Advertisement

Plasma Fibronectin: Biochemical Properties and Clinical Relevance

  • F. A. Blumenstock
  • T. M. Saba
  • J. E. Kaplan
Part of the Developments in Hematology and Immunology book series (DIHI, volume 5)

Abstract

The reticuloendothelial system (RES) consists of a network of sessile and mobile mononuclear phagocytes which perform a variety of physiological functions with respect to host defense. Those fixed macrophages that reside in the liver and spleen and comprise the majority of the RES are uniquely located anatomically such that they can monitor the circulation and have been demonstrated to remove a variety of blood-borne toxic and particulate material of both endogenous and exogenous origin (37). These cells can selectively recognize and remove from the vascular compartment endogenously generated material including cell debris (26), denatured collagen (43), fibrin aggregates (23), and a variety of exogenous colloidal and particulate material including bacteria (4,16,34,41). Early studies involved in the evaluation of the activity of this system which is responsible for the removal of circulating particulate demonstrated that activation of the system as evidenced by an enhanced rate of removal of test particulate from the blood was associated with an increased resistance to a variety of pathophysiological situations such as traumatic injury (51), infection (34), and tumor growth (4). Conversely, depression of the clearance capacity of the system resulted in an increased sensitivity of experimental animals to the same pathological insults. Therefore, the concept that the RES was important in host defense processes became firmly established.

Keywords

Host Defense Traumatic Injury Plasma Fibronectin Limb Blood Flow Opsonic Activity 
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. 1.
    Allen, C., Saba, T.M., Molnar, J.: Isolation, purification and characterization of opsonic protein. J. Reticuloendothelial Soc. 13: 410, 1973.Google Scholar
  2. 2.
    Annest, S.J., Scovill, W.A., Blumenstock, F.A., Stratton, H.H., Newell, J.C., Paloski, W.H., Saba, T.M., Powers, S.R.: Increased creatinine clearance following cryoprecipitate infusion in trauma and surgical patients with decreased renal function. J. Trauma 20: 726, 1980.CrossRefPubMedGoogle Scholar
  3. 3.
    Atherton, B.T., Hynes, R.O.: A difference between plasma and cellular fibronectins located with monoclonal antibodies. Cell 25: 133 1981.CrossRefPubMedGoogle Scholar
  4. 4.
    Biozzi, B., Stiffel, C., Halpern, B.M., Manton, D.: Etude de la fonction phagocytaire du SRE au cours du développement de tumeurs expérimentales chez le rat et la souris. Ann. Inst. Pasteur. 94: 681, 1958.Google Scholar
  5. 5.
    Biozzi, G., Benacerraf, B., Halpern, B.N.: Quantitative study of the granulopectic activity of the reticuloendothelial system. II. A study of the kinetics of the granulopectic activity of the RES in relation to the dose of carbon injected. Relationship between the weight of the organs and their activity. Brit. J. Exp. Path. 34: 441, 1953.PubMedPubMedCentralGoogle Scholar
  6. 6.
    Blumenstock, F.A., Saha, T.M.: Purification of alpha-2-opsonic glycoprotein from human serum and its measurement by immunoassay. J. Reticuloendothelial Soc. 23: 119, 1978.Google Scholar
  7. 7.
    Blumenstock, F.A., Saba, T.M., Weber, P., Cho, E.: Purification and biochemical characterization of a macrophage stimulated alpha2-globulin opsonic protein. J. Reticuloendothelial Soc. 19: 157, 1976.Google Scholar
  8. 8.
    Blumenstock, F.A., Saba, T.M., Weber, P., Laffin, R.: Biochemical and immunological characterization of human opsonic alpha-2-SB glycoprotein; Its identity with cold-insoluble globulin. J. Biol. Chem. 253: 4387, 1978.Google Scholar
  9. 9.
    Blumenstock, F.A., Weber, P.B., Saba, T.M.: Isolation and purification from rat serum of an alpha-2-opsonic glycoprotein. J. Biol. Chem. 252: 7156, 1977.PubMedGoogle Scholar
  10. 10.
    Blumenstock, F.A., Weber, P., Saba, T.M., Laffin, R.: Electroimmunoassay of alpha-2-opsonic protein during reticuloendothelial blockade. Am. J. Physiol. 232: R80, 1977.PubMedGoogle Scholar
  11. 11.
    Brodin, B., Bergham, L., Frigerg-Nielson, S., Nordstrom, H., Schildt, B.: Fibronectin in the treatment of septicemia - a preliminary report. Excerpta Medica. 7th World Congress of Anesthesiology. Hamburg, 1980, p. 504.Google Scholar
  12. 12.
    Dillon, B.C., Saba, T.M.: Starvation-induced hepatic phagocytic depression: Role of opsonic fibronectin and neutrophils in the distribution of blood-borne taphcloeoceus aureur. Abstracts of Association for Academic Surgery, 1981, p. 68.Google Scholar
  13. 13.
    Dillon, B.C., Saba, T.M., Cho, E., Lewis, E.: Opsonic fibronectin deficiency in the etiology of starvation induced reticuloendothelial phagocytic dysfunction. Exp. and Molec. Path. 36 (in press), 1982.Google Scholar
  14. 14.
    Di Luzio, N.R.: Macrophages, recognition factors and neoplasia. In: RES System. International Academy of Pathology Monograph. Baltimore, MD, Williams and Wilkins, 1975, p. 49.Google Scholar
  15. 15.
    Engel, J., Odermatt, E., Engel, A., Madri, J.A., Furthmayer, H., Rohde, H., Timpl, R.: Shapes, domain organization and flexibility of laminin in fibronectin. Two multi-functional proteins of the extracellular matrix. J. Molec. Biol. 150: 97, 1981.CrossRefPubMedGoogle Scholar
  16. 16.
    Filkins, F.P.: Detoxification of endotoxin by leukocytes and macrophages. Proc. Soc. Exp. Biol. Med. 137: 1396, 1971.CrossRefPubMedGoogle Scholar
  17. 17.
    Filkins, F.P., Chase, R.E., Smith, J.J.: Characteristics of a plasma factor governing carbon phagocytosis in the isolated per-fused rat liver. J. Reticuloendothelial Soc. 2: 287, 1965.Google Scholar
  18. 18.
    Graham, C.W., Blumenstock, F.A., Saha, T.M., Gotoff, S.: Labor modulates alpha-2-opsonic protein (2OP) for fixed macrophages. J. Reticuloendothelial Soc. 24: 31a, 1978.Google Scholar
  19. 19.
    Graham, C.W., Saba, T.M.: Opsonin in reticuloendothelial regulation during and following pregnancy. J. Reticuloendothelial Soc. 14: 121, 1973.Google Scholar
  20. 20.
    Jilek, F., Hormann, H.: Fibronectin (cold-insoluble globulin). VI. Influence of heparin and hyaluronic acid on the binding of native collagen. Hoppe-Seyler’s Z. Physiol. Chem. 360: 597, 1979.CrossRefGoogle Scholar
  21. 21.
    Kaplan, J.E., Saba, T.M.: Humoral deficiency and reticuloendothelial depression after traumatic shock. Am. J. Physiol. 230: 7, 1976PubMedGoogle Scholar
  22. 22.
    Kaplan, J.E., Saba, T.M., Cho, E.: Serological modifications of reticuloendothelial capacity and altered resistance to traumatic shock. Circ. Shock 3: 203, 1976.Google Scholar
  23. 23.
    Kaplan, J.E.: The role of the reticuloendothelial system in control of hemostatic and thrombotic mechanisms. In: Pathophysiology of the Reticuloendothelial System. eds. B.M. Altura and T.M. Saba. Raven Press, New York, 1981, p. 111.Google Scholar
  24. 24.
    Lanser, M.E., Saba, T.M., Scovill, W.A.: Opsonic glycoprotein (plasma fibronectin) levels after burn injury: Relationship to extent of burn and development ofGoogle Scholar
  25. 25.
    Manwaring, W.H., Coe, H.C.: Endothelial opsonins. J. Immunol. 1: 401, 1916.Google Scholar
  26. 26.
    Molnar, J., McLain, S., Allen, C., Laga, H., Gava, A., Gelder, R.: Specificity of a non-complement related opsonic protein. Biochem. Biophys. Acta 493: 37, 1977.PubMedGoogle Scholar
  27. 27.
    Morrison, P.R., Edsall, J.T., Miller, S.G.: Preparation and properties of serum and plasma proteins. XVIII. The separation of purified fibrinogen from fraction I of human plasma. J. Am. Chem. Soc. 70: 3103, 1948.CrossRefPubMedGoogle Scholar
  28. 28.
    Mosesson, M.W., Umfleet, R.A.: The cold-insoluble globulin of human plasma. I. Purification, primary characterization and relationship to fibrinogen and other cold-insoluble fraction components. J. Biol. Chem. 245: 572 8, 1970.Google Scholar
  29. 29.
    Mosher, D.F.: Changes in plasma cold-insoluble globulin concentration during experimental Rocky Mountain Spotted Fever infection in rhesus monkeys. Thromb. Res. 9: 37, 1976.CrossRefPubMedGoogle Scholar
  30. 30.
    Mosher, D.F.: Cross-linking of cold-insoluble globulin by fibrin stabilizing factors. J. Biol. Chem. 250: 6614, 1976.Google Scholar
  31. 31.
    Mosher, D.F., Williams, E.M.: Fibronectin concentration is decreased in plasma of severely ill patients with disseminated intra-vascular coagulation. J. Lab. Clin. Med. 91: 729, 1978.PubMedGoogle Scholar
  32. 32.
    Ruoslahti, E., Vaheri, A.: Interaction of soluble fibroblast surface antigens with fibrinogen and fibrin. Identity with cold-insoluble globulin of human plasma. J. Exp. Med. 141: 497, 1975.CrossRefPubMedGoogle Scholar
  33. 33.
    Robbins, A.B., Doran, J.E., Reese, A.C., Mansberger, A.R.: Cold-insoluble globulin levels in operative trauma: Serum depletion, wound sequestration and biological activity. Am. Surg. 46: 663, 1980.PubMedGoogle Scholar
  34. 34.
    Rogers, B.E.: Host mechanisms which act to remove bacteria from the bloodstream. Bart. Rev. 24: 50, 1960.Google Scholar
  35. 35.
    Saba, T.M.: Physiology and pathophysiology of the reticuloendothelial system. Arch. Intern. Med. 126: 1031, 1970.CrossRefPubMedGoogle Scholar
  36. 36.
    Saba, T.M.: Aspecific Opsonins. In: Proc. of 4th Internat. Convocation on immunology. In: Immune System and Infectious Diseases. S. Karger Co., Basel, 1975, p. 489.Google Scholar
  37. 37.
    Saba, T.M., Antikatzides, T.G.: Humoral mediated macrophage response during tumor growth. Brit. J. Cancer 21: 471, 1975.CrossRefGoogle Scholar
  38. 38.
    Saba, T.M., Albert, W.H., Blumenstock, F.A., Evanega, G., Staehler, F., Cho, F.: Evaluation of a rapid immunoturbidimetric assay for opsonic fibronectin in surgical and trauma patients administered cryoprecipitate. J. Lab. Clin. Med. 90: 473, 1981.Google Scholar
  39. 39.
    Saba, T.M., Blumenstock, F.A., Scovill, W.A., Bernard, H.R.: Cryoprecipitate reversal of opsonic alpha-2-surface binding glycoprotein deficiency in septic surgical and trauma patients. Science 201:622., 1977.CrossRefGoogle Scholar
  40. 40.
    Saba, T.M., Blumenstock, F.A., Weber, P., Kaplan, J.E.: Physiologic role for cold-insoluble globulin in systemic host defense: Implications of its characterization as the opsonic R2SB glycoprotein. Ann. N.Y. Acad. Sci. 312: 43, 1978.CrossRefPubMedGoogle Scholar
  41. 41.
    Saba, T.M., Di Luzio, N.R.: Kupffer cell phagocytosis and metabolism of a variety of particles as a function of opsonization. J. Reticuloendothelial Soc. 2: 437, 1965.Google Scholar
  42. 42.
    Saba, T.M., Di Luzi_o, N.R.: Reticuloendothelial blockade and recovery as a function of opsonic activity. Am. J. Physiol. 216: 197, 1969.PubMedGoogle Scholar
  43. 43.
    Saba, T.M., Jaffe, E.: Plasma fibronectin (opsonic glycoprotein): Its synthesis by vascular endothelial cells and role in cardiopulmonary integrity after trauma as related to reticuloendothelial function. Am. J. Med. 68: 577, 1980.CrossRefPubMedGoogle Scholar
  44. 44.
    Scovill, W.A., Saba, T.M., Blumenstock, F.A., Bernard, H., Powers, S.R.: Opsonic alpha-2-surface binding glycoprotein therapy during sepsis. Ann. Surg. 188: 521, 1978.CrossRefPubMedPubMedCentralGoogle Scholar
  45. 45.
    Scovill, W.A., Saba, T.M., Kaplan, J.E., Bernard, H.R., Powers, S.R.: Disturbances in circulating opsonic activity in man after operative and blunt trauma. J. Surg. Res. 22: 709, 1977.CrossRefPubMedGoogle Scholar
  46. 46.
    Snyder, E.L., Mosher, D.F., Hezzey, A., Golenwski, G.: Effect of blood transfusion on in vivo levels of plasma fibronectin. J. Lab. Clin. Med. 98: 336, 1981.PubMedGoogle Scholar
  47. 47.
    Stathakis, N.E., Fountas, A., Tsianos, E.: Plasma fibronectin in normal subjects and in various disease states. J. Clin. Pathol. 34: 504, 1981.CrossRefPubMedPubMedCentralGoogle Scholar
  48. 48.
    Stossel, T.P.: Phagocytosis. New Engl. J. Med. 290: 717, 1974.Google Scholar
  49. 49.
    Yamada, K.M., Kennedy, D.W.: Fibroblast cellular and plasma fibronectin are similar but not identical. J. Cell. Biol. 80: 492, 1979CrossRefPubMedGoogle Scholar
  50. 50.
    Yamada, K.M., Olden, K.: Fibronectin: Adhesive glycoproteins of cell surface and blood. Nature 275: 179, 1978.CrossRefPubMedGoogle Scholar
  51. 51.
    Zweifach, B.W. Benacerraf, B., Thomas, L.: Relationship between the vascular manifestation of shock produced by endotoxin, trauma and hemorrhage. II. The possible role of the RES in resistance to each type of shock. J. Exp. Med. 106: 403, 1957.CrossRefPubMedPubMedCentralGoogle Scholar

Copyright information

© Martinus Nijhoff Publishers, The Hague 1982

Authors and Affiliations

  • F. A. Blumenstock
  • T. M. Saba
  • J. E. Kaplan

There are no affiliations available

Personalised recommendations