Adsorptive Endocytosis of Fibrin Monomer by Macrophages: Evidence of a Receptor for the Amino Terminus of the Fibrin Alpha Chain

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1982 Aug 1

PMID 6289305

Citations 13

Authors

S R Gonda

J R SHAINOFF

Affiliations

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Abstract

Human fibrinogen and fibrin monomer were labeled with heme-octapeptide for cytochemical examination of their interaction with rabbit peritoneal macrophages in vitro. Upon short exposure to labeled fibrin monomer in solution with unlabeled fibrinogen, the cells became covered with surface-adsorbed monomer in nonaggregated form and having a characteristic trinodular shape. Within 30 min, the adsorbed monomer became fully internalized by vesicular uptake, with much of it being incorporated into lysosomal bodies. A concomitant loss of adsorptive capacity of the cell surface for uptake of more monomer accompanied the internalization. By contrast, labeled fibrinogen was not adsorbed by the macrophage surface. Some internalization of fibrinogen by passive fluid-phase pinocytosis was evident, but it was not accompanied by loss of absorptive capacity for fibrin monomer. The active uptake of monomer may have depended on binding to the amino terminus that is blocked by fibrinopeptide A in fibrinogen, because addition of synthetic peptide corresponding to the terminal Gly-Pro-Arg segment inhibited both the adsorption and the internalization of monomer.

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References

Wissig S, Williams M . Permeability of muscle capillaries to microperoxidase. J Cell Biol. 1978; 76(2):341-59. PMC: 2109976. DOI: 10.1083/jcb.76.2.341. View

Blomback B, Blomback M, HESSEL B, Iwanaga S . Structure of N-terminal fragments of fibrinogen and specificity of thrombin. Nature. 1967; 215(5109):1445-8. DOI: 10.1038/2151445a0. View

Karnovsky M . The ultrastructural basis of capillary permeability studied with peroxidase as a tracer. J Cell Biol. 1967; 35(1):213-36. PMC: 2107108. DOI: 10.1083/jcb.35.1.213. View

Tu A, Reinosa J, Hsiao Y . Peroxidative activity of hemepeptides from horse heart cytochrome c. Experientia. 1968; 24(3):219-21. DOI: 10.1007/BF02152778. View

Kierulf P, Abildgaard U . Studies on soluble fibrin in plasma. I. N-terminal analysis of a modified fraction I (Cohn) from normal and thrombin-incubated plasma. Scand J Clin Lab Invest. 1971; 28(2):231-40. DOI: 10.3109/00365517109086905. View

Steinman R, COHN Z . The interaction of soluble horseradish peroxidase with mouse peritoneal macrophages in vitro. J Cell Biol. 1972; 55(1):186-204. PMC: 2108752. DOI: 10.1083/jcb.55.1.186. View

SHAINOFF J, PAGE I . Deposition of modified fibrinogen within the aortic intima. Atherosclerosis. 1972; 16(3):287-305. DOI: 10.1016/0021-9150(72)90079-2. View

Kraehenbuhl J, Galardy R, JAMIESON J . Preparation and characterization of an immuno-electron microscope tracer consisting of a heme-octapeptide coupled to fab. J Exp Med. 1974; 139(1):208-23. PMC: 2139508. DOI: 10.1084/jem.139.1.208. View

Kudryk B, Collen D, Woods K, Blomback B . Evidence for localization of polymerization sites in fibrinogen. J Biol Chem. 1974; 249(10):3322-5. View

10.

Kanaide H, SHAINOFF J . Cross-linking of fibrinogen and fibrin by fibrin-stablizing factor (factor XIIIa). J Lab Clin Med. 1975; 85(4):574-97. View

11.

Simionescu N, Siminoescu M, Palade G . Permeability of muscle capillaries to small heme-peptides. Evidence for the existence of patent transendothelial channels. J Cell Biol. 1975; 64(3):586-607. PMC: 2109550. DOI: 10.1083/jcb.64.3.586. View

12.

Sherman L, Harwig S, Lee J . In vitro formation and i vivo clearance of fibrinogen: fibrin complexes. J Lab Clin Med. 1975; 86(1):100-11. View

13.

Colvin R, Dvorak H . Fibrinogen/fibrin on the surface of macrophages: detection, distribution, binding requirements, and possible role in macrophage adherence phenomena. J Exp Med. 1975; 142(6):1377-90. PMC: 2190074. DOI: 10.1084/jem.142.6.1377. View

14.

Muller-Berghaus G, Mahn I, Koveker G, Maul F . In vivo behaviour of homologous urea-soluble 131I-fibrin and 125I-fibrinogen in rabbits: the effect of fibrinolysis inhibition. Br J Haematol. 1976; 33(1):61-79. DOI: 10.1111/j.1365-2141.1976.tb00972.x. View

15.

Plattner H, Wachter E, Grobner P . A heme-nonapeptide tracer for electron microscopy. Preparation, characterization and comparison with other heme-tracers. Histochemistry. 1977; 53(3):223-42. DOI: 10.1007/BF00511078. View

16.

Laudano A, Doolittle R . Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers. Proc Natl Acad Sci U S A. 1978; 75(7):3085-9. PMC: 392718. DOI: 10.1073/pnas.75.7.3085. View

17.

Jilek F, HORMANN H . Fibronectin (cold-insoluble globulin), V[1]. Mediation of fibrin-monomer binding to macrophages. Hoppe Seylers Z Physiol Chem. 1978; 359(11):1603-5. View

18.

Muller-Berghaus G, Mahn I, Krell W . Formation and dissociation of soluble fibrin complexes in plasma at 20 degrees C and at 37 degrees C. Thromb Res. 1979; 14(4-5):561-72. DOI: 10.1016/0049-3848(79)90112-9. View

19.

Dardik B, SHAINOFF J . Crosslinking of monomeric fibrin by factor XIIIa. Thromb Haemost. 1979; 42(3):864-72. View

20.

Fowler W, Erickson H . Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy. J Mol Biol. 1979; 134(2):241-9. DOI: 10.1016/0022-2836(79)90034-2. View