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Volumn 147, Issue 2, 1999, Pages 263-275

Atherogenic properties of human monocytes induced by the carboxyl terminal proteolytic fragment of alpha-1-antitrypsin

Author keywords

Alpha 1 antitrypsin; Atherogenesis; Cytokines; Human monocytes; Lipid oxidation

Indexed keywords

ALPHA 1 ANTITRYPSIN; GLUTATHIONE REDUCTASE; LOW DENSITY LIPOPROTEIN RECEPTOR;

EID: 0032713568     PISSN: 00219150     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0021-9150(99)00194-X     Document Type: Article
Times cited : (25)

References (60)
  • 1
    • 0031969582 scopus 로고    scopus 로고
    • T-lymphocytes and monocytes in atherogenesis
    • Schmitz G., Herr A.S., Rothe G. T-lymphocytes and monocytes in atherogenesis. Herz. 23:1998;168-177.
    • (1998) Herz , vol.23 , pp. 168-177
    • Schmitz, G.1    Herr, A.S.2    Rothe, G.3
  • 2
    • 0030781917 scopus 로고    scopus 로고
    • Anti-CD43 inhibits monocyte-endothelial adhesion in inflammation and atherogenesis
    • McEvoy L.M., Jutila M.A., Tsao P.S., Cooke J.P., Butcher E.C. Anti-CD43 inhibits monocyte-endothelial adhesion in inflammation and atherogenesis. Blood. 90:1997;3587-3594.
    • (1997) Blood , vol.90 , pp. 3587-3594
    • McEvoy, L.M.1    Jutila, M.A.2    Tsao, P.S.3    Cooke, J.P.4    Butcher, E.C.5
  • 3
    • 0029805968 scopus 로고    scopus 로고
    • Modification of macrophage function and effects on atherosclerosis
    • Murakami T., Yamada N. Modification of macrophage function and effects on atherosclerosis. Curr. Opin. Lipidol. 7:1996;320-323.
    • (1996) Curr. Opin. Lipidol. , vol.7 , pp. 320-323
    • Murakami, T.1    Yamada, N.2
  • 4
    • 0017354616 scopus 로고
    • Molecular interactions in human atherosclerotic plaques
    • Smith E.B. Molecular interactions in human atherosclerotic plaques. Am. J. Pathol. 86:1977;665-674.
    • (1977) Am. J. Pathol. , vol.86 , pp. 665-674
    • Smith, E.B.1
  • 5
    • 0018571222 scopus 로고
    • Soluble proteins in the human atherosclerotic plaque. With spectral reference to immunoglobulins, C3-complement component, α1-antitrypsin and α2-macroglobulin
    • Hollander W., Colombo M.A., Kirkpatrick B., Paddock J. Soluble proteins in the human atherosclerotic plaque. With spectral reference to immunoglobulins, C3-complement component, α1-antitrypsin and α2-macroglobulin. Atherosclerosis. 34:1979;391-405.
    • (1979) Atherosclerosis , vol.34 , pp. 391-405
    • Hollander, W.1    Colombo, M.A.2    Kirkpatrick, B.3    Paddock, J.4
  • 6
  • 9
    • 0031893793 scopus 로고    scopus 로고
    • Alpha1-antitrypsin and protease complexation is induced by lipopolysacchride, interleukin-1β in monocytes
    • Knoell D.L., Ralston D.R., Coulter K.R., Wewers M.D. Alpha1-antitrypsin and protease complexation is induced by lipopolysacchride, interleukin-1β in monocytes. Am. J. Respir. Crit. Care Med. 157:1998;246-255.
    • (1998) Am. J. Respir. Crit. Care Med. , vol.157 , pp. 246-255
    • Knoell, D.L.1    Ralston, D.R.2    Coulter, K.R.3    Wewers, M.D.4
  • 10
    • 0023816765 scopus 로고
    • Distinct and additive of elastase and endotoxin on expression of α1 proteinase inhibitor in mononuclear phagocytes
    • Perlmuter D.H., Punsal P.I. Distinct and additive of elastase and endotoxin on expression of α1 proteinase inhibitor in mononuclear phagocytes. J. Biol. Chem. 263:1988;16499-16503.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16499-16503
    • Perlmuter, D.H.1    Punsal, P.I.2
  • 11
    • 0024334846 scopus 로고
    • Interferon β2/interleukin 6 modulates synthesis of α1-antitrypsin in human mononuclear phagocytes and in human hepatoma cells
    • Perlmutter D.H., May L.T., Sehgal P.B. Interferon β2/interleukin 6 modulates synthesis of α1-antitrypsin in human mononuclear phagocytes and in human hepatoma cells. J. Clin. Invest. 84:1989;138-144.
    • (1989) J. Clin. Invest. , vol.84 , pp. 138-144
    • Perlmutter, D.H.1    May, L.T.2    Sehgal, P.B.3
  • 12
    • 0030062157 scopus 로고    scopus 로고
    • The biostructural pathology of the serpins: Critical function of sheet opening mechanism
    • Carrell R.W., Stein P.E. The biostructural pathology of the serpins: critical function of sheet opening mechanism. Biol. Chem. Hoppe-Seyler. 377:1996;1-17.
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 1-17
    • Carrell, R.W.1    Stein, P.E.2
  • 13
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell R.W., Lomas D.A. Conformational disease. Lancet. 350:1997;134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 14
    • 0023700976 scopus 로고
    • Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and large increase in conformational stability upon cleavage at their reactive sites
    • Bruch M., Weiss V., Engel J. Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and large increase in conformational stability upon cleavage at their reactive sites. J. Biol. Chem. 263:1988;166626-166630.
    • (1988) J. Biol. Chem. , vol.263 , pp. 166626-166630
    • Bruch, M.1    Weiss, V.2    Engel, J.3
  • 16
    • 0025822649 scopus 로고
    • The SEC receptor recognizes a pentapeptide neodomain of α1-antitrypsin-protease complexes
    • Joslin G., Fallon R.J., Bullock J., Adams S.P., Perlmutter D.H. The SEC receptor recognizes a pentapeptide neodomain of α1-antitrypsin-protease complexes. J. Biol. Chem. 266:1991;11281-11288.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11281-11288
    • Joslin, G.1    Fallon, R.J.2    Bullock, J.3    Adams, S.P.4    Perlmutter, D.H.5
  • 18
    • 0025708374 scopus 로고
    • Human neutrophil collagenase cleaves α-1-antitrypsin
    • Michaelis J., Vissers M.C., Winterbourn C.C. Human neutrophil collagenase cleaves α-1-antitrypsin. Biochem. J. 270:1990;809-814.
    • (1990) Biochem. J. , vol.270 , pp. 809-814
    • Michaelis, J.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 20
    • 0000696617 scopus 로고
    • The inactivation of human plasma α-1-proteinase inhibitor by proteinases from Staphylococcus aureus
    • Potempa J., Watorek W., Travis J. The inactivation of human plasma α-1-proteinase inhibitor by proteinases from Staphylococcus aureus. J. Biol. Chem. 254:1979;5317-5320.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5317-5320
    • Potempa, J.1    Watorek, W.2    Travis, J.3
  • 21
    • 0020315222 scopus 로고
    • Inactivation of human plasma α-1-proteinase inhibitor by a metalloproteinase from Serratia marcescens
    • Virca G.D., Lyerly D., Kreger A., Travis J. Inactivation of human plasma α-1-proteinase inhibitor by a metalloproteinase from Serratia marcescens. Biochim. Biophys. Acta. 704:1982;267-271.
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 267-271
    • Virca, G.D.1    Lyerly, D.2    Kreger, A.3    Travis, J.4
  • 22
    • 0021254778 scopus 로고
    • Purification of human plasma α-1-proteinase inhibitor and its inactivation by Pseudomonas aeruginosa elastase
    • Morihara K., Tsuzuki H., Harada M., Iwata T. Purification of human plasma α-1-proteinase inhibitor and its inactivation by Pseudomonas aeruginosa elastase. J. Biochem. Tokyo. 95:1984;795-804.
    • (1984) J. Biochem. Tokyo , vol.95 , pp. 795-804
    • Morihara, K.1    Tsuzuki, H.2    Harada, M.3    Iwata, T.4
  • 23
    • 0026578008 scopus 로고
    • Identification of hydrophobic fragments of α-antitrypsin and C1 protease inhibitor in human bile, plasma and spleen
    • Johansson J., Gröndal S., Sjövall J., Jörnvall H., Curstedt T. Identification of hydrophobic fragments of α-antitrypsin and C1 protease inhibitor in human bile, plasma and spleen. FEBS Lett. 299:1992;146-148.
    • (1992) FEBS Lett. , vol.299 , pp. 146-148
    • Johansson, J.1    Gröndal, S.2    Sjövall, J.3    Jörnvall, H.4    Curstedt, T.5
  • 24
    • 0026664099 scopus 로고
    • Isolation and serine proteinase activity of the 44-residue C-terminal fragment of α-1-antitrypsin from human placenta
    • Niemann M.A., Narkates A.J., Miller A.J. Isolation and serine proteinase activity of the 44-residue C-terminal fragment of α-1-antitrypsin from human placenta. Matrix. 12:1992;233-241.
    • (1992) Matrix , vol.12 , pp. 233-241
    • Niemann, M.A.1    Narkates, A.J.2    Miller, A.J.3
  • 25
    • 0017651799 scopus 로고
    • Alpha-1-antitrypsin immunoreactivity in islet cells of adult human pancreas
    • Ray M.B., Geboes K., Callea F., Desmer V.J. Alpha-1-antitrypsin immunoreactivity in islet cells of adult human pancreas. Cell Tissue Res. 185:1977;63-68.
    • (1977) Cell Tissue Res. , vol.185 , pp. 63-68
    • Ray, M.B.1    Geboes, K.2    Callea, F.3    Desmer, V.J.4
  • 27
    • 0030878985 scopus 로고    scopus 로고
    • Binding of SPAAT, the 44-residue C-terminal peptide of α-1-antitrypsin, to proteins of the extracellular matrix
    • Niemann M.A., Baggott J.E., Miller E.J. Binding of SPAAT, the 44-residue C-terminal peptide of α-1-antitrypsin, to proteins of the extracellular matrix. J. Cell. Biochem. 66:1997;346-357.
    • (1997) J. Cell. Biochem. , vol.66 , pp. 346-357
    • Niemann, M.A.1    Baggott, J.E.2    Miller, E.J.3
  • 28
    • 0026026432 scopus 로고
    • Effect of pseudomonas elastase on human mononuclear phagocyte α-1-antitrypsin expression
    • Barbey-Morel C., Perlmutter D.H. Effect of pseudomonas elastase on human mononuclear phagocyte α-1-antitrypsin expression. Pediatr. Res. 29:1991;133-140.
    • (1991) Pediatr. Res. , vol.29 , pp. 133-140
    • Barbey-Morel, C.1    Perlmutter, D.H.2
  • 30
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic istel amyloid peptide amylin
    • Mirzabekov T.A., Lin M., Kagan B.L. Pore formation by the cytotoxic istel amyloid peptide amylin. J. Biol. Chem. 271:1996;1988-1992.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.2    Kagan, B.L.3
  • 31
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 32
    • 0029964207 scopus 로고    scopus 로고
    • Amyloid fibril toxicity in Alzheimer's disease and diabetes
    • Lorenzo A., Yankner B.A. Amyloid fibril toxicity in Alzheimer's disease and diabetes. Ann. New York Acad. Sci. 777:1996;89-95.
    • (1996) Ann. New York Acad. Sci. , vol.777 , pp. 89-95
    • Lorenzo, A.1    Yankner, B.A.2
  • 33
    • 0029337177 scopus 로고
    • In vitro fibril formation from α-1-antitrypsin-derived C-terminal peptides
    • Janciauskiene S., Carlemalm E., Eriksson S. In vitro fibril formation from α-1-antitrypsin-derived C-terminal peptides. Biol. Chem. Hoppe-Seyler. 376:1995;415-423.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 415-423
    • Janciauskiene, S.1    Carlemalm, E.2    Eriksson, S.3
  • 34
    • 0032526265 scopus 로고    scopus 로고
    • The C-terminal peptide of α-1-antitrypsin increases low density lipoprotein binding in HepG2 cells
    • Janciauskiene S., Lindgren S., Wright T.H. The C-terminal peptide of α-1-antitrypsin increases low density lipoprotein binding in HepG2 cells. Eur. J. Biochem. 254:1998;460-467.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 460-467
    • Janciauskiene, S.1    Lindgren, S.2    Wright, T.H.3
  • 35
    • 0032984941 scopus 로고    scopus 로고
    • Effects of fibrillar C-terminal fragment of cleaved α-1-antitrypsin on cholesterol homeostasis in HepG2 cells
    • Janciauskiene S., Lindgren S. Effects of fibrillar C-terminal fragment of cleaved α-1-antitrypsin on cholesterol homeostasis in HepG2 cells. Hepatology. 29:1999;434-442.
    • (1999) Hepatology , vol.29 , pp. 434-442
    • Janciauskiene, S.1    Lindgren, S.2
  • 36
    • 34548003946 scopus 로고
    • Efficient trace-labelling of proteins with iodine [Abstract]
    • Mc Farlane A.S. Efficient trace-labelling of proteins with iodine [Abstract]. Nature. 182:1958;53.
    • (1958) Nature , vol.182 , pp. 53
    • Mc Farlane, A.S.1
  • 38
    • 0016961001 scopus 로고
    • Isolation of lymphocytes, granulocytes and macrophages
    • Böyum A. Isolation of lymphocytes, granulocytes and macrophages. Scand. J. Immunol. Suppl. 5:1976;9-15.
    • (1976) Scand. J. Immunol. Suppl. , vol.5 , pp. 9-15
    • Böyum, A.1
  • 39
    • 0000415004 scopus 로고
    • Preparation and analysis of RNA from eukaryotic cells
    • L.G. Davis. New York: Elsevier
    • Davis L.G., Dibner M.D., Battey J.F. Preparation and analysis of RNA from eukaryotic cells. Davis L.G. Basic Methods in Molecular Biology. 1986;129-156 Elsevier, New York.
    • (1986) Basic Methods in Molecular Biology , pp. 129-156
    • Davis, L.G.1    Dibner, M.D.2    Battey, J.F.3
  • 40
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Choczynski P., Nicoletta S. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Choczynski, P.1    Nicoletta, S.2
  • 42
    • 0026054801 scopus 로고
    • Isolation of cell membranes for epidermal growth factor receptor studies
    • Lin P.H., Selinfreund R., Wharton W. Isolation of cell membranes for epidermal growth factor receptor studies. Methods Enzymol. 198:1991;251-259.
    • (1991) Methods Enzymol. , vol.198 , pp. 251-259
    • Lin, P.H.1    Selinfreund, R.2    Wharton, W.3
  • 43
    • 0019486813 scopus 로고
    • The participation of sterol carrier protein2 in the conversion of cholesterol to cholesterol ester by rat liver microsomes
    • Gavey K.L., Noland B.J., Scallen T.J. The participation of sterol carrier protein2 in the conversion of cholesterol to cholesterol ester by rat liver microsomes. J. Biol. Chem. 256:1981;2993-2999.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2993-2999
    • Gavey, K.L.1    Noland, B.J.2    Scallen, T.J.3
  • 45
    • 0031911329 scopus 로고    scopus 로고
    • Monocyte-endothelial cell interaction in atherogenesis and thrombosis
    • Ikeda U., Takahashi M., Shimada K. Monocyte-endothelial cell interaction in atherogenesis and thrombosis. Clin. Cardiol. 21:1998;11-14.
    • (1998) Clin. Cardiol. , vol.21 , pp. 11-14
    • Ikeda, U.1    Takahashi, M.2    Shimada, K.3
  • 47
    • 0032562276 scopus 로고    scopus 로고
    • Expression of LDL receptor, VLDL receptor, LDL receptor-related protein, and scavenger receptor in rabbit atherosclerotic lesions: Marked induction of scavenger receptor and VLDL receptor expression during lesion development
    • Hiltunen T.P., Luoma J.S., Nikkari T., Yla-Herttuala S. Expression of LDL receptor, VLDL receptor, LDL receptor-related protein, and scavenger receptor in rabbit atherosclerotic lesions: marked induction of scavenger receptor and VLDL receptor expression during lesion development. Circulation. 97:1998;1079-1089.
    • (1998) Circulation , vol.97 , pp. 1079-1089
    • Hiltunen, T.P.1    Luoma, J.S.2    Nikkari, T.3    Yla-Herttuala, S.4
  • 48
    • 0017648208 scopus 로고
    • Evidence for hydroxyl radical generation by human monocytes
    • Weiss S.J., King G.W., LoBuglio A.F. Evidence for hydroxyl radical generation by human monocytes. J. Clin. Invest. 60:1977;370-373.
    • (1977) J. Clin. Invest. , vol.60 , pp. 370-373
    • Weiss, S.J.1    King, G.W.2    Lobuglio, A.F.3
  • 49
    • 0344547364 scopus 로고    scopus 로고
    • Inflammatory and immunological nature of atherosclerosis
    • Watanabe T., Haraoka S., Shimokama T. Inflammatory and immunological nature of atherosclerosis. Int. J. Cardiol. 54(Suppl.):1996;S51-S60.
    • (1996) Int. J. Cardiol. , vol.54 , Issue.SUPPL.
    • Watanabe, T.1    Haraoka, S.2    Shimokama, T.3
  • 50
    • 0026096139 scopus 로고
    • Production of monoclonal antibodies against inactivated α-1-antitrypsin. Cross-reactivity with complexed α-1-antitrypsin and application in an assay to determine inactivated and complexed α-1-antitrypsin in biological fluids
    • Abbink J.J., Kamp A.M., Swaak A.J., Hack C.E. Production of monoclonal antibodies against inactivated α-1-antitrypsin. Cross-reactivity with complexed α-1-antitrypsin and application in an assay to determine inactivated and complexed α-1-antitrypsin in biological fluids. J. Immunol. Methods. 143:1991;197-208.
    • (1991) J. Immunol. Methods , vol.143 , pp. 197-208
    • Abbink, J.J.1    Kamp, A.M.2    Swaak, A.J.3    Hack, C.E.4
  • 51
    • 0026705310 scopus 로고
    • Proteolytic inactivation of α1-proteinase inhibitor and α1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases
    • Desrochers P.E., Mookhtiar K., Van Wart H.E., Hasty K.A., Weiss S.J. Proteolytic inactivation of α1-proteinase inhibitor and α1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases. J. Biol. Chem. 267:1992;5005-5012.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5005-5012
    • Desrochers, P.E.1    Mookhtiar, K.2    Van Wart, H.E.3    Hasty, K.A.4    Weiss, S.J.5
  • 52
    • 0025997534 scopus 로고
    • Kinetics and physiologic relevance of the inactivation of α1-proteinase inhibitor, α1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin)
    • Mast A.E., Enghild J.J., Nagase H., Suzuki K., Pizzo S.V., Salvesen G. Kinetics and physiologic relevance of the inactivation of α1-proteinase inhibitor, α1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin). J. Biol. Chem. 266:1991;15810-15816.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15810-15816
    • Mast, A.E.1    Enghild, J.J.2    Nagase, H.3    Suzuki, K.4    Pizzo, S.V.5    Salvesen, G.6
  • 55
    • 0031889824 scopus 로고    scopus 로고
    • Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation
    • Badman M.K., Pryce R.A., Charge S.B.P., Morris J.F., Clark A. Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation. Cell Tissue Res. 291:1998;285-294.
    • (1998) Cell Tissue Res. , vol.291 , pp. 285-294
    • Badman, M.K.1    Pryce, R.A.2    Charge, S.B.P.3    Morris, J.F.4    Clark, A.5
  • 56
    • 14844353470 scopus 로고
    • TNF-induced superoxide anion production in adherent human neutrophils involves both the p55 and p75 TNF receptors
    • Richter J., Gullberg U., Lantz M. TNF-induced superoxide anion production in adherent human neutrophils involves both the p55 and p75 TNF receptors. J. Immunol. 154:1995;4142-4149.
    • (1995) J. Immunol. , vol.154 , pp. 4142-4149
    • Richter, J.1    Gullberg, U.2    Lantz, M.3
  • 57
    • 0027417423 scopus 로고
    • Modified forms of low-density lipoprotein and atherosclerosis
    • Steinberg D. Modified forms of low-density lipoprotein and atherosclerosis. J. Int. Med. 233:1993;227-232.
    • (1993) J. Int. Med. , vol.233 , pp. 227-232
    • Steinberg, D.1
  • 58
    • 0031957128 scopus 로고    scopus 로고
    • Human CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, and VLDL
    • Calvo D., Gomez-Coronado D., Suarez Y., Lasuncion M.A., Vega M.A. Human CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, and VLDL. J. Lipid Res. 39:1998;777-788.
    • (1998) J. Lipid Res. , vol.39 , pp. 777-788
    • Calvo, D.1    Gomez-Coronado, D.2    Suarez, Y.3    Lasuncion, M.A.4    Vega, M.A.5
  • 60
    • 0031754371 scopus 로고    scopus 로고
    • LDL oxidation by activated monocytes: Characterization of the oxidized LDL and requirement for transition metal ions
    • Xing X., Baffic J., Sparrow C.P. LDL oxidation by activated monocytes: characterization of the oxidized LDL and requirement for transition metal ions. J. Lipid Res. 39:1998;2201-2208.
    • (1998) J. Lipid Res. , vol.39 , pp. 2201-2208
    • Xing, X.1    Baffic, J.2    Sparrow, C.P.3


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