Plasma Clearance of Products of Fibrinolysis
Alterations in fibrinogen metabolism frequently occur in physiologic adaptations to stress and also accompany many pathologic states. Unfortunately, the significance of such alterations remains unknown. However, fibrin deposits can impair organ function and are likely to be major contributors to the debilitation eventuating with numerous diseases of unrelated etiologies. Fibrin deposition and its removal are recognized problems in the thrombotic diseases such as myocardial infarction and cerebrovascular thrombosis. But only recently has fibrin deposition alone and in association with immunologic diseases been considered of consequence in renal dysfunction . Even more recent is the still limited appreciation of the role of fibrin deposits in perpetuating and recycling joint inflammations occuring in rheumatoid diseases [2, 3]. Of obvious value is the further identification and improved understanding of the mechanisms available for resolving the problems of fibrinogen metabolism and fibrin deposition and degradation. The purpose of this communication is to report on the cellular mechanisms for eliminating altered fibrinogen and fibrin and their degradation products from the circulation.
KeywordsPlasma Clearance Thrombotic Thrombocytopenic Purpura Plasma Fibrinogen Clearance Time Fibrin Deposition
Unable to display preview. Download preview PDF.
- 1.R. T. McCluskey, P. Vassalli, G. Gallo, and D.S. Baldwin, “An immunofluorescent study of pathogenic mechanisms in glomerular diseases,” New Engl. J. Med., 274: 695 - 701, 1966.Google Scholar
- 2.J.M. Riddle, G.B. Bluhm, and M.I. Barnhart, “Interrelationships between fibrin, neutrophils, and rheumatoid synovitis,” J. Reticuloendothelial Soc., 2: 420 - 436, 1965.Google Scholar
- 3.G. B. Bluhm, J.M. Riddle, and M.I. Barnhart, “Significance of fibrin and other particulates in rheumatoid joint inflammation,” Henry Ford Hospital Med. Bull., 14: 119 - 130, 1966.Google Scholar
- 5.M.I. Barnhart, “Importance of neutrophilic leucocytes in the resolution of fibrin,” Federation Proc., 24: 846 - 853, 1965.Google Scholar
- 6.M.I. Barnhart, “Cellular fibrinogen,” Thromb. Diath. Hemorrhag., 10: 157 - 165, 1964.Google Scholar
- 8.M.I. Barnhart, S.A. McCutcheon, J.M. Riddle, and J.M. Ohorodnik, “Thrombotic thrombocytopenic purpura as a model of accelerated protein synthesis,” Thromb. Diath. Hemorrhag., 12: 211 - 231, 1964.Google Scholar
- 13.M.I. Barnhart and W. B. Forman, “The cellular localization of fibrinogen as revealed by the fluorescent antibody technique,” Vox Sanguins, 8:461-473, 1963.Google Scholar
- 14.M.I. Barnhart, D.C. Cress, R. L. Henry, and J. M. Riddle, “Influence of fibrinogen split products on platelets,” Thromb. Diath. Hemorrhag., 17: 78 - 98, 1967.Google Scholar
- 15.V. Nussenzweig, M. Seligmann, and P. Grabar, “Les products de degradation du fibrinogene aumain par la plasmin,” Ann.Inst. Pasteur, 100: 490 - 508, 1961.Google Scholar
- 16.B. Benacerraf, G. Biozzi, B. N. Halpern, C. Stiffel, and D. Mouton, “Phagocytosis of heat-denatured human serum albumin labeled with 131I and its use as a means of investigating blood flow,” Brit. J. Exptl. Pathol., 38: 35 - 48, 1957.Google Scholar