Secretion of plasminogen activator by the human macrophage‐like cell line, GCT: separation from colony‐stimulating and erythropoiesis‐enhancing activities

Summary. The human macrophage‐like cell line, GCT, elaborates monokines such as colony‐stimulating activity (CSA) and erythropoiesis‐enhancing activity (EEA) which stimulate the growth of primitive blood progenitors in culture. These cells also secrete a fibrinolysis activator (FA), which can be identified if cells are cultured in serum‐free medium. FA was found to have a similar molecular weight to CSA and EEA by gel filtration but could be separated from them by ion exchange chromatography. Subcellular fractionation of GCT cells indicated that fibrinolytic activity was present in the cell membranes and cytosol, whereas CSA and EEA were present only in the cytosol. FA resembled urokinase in molecular weight and its strict requirement for plasminogen as a substrate. Double immunodiffusion of GCT activator and urokinase against anti‐urokinase antiserum resulted in a line of identity, and incubation of activator with antiserum resulted in loss of its fibrinolytic activity. Thus, GCT activator was similar, if not identical to the plasminogen activator, urokinase.

[1]  A. Lichtman,et al.  Calcium transport and calcium-ATPase activity in human lymphocyte plasma membrane vesicles. , 1981, The Journal of biological chemistry.

[2]  D. Rijken,et al.  PRODUCTION BY HUMAN TISSUES IN CULTURE OF IMMUNOLOGICALLY DISTINCT, MULTIPLE MOLECULAR WEIGHT FORMS OF PLASMINOGEN ACTIVATORS * , 1981, Annals of the New York Academy of Sciences.

[3]  M. Wainberg,et al.  Plasminogen activator is an apparent lymphocyte mitogen. , 1981, Journal of immunology.

[4]  J. Maillard,et al.  Plasminogen activation by normal B lymphocytes, a function associated with the cell membrane. , 1981, Journal of immunology.

[5]  J. Dipersio,et al.  The fractionation, characterization, and subcellular localization of colony-stimulating activities released by the human monocyte-like cell line, GCT. , 1980, Blood.

[6]  P. Rowley,et al.  Trypsin enhances erythropoiesis in vitro. , 1980, The Journal of laboratory and clinical medicine.

[7]  C. Francis,et al.  Plasmic degradation of crosslinked fibrin. I. Structural analysis of the particulate clot and identification of new macromolecular-soluble complexes. , 1980, Blood.

[8]  R. Roblin,et al.  Dexamethasone regulation of plasminogen activator in embryonic and tumor-derived human cells. , 1980, Cancer research.

[9]  A. Burgess,et al.  Stimulation of macrophage plasminogen activator activity by colony‐stimulating factors , 1980, Journal of cellular physiology.

[10]  P. Black,et al.  Evidence for membrane association of plasminogen activator activity in mouse macrophages. , 1980, Biochemical and biophysical research communications.

[11]  R. Roblin,et al.  Immunological quantitation and immunoadsorption of urokinase-like plasminogen activators secreted by human cells. , 1980, The Journal of biological chemistry.

[12]  E. Hoal,et al.  Molecular species of plasminogen activators secreted by normal and neoplastic human cells. , 1980, Cancer research.

[13]  S. Gordon,et al.  Secretion of plasminogen activator by bone marrow-derived mononuclear phagocytes and its enhancement by colony-stimulating factor , 1979, The Journal of experimental medicine.

[14]  R. Roblin,et al.  Immunological characterization of multiple weight forms of human cell plasminogen activators. , 1979, The Journal of biological chemistry.

[15]  Z. Werb Biochemical actions of glucocorticoids on macrophages in culture. Specific inhibition of elastase, collagenase, and plasminogen activator secretion and effects on other metabolic functions , 1978, The Journal of experimental medicine.

[16]  Z. Cohn,et al.  Bacille Calmette-Guerin infection in the mouse. Regulation of macrophage plasminogen activator by T lymphocytes and specific antigen , 1978, The Journal of experimental medicine.

[17]  K.,et al.  Human cell lines that elaborate colon-stimulating activity for the marrow cells of man and other species. , 1978, Blood.

[18]  D. Loskutoff,et al.  Synthesis of a fibrinolytic activator and inhibitor by endothelial cells. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[19]  J. Vassalli,et al.  Macrophage plasminogen activator: induction by concanavalin A and phorbol myristate acetate , 1977, Cell.

[20]  A. Yunis,et al.  Purification and characterization of a plasminogen activator secreted by cultured human pancreatic carcinoma cells. , 1977, Biochemistry.

[21]  J. Vassalli,et al.  Macrophage plasminogen activator: induction by products of activated lymphoid cells , 1977, The Journal of experimental medicine.

[22]  G. Barlow,et al.  Plasminogen activator from human embryonic kidney cell cultures. Evidence for a proactivator. , 1977, Biochimica et biophysica acta.

[23]  L. Holmberg,et al.  Purification of urokinase by affinity chromatography. , 1976, Biochimica et biophysica acta.

[24]  J. Vassalli,et al.  Macrophage plasminogen activator: Modulation of enzyme production by anti-inflammatory steroids, mitotic inhibitors, and cyclic nucleotides , 1976, Cell.

[25]  W. Doleschel [Isolation of a third human urokinase (S0 type)]. , 1975, Wiener klinische Wochenschrift.

[26]  Z. Cohn,et al.  INDUCTION OF MACROPHAGE PLASMINOGEN ACTIVATOR BY ENDOTOXIN STIMULATION AND PHAGOCYTOSIS , 1974, The Journal of experimental medicine.

[27]  C. Bona,et al.  Proteases as mitogens. The Effect of trypsin and pronase on mouse and human lymphocytes. , 1974, Experimental cell research.

[28]  J. Unkeless,et al.  SECRETION OF PLASMINOGEN ACTIVATOR BY STIMULATED MACROPHAGES , 1974, The Journal of experimental medicine.

[29]  D. Neville Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system. , 1971, The Journal of biological chemistry.

[30]  H. Rubin,et al.  Release from Density Dependent Growth Inhibition by Proteolytic Enzymes , 1970, Nature.

[31]  M. Burger Proteolytic Enzymes Initiating Cell Division and Escape from Contact Inhibition of Growth , 1970, Nature.

[32]  H. Kwaan,et al.  Origin of fibrinolytic activity in cultures of the human kidney. , 1967, The Journal of laboratory and clinical medicine.

[33]  J. Margolis,et al.  Polyacrylamide Gel-electrophoresis across a Molecular Sieve Gradient , 1967, Nature.

[34]  J. Monier,et al.  Antinuclear Autoantibodies in Swiss Mice Thymectomized at Birth , 1967, Nature.

[35]  W. White,et al.  The isolation and characterization of plasminogen activators (urokinase) from human urine. , 1966, Biochemistry.

[36]  M. Tsapogas,et al.  EXPERIMENTAL THROMBOLYSIS WITH STREPTOKINASE AND UROKINASE , 1964 .

[37]  T. Astrup,et al.  The fibrin plate method for estimating fibrinolytic activity. , 1952, Archives of biochemistry and biophysics.

[38]  D. Rijken,et al.  Immunological characterization of plasminogen activator activities in human tissues and body fluids. , 1981, The Journal of laboratory and clinical medicine.

[39]  J. Dipersio,et al.  Erythropoietic enhancing activity (EEA) secreted by the human cell line, GCT. , 1980, Journal of supramolecular structure.

[40]  O OUCHTERLONY,et al.  Diffusion-in-gel methods for immunological analysis. , 1958, Progress in allergy.