol Acyl Transferase Homozygous Familial Hypercholesterolemia 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Ahlstedt, S., 1980, Inflammatory potency of antigen-antibody complexes and C-reactive protein in a wound chamber model in rats, Int. Arch. Allergy Appl. Immunol. 62:341.PubMedCrossRefGoogle Scholar
  2. Alitalo, K., Hovi, T., and Vaheri, A., 1980, Fibronectin is produced by human macrophages, J. Exp. Med. 151:602.PubMedCrossRefGoogle Scholar
  3. Alper, C. A., Raum, D., Awdeh, Z. L., Petersen, B. H., Taylor, P. D., and Starzl, T. E., 1980, Studies of hepatic synthesis in vivo of plasma proteins, including orosomucoid, transferrin, α1-antitrypsin, C8, and factor B, Clin. Immunol. Immunopathol. 16:84.PubMedCrossRefGoogle Scholar
  4. Ambruso, D. R., and Johnston, R. B., Jr., 1981, Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and an enzymatic generating system, J. Clin. Invest. 67:352.PubMedCrossRefGoogle Scholar
  5. Arora, P. K., Miller, H. C., and Aronson, L. D., 1978, α1-Antitrypsin is an effector of immunological stasis, Nature (London) 274:589.CrossRefGoogle Scholar
  6. Balian, G., Click, E. M., Crouch, E., Davidson, J. M., and Bornstein, P., 1979, Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin, J. Biol. Chem. 254:1429.PubMedGoogle Scholar
  7. Bata, J., Deviller, P., and Revillard, J. P., 1981, Binding of alpha 1 antitrypsin α1 protease inhibitor) to human lymphocytes, Biochem. Biophys. Res. Commun. 98:709.PubMedCrossRefGoogle Scholar
  8. Beamish, M. R., Jobbins, K., and Cavill, I., 1971, The cellular distribution of transferrin-bound iron in the skin, Br. J. Dermatol. 85:49.PubMedCrossRefGoogle Scholar
  9. Bensusan, H. B., Koh, T. L., Henry, K. G., Murray, B. A., and Culp, L. A., 1978, Evidence that fibronectin is the collagen receptor on platelet membranes, Proc. Natl. Acad. Sci. USA 75:5864.PubMedCrossRefGoogle Scholar
  10. Berghem, L., Ahlgren, T., and Lahnborg, G., 1979, Immunoassay of macrophage stimulating α2SB (surface binding) glycoprotein in pig plasma following missile trauma, Acta Chir. Scand. Suppl. 489:239.PubMedGoogle Scholar
  11. Blaauboer, B. J., and Paine, A. J., 1979, Attachment of rat hepatocytes to plastic substrata in the absence of serum requires protein synthesis, Biochem. Biophys. Res. Commun. 90:368.PubMedCrossRefGoogle Scholar
  12. Bloom, W., and Fawcett, D. W., 1975, A Textbook of Histology, 10th ed., pp. 178–181, Saunders, Philadelphia.Google Scholar
  13. Blumberg, P. M., and Robbins, P. W., 1975, Effect of proteases on activation of resting chick embryo fibroblasts and on cell surface proteins, Cell 6:137.PubMedCrossRefGoogle Scholar
  14. Blumenstock, F., Saba, T. M., Weber, P., and Cho, E., 1976, Purification and biochemical characterization of a macrophage stimulating alpha-2-globulin opsonic protein, J. Reticuloendothelial Soc. 19:157.Google Scholar
  15. Bostian, K. A., Blackburn, B. S., Wannemacher, R. W., Jr., McGann, V. G., and Beisel, W. R., 1976, Sequential changes in the concentration of specific serum proteins during typhoid fever infection in man, J. Lab. Clin. Med. 87:577.PubMedGoogle Scholar
  16. Brown, M. S., and Goldstein, J. L., 1974, Familial hypercholesterolemia: Defective binding of lipoproteins to cultured fibroblasts associated with impaired regulation of 3-hydroxy-3-meth-ylglutaryl coenzyme A reductase activity, Proc. Natl. Acad. Sci. USA 71:788.PubMedCrossRefGoogle Scholar
  17. Brown, M. S., and Goldstein, J. L., 1983, Lipoprotein metabolism in the macrophage: Implications for cholesterol deposition in atherosclerosis, Ann. Rev. Biochem. 52:223.PubMedCrossRefGoogle Scholar
  18. Brown, M. S., Ho, Y. K., and Goldstein, J. L., 1980, The cholesteryl ester cycle in macrophage foam cells, J. Biol. Chem. 255:9344.PubMedGoogle Scholar
  19. Cabana, V. G., Gerwurz, H., and Siegel, J. N., 1982, Interaction of very low density lipoproteins (VLDL) with rabbit C-reactive protein, J. Immunol. 128:2342.PubMedGoogle Scholar
  20. Chisari, F. V., 1980, Modulation of the in vivo immune response by human plasma very low-density lipoproteins, Cell. Immunol. 52:223.PubMedCrossRefGoogle Scholar
  21. Chisari, F. V., and Edgington, T. S., 1975, Lymphocyte E rosette inhibitory factor: A regulatory serum lipoprotein, J. Exp. Med. 142:1092.PubMedCrossRefGoogle Scholar
  22. Claus, D. R., Osmand, A. P., and Gewurz, H., 1976, Radioimmunoassay of human C-reactive protein and levels in normal sera, J. Lab. Clin. Med. 87:120.PubMedGoogle Scholar
  23. Cox, D. W., and Huber, O., 1980, Association of severe rheumatoid arthritis with heterozygosity for α1-antitrypsin deficiency, Clin. Genet. 17:153.PubMedCrossRefGoogle Scholar
  24. Croft, S. M., Mortensen, R. F., and Gewurz, H., 1976, Binding of C-reactive protein to antigeninduced but not mitogen-induced T lymphoblasts, Science 193:685.PubMedCrossRefGoogle Scholar
  25. Cryer, A., 1981, Tissue lipoprotein lipase activity and action in lipoprotein metabolism, Int. J. Biochem. 13:525.PubMedCrossRefGoogle Scholar
  26. Curtiss, L. K., DeHeer, D. H., and Edgington, T. S., 1977, In vivo suppression of the primary immune response by a species of low density serum lipoprotein, J. Immunol. 118:648.PubMedGoogle Scholar
  27. Curtiss, L. K., DeHeer, D. H., and Edgington, T. S., 1980, Influence of the immunoregulatory serum lipoprotein LDL-In on the in vivo proliferation and differentiation of antigen-binding and antibody-secreting lymphocytes during a primary immune response, Cell. Immunol. 49:1.PubMedCrossRefGoogle Scholar
  28. Daerr, W. H., Gianturco, S. H., Patsch, J. R., Smith, L. C., and Gotto, A. M., 1980, Stimulation and suppression of 3-hydroxy-3-methyl glutaryl coenzyme A reductase in normal human fibroblasts by high density lipoprotein subclasses, Biochim. Biophys. Acta 619:287.PubMedCrossRefGoogle Scholar
  29. Daniels, J. C., Larson, D. L., Abston, S., and Ritzmann, S. E., 1974a, Serum protein profiles in thermal burns. I. Serum electrophoretic patterns, immunoglobulins, and transport proteins, J. Trauma 14:137.PubMedCrossRefGoogle Scholar
  30. Daniels, J. C., Larson, D. L., Abston, S., and Ritzmann, S. E., 1974b, Serum protein profiles in thermal burns. II. Protease inhibitors, complement factors, and C-reactive protein, J. Trauma 14:153.PubMedCrossRefGoogle Scholar
  31. Debanne, M. T., Bell, R., and Dolovich, J., 1975, Uptake of proteinase-α-macroglobulin complexes by macrophages, Biochim. Biophys. Acta 411:295.PubMedCrossRefGoogle Scholar
  32. Dickson, I. R., and Manning, C. W., 1972, Changes in serum-alpha2-macroglobulin levels in children after major bone surgery, Lancet 2:484.PubMedCrossRefGoogle Scholar
  33. Dolovich, J., Debanne, M. T., and Bell, R., 1975, The role of alpha1-antitrypsin and alpha-macroglobulins in the uptake of proteinase by rabbit alveolar macrophages, Am. Rev. Respnr. Dis. 112:521.Google Scholar
  34. Durrington, P. N., 1982, High-density lipoprotein cholesterol: Methods and clinical significance, CRC Crit. Rev. Clin. Lab. Sci. 18:31.CrossRefGoogle Scholar
  35. Eisenberg, S., 1980, Plasma lipoprotein conversion: The origin of low-density and high-density lipoprotein, Ann. NY Acad. Sci. 348:30.PubMedCrossRefGoogle Scholar
  36. Elwyn, D. H., 1970, The role of the liver in regulation of amino acid and protein metabolism, in: Mammalian Protein Metabolism (H. N. Munro, ed.), pp. 523–557, Academic Press, New York.Google Scholar
  37. Emmelot, P., 1977, The organization of the plasma membranes of mammalian cells: Structure and relation to function, in: Mammalian Cell Membranes (G. A. Jamieson and D. M. Robinson, eds.), Vol. II, pp. 1–54, Butterworths, London.Google Scholar
  38. Eriksson, S., and Larsson, C., 1975, Purification and partial characterization of PAS-positive inclusion bodies from the liver in alpha1-antitrypsin deficiency, N. Engl. J. Med. 292:176.PubMedCrossRefGoogle Scholar
  39. Evans, G. W., and Winter, T. W., 1975, Zinc transport by transferrin in rat portal blood plasma, Biochem. Biophys. Res. Commun. 66:1218.PubMedCrossRefGoogle Scholar
  40. Farrow, S. P., and Baar, S., 1973, The metabolism of α2-macroglobulin in mildly burned patients, Clin. Chim. Acta 46:39.PubMedCrossRefGoogle Scholar
  41. Fiedel, B. A., and Gewurz, H., 1976, Effects of C-reactive protein on platelet function. I. Inhibition of platelet aggregation and release reactions, J. Immunol. 116:1289.PubMedGoogle Scholar
  42. Fischer, C. L., Gill, C., Forrester, M. G., and Nakamura, R., 1976, Quantitation of “acute-phase proteins” postoperatively: Value in detection and monitoring of complications, Am. J. Clin. Pathol. 66:840.PubMedGoogle Scholar
  43. Fryand, O., 1979, Studies on fibronectin in the skin. I. Indirect immunofluorescence studies in normal human skin, Br. J. Dermatol. 101:261.Google Scholar
  44. Fryand, O., 1980, Studies on fibronectin in the skin. VI. Intra-epidermal depositions in vulgar psoriasis, lupus erythematosus, bullous pemphigoid and dermatitis herpetiformis, Acta Dermatovener 60:393.Google Scholar
  45. Glaser, M., Nelken, D., Ofek, I., Bergner-Rabinowitz, S., and Ginsburg, I., 1973, Alpha globulin decreases resistance of mice to infection with group A Streptococcus, J. Infect. Dis. 127:303.PubMedCrossRefGoogle Scholar
  46. Goldstein, B. D., Witz, G., Amoruso, M., and Troll, W., 1979, Protease inhibitors antagonize the activation of polymorphonuclear leukocyte oxygen consumption, Biochem. Biophys. Res. Commun. 88:854.PubMedCrossRefGoogle Scholar
  47. Goldstein, J. L., and Brown, M. S., 1974, Binding and degradation of low density lipoproteins by cultured human fibroblasts: Comparison of cells from a normal subject and from a patient with homozygous familial hypercholesterolemia, J. Biol. Chem. 249:5153.PubMedGoogle Scholar
  48. Goldstein, J. L., and Brown, M. S., 1983, Familial hypercholesterolemia, in: Metabolic Basis of Inherited Disease (J. B. Stanbury, J. B. Wyngaarden, D. S. Fredrickson, J. L. Goldstein, and M. S. Brown, eds.), 5th edition, p. 672–712, McGraw-Hill, New York.Google Scholar
  49. Goldstein, J. L., Ho, Y. K., Basu, S. K., and Brown, M. S., 1979, Binding site on macrophages that mediates uptake and degradation of acetylated low density lipoprotein, producing massive cholesterol deposition, Proc. Nat. Acad. Sci. USA, 76:333.PubMedCrossRefGoogle Scholar
  50. Goldstein, J. L., Ho, Y. K., Brown, M. S., Innerarity, T. L., and Mahley, R. W., 1980, Cholesteryl ester accumulation in macrophages resulting from receptor-mediated uptake and degradation of hypercholesterolemic canine β-very low density lipoproteins, J. Biol. Chem. 255:1839.PubMedGoogle Scholar
  51. Goutner, A., Simmler, M. C., Tapon, J., and Rosenfeld, C., 1976, Modulation by α-2 macroglobulin of human lymphocyte proliferation in response to mitogens and antigen, Differentiation 5:171.PubMedCrossRefGoogle Scholar
  52. Gravagna, P., Gianazza, E., Arnaud, P., Neels, M., and Ades, E. W., 1982, Modulation of the immune response by plasma protease inhibitors. II. Alpha2-macroglobulin subunits inhibit natural killer cell cytotoxicity and antibody-dependent cell-mediated cytotoxicity, Scand. J. Immunol. 15:115.PubMedCrossRefGoogle Scholar
  53. Grinnell, F., and Feld, M. K., 1979, Initial adhesion of human fibroblasts in serum-free medium: Possible role of secreted fibronectin, Cell 17:117.PubMedCrossRefGoogle Scholar
  54. Grinnell, F., Feld, M., and Snell, W., 1979, The influence of cold insoluble globulin on platelet morphological response to substrata, Cell Biol. Int. Rep. 3:585.PubMedCrossRefGoogle Scholar
  55. Haas, R. H., Dyck, R. F., Dubowitz, V., and Pepys, M. B., 1982, C-reactive protein in childhood dermatomyositis, Ann. Rheum. Dis. 41:483.PubMedCrossRefGoogle Scholar
  56. Harpel, P. C., 1982, Blood proteolytic enzyme inhibitors: their role in modulating blood coagulation and fibrinlytic enzyme pathways, in: Hemostasis and Thrombosis: Basic Principles and Clinical Practice (R. W. Colman, J. Hirsch, V. J. Marder and E. W. Salzman, eds.), pp. 738–747, J. B. Lippincott Co., Philadelphia.Google Scholar
  57. Hatcher, V. B., Lazarus, G. S., Levine, N., Burk, P. G., and Yost, F. J., Jr., 1977, Characterization of a chemotactic and cytotoxic proteinase from human skin, Biochim. Biophys. Acta 483:160.PubMedCrossRefGoogle Scholar
  58. Hayman, E. G., and Ruoslahti, E., 1979, Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix, J. Cell Biol. 83:255.PubMedCrossRefGoogle Scholar
  59. Henricksen, T., Evensen, S. A., and Carlander, B., 1979, Injury to cultured endothelial cells induced by low-density lipoproteins: protection by high density lipoproteins, Scand. J. Clin. Lab Invest. 39:369.CrossRefGoogle Scholar
  60. Ho, Y. K., Faust, J. R., Bilheimer, D. W., Brown, M. S., and Goldstein, J. L., 1977, Regulation of cholesterol synthesis by low density lipoprotein in isolated human lymphocytes: Comparison of cells from normal subjects and patients with homozygous familial hypercholesterolemia and abetalipoproteinemia, J. Exp. Med. 145:1531.PubMedCrossRefGoogle Scholar
  61. Hodges, J. R., Millward-Sadler, G. H., Barbatis, C., and Wright, R., 1981, Heterozygous MZ alpha1 antitrypsin deficiency in adults with chronic active hepatitis and cryptogenic cirrhosis, N. Engl. J. Med. 304:557.PubMedCrossRefGoogle Scholar
  62. Hokama, Y., Coleman, M. K., and Riley, R. F., 1962, In vitro effects of C-reactive protein on phagocytosis, J. Bacteriol. 83:1017.PubMedGoogle Scholar
  63. Hovi, T., Mosher, D., and Vaheri, A., 1977, Cultured human monocytes synthesize and secrete α2-macroglobulin, J. Exp. Med. 145:1580.PubMedCrossRefGoogle Scholar
  64. Howard, R. J., and Simmons, R. L., 1974, Acquired immunologic deficiencies after trauma and surgical procedures, Surg. Gynecol. Obstet. 139:771.PubMedGoogle Scholar
  65. Hsu, K-H. L., Ghanta, V. K., Duncan, L. A., Hunt, C. E., and Hiramoto, R. N., 1980, Characterization of an auto-rosette inhibitory fraction in mouse serum, J. Immunol. 125:1298.PubMedGoogle Scholar
  66. Hubbard, W. J., 1978, Hypothesis: Alpha-2 macroglobulin-enzyme complexes as suppressors of cellular activity, Cell. Immunol. 39:388.PubMedCrossRefGoogle Scholar
  67. Huybrechts-Godin, G., Hauser, P., and Vaes, G., 1979, Macrophage-fibroblast interactions in collagenase production and cartilage degradation, Biochem. J. 184:643.PubMedGoogle Scholar
  68. Innerarity, T. L., and Mahley, R. W., 1978, Enhanced binding by cultured human fibroblasts of apo-E containing lipoproteins as compared with low density lipoproteins, Biochemistry 17:1440.PubMedCrossRefGoogle Scholar
  69. Isaacson, P., Jones, D. B., and Judd, M. A., 1979, α1-Antitrypsin in human macrophages [Letter], Lancet 2:964.PubMedCrossRefGoogle Scholar
  70. James, K., Merriman, J., Gray, R. S., Duncan, L. J. P., and Herd, R., 1980, Serum α2-macroglobulin levels in diabetes, J. Clin. Pathol. 33:163.PubMedCrossRefGoogle Scholar
  71. James, K., Baum, L. L., Vetter, M. L., and Gewürz, H., 1982, Interactions of C-reactive protein with lymphoid cells, Ann. NY Acad. Sci. 389:274.PubMedCrossRefGoogle Scholar
  72. Janoff, A., Carp, H., Laurent, P., and Raju, L., 1983, The role of oxidative processes in emphysema, Am. Rev. Respir. Dis. 127:531.Google Scholar
  73. Jeejeebhoy, K. N., Ho, J., Greenberg, G. R., Phillips, M. J., Bruce-Robertson, A., and Sodtke, U., 1975, Albumin, fibrinogen and transferrin synthesis in isolated rat hepatocyte suspensions: A model for the study of plasma protein synthesis, Biochem. J. 146:141.PubMedGoogle Scholar
  74. Jeejeebhoy, K. N., Ho, J., Mehra, R., Jeejeebhoy, J., and Bruce-Robertson, A., 1977, Effects of hormones on the synthesis of α1 (acute-phase) glycoprotein in isolated rate hepatocytes, Biochem. J. 168:347.PubMedGoogle Scholar
  75. Jilek, F., and Hörmann, H., 1978, Fibronectin (cold-insoluble globulin). V. Mediation of fibrinmonomer binding to macrophages, Hoppe-Seylers Z. Physiol. Chem. 359:1603.PubMedGoogle Scholar
  76. Johansson, S., Rubin, K., Höök, M., Ahlgren, T., and Seljelid, R., 1979, In vitro biosynthesis of cold insoluble globulin (fibronectin) by mouse peritoneal macrophages, FEBS Lett. 105:313.PubMedCrossRefGoogle Scholar
  77. Johnson, K. J., and Varani, J., 1981, Substrate hydrolysis by immune complex-activated neutrophils: Effects of physical presentation of complexes and protease inhibitors, J. Immunol. 127:1875.PubMedGoogle Scholar
  78. Kampschmidt, R. F., 1978, Leukocytic endogenous mediator, J. Reticuloendothelial Soc. 23:287.Google Scholar
  79. Kaplan, J., and Nielsen, M. L., 1979, Analysis of macrophage surface receptors. II. Internalization of α-macroglobulin-trypsin complexes by rabbit alveolar macrophages, J. Biol. Chem. 254:7329.PubMedGoogle Scholar
  80. Kaplan, J. E., Molnar, J., Saba, T. M., and Allen, C., 1976, Comparative disappearance and localization of isotopically labeled opsonic protein and soluble albumin following surgical trauma, J. Reticuloendothelial Soc. 20:375.Google Scholar
  81. Kaplan, M. H., and Volanakis, J. E., 1974, Interaction of C-reactive protein complexes with the complement system. I. Consumption of human complement associated with the reaction of CRP with pneumococcal C-polysaccharide and with choline phosphatides, lecithin and sphingomyelin, J. Immunol. 112:2135.PubMedGoogle Scholar
  82. Kayden, H. J., Hatam, L., and Beratis, N. G., 1976, Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and the esterification of cholesterol in human long term lymphoid cell lines, Biochemistry 15:521.PubMedCrossRefGoogle Scholar
  83. Keski-Oja, J., Sen, A., and Todaro, G. J., 1980, Direct association of fibronectin and actin molecules in vitro, J. Cell Biol. 85:527.PubMedCrossRefGoogle Scholar
  84. Kindmark, C.-O., 1971, Stimulating effect of C-reactive protein on phagocytosis of various species of pathogenic bacteria, Clin. Exp. Immunol. 8:941.PubMedGoogle Scholar
  85. Kinnaert, P., Mahieu, A., and Van Geertruyden, N., 1978, Stimulation of antibody synthesis induced by surgical trauma in rats, Clin. Exp. Immunol. 32:243.PubMedGoogle Scholar
  86. Kitagawa, S., Takaku, F., and Sakamoto, S., 1980, Evidence that proteases are involved in superoxide production by human polymorphonuclear leukocytes and monocytes, J. Clin. Invest. 65:74.PubMedCrossRefGoogle Scholar
  87. Kluger, M. J., and Rothenburg, B. A., 1979, Fever and reduced iron: Their interaction as a host defense response to bacterial infection, Science 203:374.PubMedCrossRefGoogle Scholar
  88. Knowles, B. B., Howe, C. C., and Aden, D. P., 1980, Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen, Science 209:497.PubMedCrossRefGoogle Scholar
  89. Kronick, P. L., and Jimenez, S. A., 1979, Direct measurement of the amount of bound collagen which stimulates platelet aggregation, Thromb. Haemostasis 41:498.Google Scholar
  90. Kruth, H. S., Avigan, J., Gamble, W., and Vaughan, M., 1979, Effect of cell density on binding and uptake of low density lipoprotein by human fibroblasts, J. Cell Biol. 83:588.PubMedCrossRefGoogle Scholar
  91. Kukral, J. C., Sporn, J., Louch, J., and Winzler, R. J., 1963, Synthesis of alpha-and beta-globulins in normal and liverless dog, Am. J. Physiol. 204:262.Google Scholar
  92. Kushner, I., and Feldmann, G., 1978, Control of the acute phase response: Demonstration of C-reactive protein synthesis and secretion by hepatocytes during acute inflammation in the rabbit, J. Exp. Med. 148:466.PubMedCrossRefGoogle Scholar
  93. Kushner, I., and Kaplan, M. H., 1961, Studies of acute phase protein. I. An immunohistochemical method for the localization of Cx-reactive protein in rabbits: Association with necrosis in local inflammatory lesions, J. Exp. Med. 114:961.PubMedCrossRefGoogle Scholar
  94. Kushner, I., and Somerville, J. A., 1971, Permeability of human synovial membrane to plasma proteins: Relationship to molecular size and inflammation, Arthritis Rheum. 14:560.PubMedCrossRefGoogle Scholar
  95. Kushner, I., Rakita, L., and Kaplan, M. H., 1963, Studies of acute-phase protein. II. Localization of Cx-reactive protein in heart in induced myocardial infarction in rabbits, J. Clin. Invest. 42:286.PubMedCrossRefGoogle Scholar
  96. Kushner, I., Broder, M. L., and Karp, D., 1978, Control of the acute phase response: Serum C-reactive protein kinetics after acute myocardial infarction, J. Clin. Invest. 61:235.PubMedCrossRefGoogle Scholar
  97. Lanser, M. E., Saba, T. M., and Scovill, W. A., 1980, Opsonic glycoprotein (plasma fibronectin) levels after burn injury: Relationship to extent of burn and development of sepsis, Ann. Surg. 192:776.PubMedCrossRefGoogle Scholar
  98. Laurell, C.-B., and Jeppsson, J.-O., 1975, Protease inhibitors in plasma, in: The Plasma Proteins: Structure, Function and Genetic Control (F. W. Putnam, ed.), Vol. I, 2nd ed., pp. 229–264, Academic Press, New York.Google Scholar
  99. Layman, D. L., Jelen, B. J., and Illingworth, D. R., 1980, Inability of serum from abetalipoproteinemic subjects to stimulate proliferation of human smooth muscle cells and dermal fibroblasts in vitro, Proc. Natl. Acad. Sci. USA 77:1511.PubMedCrossRefGoogle Scholar
  100. Le Guilly, Y., Launois, B., Lenoir, P., and Bourel, M., 1973, Production of serum proteins by primary cultures of adult human liver, Biomedicine 19:248.Google Scholar
  101. Leibovich, S. J., and Ross, R., 1975, The role of the macrophage in wound repair: A study with hydrocortisone and antimacrophage serum, Am. J. Pathol. 78:71.PubMedGoogle Scholar
  102. Lieberman, J., 1973, Involvement of leukocytic proteases in emphysema and antitrypsin deficiency, Arch. Environ. Health 27:196.PubMedGoogle Scholar
  103. McDaniel, M. C., Laudico, R., and Papermaster, B. W., 1976, Association of macrophage-activation factor from a human cultured lymphoid cell line with albumin and α2-macroglobulin, Clin. Immunol. Immunopathol. 5:91.PubMedCrossRefGoogle Scholar
  104. McDonald, J. A., Baum, B. J., Rosenberg, D. M., Kelman, J. A., Brin, S. C., and Crystal, R. G., 1979, Destruction of a major extracellular adhesive glycoprotein (fibronectin) of human fibroblasts by neutral proteases from polymorphonuclear leukocyte granules, Lab. Invest. 40:350.PubMedGoogle Scholar
  105. Mahley, R. W., Inneraity, T. L., Pitas, R. E., Weisgraber, K. H., Brown, J. H., and Gross, E., 1977, Inhibition of lipoprotein binding to cell surface receptors of fibroblasts following selective modification of arginyl residues in arginine rich and B-apoproteins, J. Biol. Chem. 252:7279.PubMedGoogle Scholar
  106. Mahmoud, A. A. F., Rodman, H. M., Mandel, M. A., and Warren, K. S., 1976, Induced and spontaneous diabetes mellitus and suppression of cell-mediated immunologic responses: Granuloma formation, delayed dermal reactivity, and allograft rejection, J. Clin. Invest. 57:362.PubMedCrossRefGoogle Scholar
  107. Markowetz, B., van Snick, J. L., and Masson, P. L., 1979, Binding and ingestion of human lactoferrin by mouse alveolar macrophages, Thorax 34:209.PubMedCrossRefGoogle Scholar
  108. Maxfield, F. R., Schlessinger, J., Shechter, Y., Pastan, I., and Willingham, M. C., 1978, Collection of insulin, EGF and α2-macroglobulin in the same patches on the surface of cultured fibroblasts and common internalization, Cell 14:805.PubMedCrossRefGoogle Scholar
  109. Mehta, N. G., 1977, The site of synthesis and functions of acute phase plasma proteins: Close relationship with the reticulo-endothelial system, Med. Hypotheses 3:63.PubMedCrossRefGoogle Scholar
  110. Messner, R. P., Lindström, F. D., and Williams, R. C., Jr., 1973, Peripheral blood lymphocyte cell surface markers during the course of systemic lupus erythematosus, J. Clin. Invest. 52:3046.PubMedCrossRefGoogle Scholar
  111. Miller, L. L., and Bale, W. F., 1954, Synthesis of all plasma protein fractions except gamma globulins by the liver: The use of zone electrophoresis and lysine-∈-C14 to define the plasma proteins synthesized by the isolated perfused liver, J. Exp. Med. 99:125.PubMedCrossRefGoogle Scholar
  112. Minchin Clarke, H. G., Freeman, T., and Pryse-Phillips, W., 1971, Serum protein changes after injury, Clin. Sci. 40:337.Google Scholar
  113. Minor, R. R., 1980, Collagen metabolism: A comparison of diseases of collagen and diseases affecting collagen, Am. J. Pathol. 98:227.Google Scholar
  114. Mold, C., Rodgers, C. P., Kaplan, R. L., and Gewurz, H., 1982, Binding of human C-reactive protein to bacteria, Infect. Immun. 38:392.PubMedGoogle Scholar
  115. Mold, C., and Gerwurz, H., 1981, Inhibitory effect of C-reactive protein on alternate C pathway activation by liposomes and Steptococcus pneumoniae, J. Immunol. 127:2089.PubMedGoogle Scholar
  116. Mortensen, R. F., 1979, C-reactive protein (CRP)-mediated inhibition of the induction of in vitro antibody formation. I. T-cell dependence of the inhibition, Cell Immunol. 44:270.PubMedCrossRefGoogle Scholar
  117. Mortensen, R. F., Osmand, A. P., and Gewurz, H., 1975, Effects of C-reactive protein on the lymphoid system. I. Binding to thymus-dependent lymphocytes and alteration of their functions, J. Exp. Med. 141:821.PubMedGoogle Scholar
  118. Mortensen, R. F., 1982, Inhibition of the polyclonal antibody plaque-forming cell response of human B lymphocytes by C-reactive protein (CRP) and CRP complexes, Cell Immunol. 66:99.PubMedCrossRefGoogle Scholar
  119. Mosesson, M. W., 1977, Cold-insoluble globulin (CIg), a circulating cell surface protein, Thromb. Haemostasis 38:742.Google Scholar
  120. Mosher, D. F., 1976a, Action of fibrin-stabilizing factor on cold-insoluble globulin and α2-macroglobulin in clotting plasma, J. Biol. Chem. 251:1639.PubMedGoogle Scholar
  121. Mosher, D. F., 1976b, Changes in plasma cold-insoluble globulin concentration during experimental Rocky Mountain spotted fever infection in rhesus monkeys, Thromb. Res. 9:37.PubMedCrossRefGoogle Scholar
  122. Mosher, D. F., and Vaheri, A., 1980, Binding and degradation of α2-macroglobulin by cultured fibroblasts, Biochim. Biophys. Acta 627:113.PubMedCrossRefGoogle Scholar
  123. Mosher, D. F., and Wing, D. A., 1976, Synthesis and secretion of α2-macroglobulin by cultured human fibroblasts, J. Exp. Med. 143:462.PubMedCrossRefGoogle Scholar
  124. Mosher, D. F., Schad, P. E., and Kleinman, H. K., 1979, Cross-linking of fibronectin to collagen by blood coagulation Factor XIIIa, J. Clin. Invest. 64:781.PubMedCrossRefGoogle Scholar
  125. Munster, A. M., 1976, Post-traumatic immunosuppression is due to activation of suppressor T cells, Lancet 1:1329.PubMedCrossRefGoogle Scholar
  126. Murphy, P. A., Simon, P. L., and Willoughby, W. F., 1980, Endogenous pyrogens made by rabbit peritoneal exudate cells are identical with lymphocyte-activating factors made by rabbit alveolar macrophages, J. Immunol. 124:2498.PubMedGoogle Scholar
  127. Nelson, K. M., and Filkins, J. P., 1979, Effects of traumatic injury on sensitivity to insulin, Circ. Shock 6:285.PubMedGoogle Scholar
  128. Niehaus, G. D., Schumacker, P. R., and Saba, T. M., 1980, Reticuloendothelial clearance of bloodborne particulates: Relevance to experimental lung microembolization and vascular surgery, Ann. Surg. 191:479.PubMedCrossRefGoogle Scholar
  129. Octave, J.-N., Schneider, Y.-J., Hoffmann, P., Trouet, A., and Crichton, R. R., 1979, Transferrin protein and iron uptake by cultured rat fibroblasts, FEBS Lett. 108:127.PubMedCrossRefGoogle Scholar
  130. Ohlsson, K., 1975, α1antitrypsin and α2-macroglobulin: Interactions with human neutrophil collagenase and elastase, Ann. N.Y. Acad. Sci. 256:409.PubMedCrossRefGoogle Scholar
  131. Olsen, G. N., Harris, J. O., Castle, J. R., Waldman, R. H., and Karmgard, H. J., 1975, Alpha-1-antitrypsin content in the serum, alveolar macrophages, and alveolar lavage fluid of smoking and nonsmoking normal subjects, J. Clin. Invest. 55:427.PubMedCrossRefGoogle Scholar
  132. Osgood, E. E., 1954, Number and distribution of human hemic cells, Blood 9:1141.PubMedGoogle Scholar
  133. O’Shea, M. J., Kershenobich, D., and Tavill, A. S., 1973, Effects of inflammation on iron and transferrin metabolism, Br. J. Haematol. 25:707.PubMedCrossRefGoogle Scholar
  134. Osmand, A. P., Mortensen, R. F., Siegel, J., and Gewurz, H., 1975, Interactions of C-reactive protein with the complement system. III. Complement-dependent passive hemolysis initiated by CRP, J. Exp. Med. 142:1065.CrossRefGoogle Scholar
  135. Parisi, A. F., and Vallee, B. L., 1970, Isolation of a zinc α2-macroglobulin from human serum, Biochemistry 9:2421.PubMedCrossRefGoogle Scholar
  136. Phillips, J. L., 1976, Specific binding of zinc transferrin to human lymphocytes, Biochem. Biophys. Res. Commun. 72:634.PubMedCrossRefGoogle Scholar
  137. Phillips, J. L., and Azari, P., 1974, Zinc transferrin: Enhancement of nucleic acid synthesis in phytohemagglutinin-stimulated human lymphocytes, Cell. Immunol. 10:31.PubMedCrossRefGoogle Scholar
  138. Phillips, N. C., 1982, Exacerbation of experimental poly-D-lysine arthritis by C-reactive protein, Agents and Actions 12:344.PubMedCrossRefGoogle Scholar
  139. Pierce, C. W., 1980, Macrophages: Modulators of immunity, Am. J. Pathol. 98:10.PubMedGoogle Scholar
  140. Plow, E. F., and Ginsberg, M. H., 1981, Specific and saturable binding of plasma fibronectin. J. Biol. Chem. 256:9477.PubMedGoogle Scholar
  141. Powanda, M. C., 1977, Changes in body balances of nitrogen and other key nutrients: Description and underlying mechanisms, Am. J. Clin. Nutr. 30:1254.PubMedGoogle Scholar
  142. Powanda, M. C., and Beisel, W. R., 1982, Hypothesis: Leukocyte endogenous mediator/endogenous pyrogen/lymphocyte—activating factor modulates the development of nonspecific and specific immunity and affects nutritional status, Am. J. Clin. Nutr. 35:762.PubMedGoogle Scholar
  143. Powanda, M. C., and Moyer, E. D., 1981, Plasma proteins and wound healing, Surg. Gynecol. Obstet. 153:749.PubMedGoogle Scholar
  144. Powanda, M. C., Wannemacher, R. W., Jr., and Cockerell, G. L., 1972, Nitrogen metabolism and protein synthesis during pneumococcal sepsis in rats, Infect. Immun. 6:266.PubMedGoogle Scholar
  145. Powanda, M. C., Cockerell, G. L., Moe, J. B., Abeles, F. B., Pekarek, R. S., and Canonico, P. G., 1975, Induced metabolic sequelae of tularemia in the rat: Correlation with tissue damage, Am. J. Physiol. 229:479.PubMedGoogle Scholar
  146. Powanda, M. C., Abeles, F. B., Bostian, K. A., Fowler, J. P., and Hauer, E. C., 1979, Differential effects of clofibrate on inflammation-induced alterations in plasma proteins in the rat, Biochem. J. 178:633.PubMedGoogle Scholar
  147. Rapaport, F. T., and Bachvaroff, R. J., 1976, Kinetics of humoral responsiveness in severe thermal injury, Ann. Surg. 184:51.PubMedCrossRefGoogle Scholar
  148. Redgrave, T. G., 1970, Formation of cholesteryl ester-rich particulate lipid during metabolism of chylomicrons, J. Clin. Invest. 49:465.PubMedCrossRefGoogle Scholar
  149. Remold-O’Donnell, E., and Lewandrowski, K., 1983, Two proteinase inhibitors associated with peritoneal macrophages, J. Biol. Chem. 258:3251.PubMedGoogle Scholar
  150. Rinderknecht, H., and Geokas, M. C., 1973, On the physiological role of α2-macroglobulin, Biochim. Biophys. Acta 295:233.PubMedCrossRefGoogle Scholar
  151. Ruoslahti, E., and Hayman, E. G., 1979, Two active sites with different characteristics in fibronectin, FEBS Lett. 97:221.PubMedCrossRefGoogle Scholar
  152. Ruoslahti, E., and Vaheri, A., 1975, Interaction of soluble fibroblast surface antigen with fibrinogen and fibrin: Identity with cold insoluble globulin of human plasma, J. Exp. Med. 141:497.PubMedCrossRefGoogle Scholar
  153. Ruoslahti, E., Engvall, E., and Hayman, E. G., 1981, Fibronectin: Current concepts of its structure and functions, Coll. Res. 1:95.CrossRefGoogle Scholar
  154. Ryan, N. T., Blackburn, G. I., and Clowes, G. H. A., Jr., 1974, Differential tissue sensitivity to elevated endogenous insulin levels during experimental peritonitis in rats, Metabolism 23:1081.PubMedCrossRefGoogle Scholar
  155. Saba, T. M., Blumenstock, F. A., Scovill, W. A., and Bernard, H., 1978, Cryoprecipitate reversal of opsonic α2-surface binding glycoprotein deficiency in septic surgical and trauma patients, Science 201:622.PubMedCrossRefGoogle Scholar
  156. Santoro, S. A., and Cunningham, L. W., 1979, Fibronectin and the multiple interaction model for platelet-collagen adhesion, Proc. Natl. Acad. Sci. USA 76:2644.PubMedCrossRefGoogle Scholar
  157. Scanu, A. M., Byrne, R. E., and Mihovilovic, M., 1982, Functional roles of plasma high density lipoproteins, CRC Crit. Rev. Biochem. 13:109.PubMedCrossRefGoogle Scholar
  158. Schapira, M., Scott, C. F., and Colman, R. W., 1982, Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma, J. Clin. Invest. 69:462.PubMedCrossRefGoogle Scholar
  159. Schuh, J., Novogrodsky, A., and Haschemeyer, R. H., 1978, Inhibition of lymphocyte mitogenesis by autooxidized low-density lipoprotein, Biochem. Biophys. Res. Commun. 84:763.PubMedCrossRefGoogle Scholar
  160. Siegel, J., Rent, R., and Gewurz, H., 1974, Interactions of C-reactive protein with the complement system. I. Protamine-induced consumption of complement in acute phase sera, J. Exp. Med. 140:631.PubMedCrossRefGoogle Scholar
  161. Spain, M. J., Wosu, L. O., and Kalant, N., 1979, Multiple effects of serum low-density lipoprotein on cultured human fibroblasts, Can. J. Biochem. 57:684.PubMedCrossRefGoogle Scholar
  162. Stecher, V. J., and Thorbecke, G. J., 1967a, Sites of synthesis of serum proteins. I. Serum proteins produced by macrophages in vitro, J. Immunol. 99:643.PubMedGoogle Scholar
  163. Stecher, V. J., and Thorbecke, G. J., 1967b, Sites of synthesis of serum proteins. III. Production of β1C, β1E, and transferrin by primate and rodent cell lines, J. Immunol. 99:660.PubMedGoogle Scholar
  164. Stein-Streilein, J., and Hart, D. A., 1980, Protease inhibitors modulate in-vitro antibody formation, Fed. Proc. 39:807A.Google Scholar
  165. Szabó, S., Barbu, Z., Lakatos, L., László, I., and Szabó, A., 1980, Local production of proteins in normal human bronchial secretion, Respiration 39:172.PubMedCrossRefGoogle Scholar
  166. Tada, N., Fidge, N., and Nestel, P., 1979, Identification and characterization of mixed disulphide complexes of E apoprotein in high density lipoprotein of patients with acute alcoholic hepatitis, Biochem. Biophys. Res. Commun. 90:297.PubMedCrossRefGoogle Scholar
  167. Teodorescu, M., Ganea, D., Lee, T. T., Skosey, J. L., and Rutter, G., 1982, The effect of protease inhibitors on the polyclonal B cell activator from the serum of patients with rheumatoid arthritis, Int. J. Immunopharmac. 4:1.CrossRefGoogle Scholar
  168. Thorbecke, G. J., Liem, H. H., Knight, S., Cox, K., and Müller-Eberhard, U., 1973, Sites of formation of the serum proteins transferrin and hemopexin, J. Clin. Invest. 52:725.PubMedCrossRefGoogle Scholar
  169. Travis, J., and Salvesen, G. S., 1983, Human plasma proteinase inhibitors, Ann. Rev. Biochem. 52:655.PubMedCrossRefGoogle Scholar
  170. Tunstall, A. M., and James, K., 1974, Preliminary studies on the synthesis of alpha2-macroglobulin by human lymphocytes in vitro, Clin. Exp. Immunol. 17:697.PubMedGoogle Scholar
  171. Tunstall, A. M., and James, K., 1975, The effect of human α2-macroglobulin on the restoration of humoral responsiveness in X-irradiated mice, Clin. Exp. Immunol. 21:173.PubMedGoogle Scholar
  172. Turinsky, J., and Patterson, S. A., 1979, Proximity to a burn wound as a new factor in considerations of postburn insulin resistance, J. Surg. Res. 26:171.PubMedCrossRefGoogle Scholar
  173. Ulrich, F., 1979, Protease potentiation of thymocyte blastogenesis, Immunology 38:705.PubMedGoogle Scholar
  174. van Leuven, F., Cassiman, J. J., and van den Berghe, H., 1978, Uptake and degradation of α2-macroglobulin-protease complexes in human cells in culture, Exp. Cell Res. 117:273.PubMedCrossRefGoogle Scholar
  175. van Snick, J. L., Masson, P. L., and Heremans, J. F., 1974, The involvement of lactoferrin in the hyposideremia of acute inflammation, J. Exp. Med. 140:1068.PubMedCrossRefGoogle Scholar
  176. Verburgh, H. A., Peterson, P. K., Smith, D. E., Nguyen, B-Y. T., Hoidal, J. R., Wilkinson, B. J., Verhoef, J., and Furcht, L. T., 1981, Human fibronectin binding to staphylococcal surface protein and its relative inefficiency in promoting phagocytosis by human polymorphonuclear leukocytes, monocytes and alveolar macrophages, Infec. Immun. 33:811.Google Scholar
  177. Vetter, M. L., Gerwurz, H., Hansen, B., James, K., and Baum, L. L., 1983, Effects of C-reactive protein on human lymphocyte responsiveness, J. Immunol. 130:2121.PubMedGoogle Scholar
  178. Via, D. P., Willingham, M. C., Pastan, I., Gotto, A. M., Jr., and Smith, L. C., 1982, Co-clustering and internalization of low-density lipoproteins and α2-macroglobulin in human skin fibroblasts, Exp. Cell. Res. 141:15.PubMedCrossRefGoogle Scholar
  179. Vischer, T. L., and Berger, D., 1980, Activation of macrophages to produce neutral proteinases by endocytosis of alpha2-macroglobulin-trypsin complexes, J. Reticuloendothelial Soc. 28:427.Google Scholar
  180. Volenec, F. J., Mani, M. M., Clark, G. M., Robinson, D. W., and Humphrey, L. J., 1977, Peripheral blood T and B lymphocytes in patients with burns. II. Sequential rosette analyses considering burn severity and pseudomonas sepsis, Burns 4:7.CrossRefGoogle Scholar
  181. Voss, B., Allam, S., Rauterberg, J., Ullrich, K., Gieselmann, V., and von Figura, K., 1979, Primary cultures of rat hepatocytes synthesize fibronectin, Biochem. Biophys. Res. Commun. 90:1348.PubMedCrossRefGoogle Scholar
  182. Wannemacher, R. W., Jr., 1975, Protein metabolism (applied biochemistry), in: Total Parenteral Nutrition: Premises & Promises (H. Ghadimi, ed.), pp. 85–153, Wiley, New York.Google Scholar
  183. Wannemacher, R. W., Jr., Powanda, M. C., and Dinterman, R. E., 1974, Amino acid flux and protein synthesis after exposure of rats to either Diplococcus pneumoniae or Salmonella typhimurium, Infect. Immun. 10:60.PubMedGoogle Scholar
  184. Weeke, B., and Krasilnikoff, P. A., 1972, The concentration of 21 serum proteins in normal children and adults, Acta Med. Scand. 192:149.PubMedCrossRefGoogle Scholar
  185. Weinberg, E. D., 1978, Iron and infection, Microbiol. Rev. 42:45.PubMedGoogle Scholar
  186. Weisgraber, K. H., and Mahley, R. W., 1978, Apoprotein (E-A-II) complex of human plasma lipoproteins. I. Characterization of this mixed disulfide and its indentification in a high density lipoprotein subfraction, J. Biol. Chem. 253:6281.PubMedGoogle Scholar
  187. Weiss, R. E., and Reddi, A. H., 1981, Role of fibronectin in collagenous matrix-induced mesenchymal cell proliferation and differentiation in vivo, Exp. Cell Res. 133:247.PubMedCrossRefGoogle Scholar
  188. Weissman, S. M., Wochner, R. D., Mullins, F. X., Wynngate, A., and Waldmann, T. A., 1966, Synthesis of plasma proteins by hepatectomized dogs, Am. J. Physiol. 210:128.PubMedGoogle Scholar
  189. Werner, M., 1969, Serum protein changes during the acute phase reaction, Clin. Claim. Acta 25:299.CrossRefGoogle Scholar
  190. Werner, M., and Cohnen, G., 1969, Changes in serum proteins in the immediate postoperative period, Clin. Sci. 36:173.PubMedGoogle Scholar
  191. White, R., Lee, D., Habicht, G., and Janoff, A., 1981, Secretion of alpha-1-proteinase inhibitor by cultured alveolar rat macrophages, Am. Rev. Respir. Dis. 123:477.Google Scholar
  192. Williams, R. O., and Loeb, L. A., 1973, Zinc requirement for DNA replication in stimulated human lymphocytes, J. Cell Biol. 58:594.PubMedCrossRefGoogle Scholar
  193. Willingham, M. C., Maxfield, F. R., and Pastan, I. H., 1979, α2Macroglobulin binding to the plasma membrane of cultured fibroblasts: Diffuse binding followed by clustering in coated regions, J. Cell Biol. 82:614.PubMedCrossRefGoogle Scholar
  194. Wilson, G. B., Walker, J. H., Jr., Watkins, J. H., Jr., and Wolgroch, D., 1980, Determination of subpopulations of leukocytes involved in the synthesis of α1-antitrypsin in vitro, Proc. Soc. Exp. Biol. Med. 164:105.PubMedGoogle Scholar
  195. Wolfe, R. R., Durkot, M. J., Allsop, J. R., and Burke, J. F., 1979, Glucose metabolism in severely burned patients, Metabolism 28:1031.PubMedCrossRefGoogle Scholar
  196. Wybran, J., and Fudenberg, H. H., 1973, Thymus-derived rosette-forming cells in various human disease states: Cancer, lymphoma, bacterial and viral infections, and other diseases, J. Clin. Invest. 52:1026.PubMedCrossRefGoogle Scholar
  197. Wyllie, J. C., 1977, Transferrin uptake by rabbit alveolar macrophages in vitro, Br. J. Haematol. 37:17.PubMedGoogle Scholar
  198. Wyllie, J. C., 1979, The subcellular distribution of iron in rabbit alveolar macrophages, Biochem. Biophys. Res. Commun. 89:1307.PubMedCrossRefGoogle Scholar
  199. Yamada, K. M., and Kennedy, D. W., 1979, Fibroblast cellular and plasma fibronectins are similar but not identical, J. Cell Biol. 80:492.PubMedCrossRefGoogle Scholar
  200. Yamada, K. M., and Olden, K., 1978, Fibronectins—Adhesive glycoproteins of cell surface and blood, Nature (London) 275:179.CrossRefGoogle Scholar
  201. Zeineh, R. A., and Kukral, J. C., 1970, The turnover rate of orosomucoid in burned patients, J. Trauma 10:493.PubMedCrossRefGoogle Scholar
  202. Zeineh, R. A., Barrett, B., Niemirowski, L., and Fiorella, B. J., 1972, Turnover rate of orosomucoid in the dog with sterile abscess, Am. J. Physiol. 222:1326.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Michael C. Powanda
    • 1
  • Elizabeth D. Moyer
    • 2
  1. 1.Biochemistry BranchU.S. Army Institute of Surgical ResearchFort Sam HoustonUSA
  2. 2.Departments of Surgery and BiochemistryState University of New YorkBuffaloUSA

Personalised recommendations