메뉴 건너뛰기




Volumn 242, Issue 2, 1998, Pages 439-450

Secretion of plasminogen activator inhibitor 2 by human peripheral blood monocytes occurs via an Endoplasmic Reticulum-Golgi-independent pathway

Author keywords

ER Golgi independent; Monocytes; PAI 2; Secretion

Indexed keywords

LACTATE DEHYDROGENASE; PLASMINOGEN ACTIVATOR INHIBITOR 2; TUMOR NECROSIS FACTOR ALPHA;

EID: 0032145308     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4118     Document Type: Article
Times cited : (37)

References (51)
  • 1
    • 0027393310 scopus 로고
    • The ovalbumin family of serpin proteins
    • Remold O'Donnell E. The ovalbumin family of serpin proteins. FEBS. Lett. 315:1993;105-108.
    • (1993) FEBS. Lett. , vol.315 , pp. 105-108
    • Remold O'Donnell, E.1
  • 3
    • 0027367496 scopus 로고
    • Cloning and molecular characterization of a human intracellular serine proteinase inhibitor
    • Coughlin P., Sun J., Cerruti L., Salem H. H., Bird P. Cloning and molecular characterization of a human intracellular serine proteinase inhibitor. Proc. Natl. Acad. Sci. USA. 90:1993;9417-9421.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9417-9421
    • Coughlin, P.1    Sun, J.2    Cerruti, L.3    Salem, H.H.4    Bird, P.5
  • 4
    • 0028196819 scopus 로고
    • Isolation and characterization of an intracellular serine proteinase inhibitor from a monkey kidney epithelial cell line
    • Morgenstern K. A., Sprecher C. A., Holth L., Foster D., Grant F. J., Ching A., Kisiel W. Isolation and characterization of an intracellular serine proteinase inhibitor from a monkey kidney epithelial cell line. Biochemistry. 33:1994;3432-3441.
    • (1994) Biochemistry , vol.33 , pp. 3432-3441
    • Morgenstern, K.A.1    Sprecher, C.A.2    Holth, L.3    Foster, D.4    Grant, F.J.5    Ching, A.6    Kisiel, W.7
  • 5
    • 0029588530 scopus 로고
    • Molecular cloning, expression and partial characterization of two novel members of the ovalbumin family of serine proteinase inhibitors
    • Sprecher C. A., Morgenstern K. A., Mathewes S., Dahlen J. R., Schrader S. K., Foster D. C., Kisiel W. Molecular cloning, expression and partial characterization of two novel members of the ovalbumin family of serine proteinase inhibitors. J. Biol. Chem. 270:1995;29854-29861.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29854-29861
    • Sprecher, C.A.1    Morgenstern, K.A.2    Mathewes, S.3    Dahlen, J.R.4    Schrader, S.K.5    Foster, D.C.6    Kisiel, W.7
  • 6
    • 0028822769 scopus 로고
    • Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow
    • Riewald M., Schleef R. R. Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow. J. Biol. Chem. 270:1995;26754-26757.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26754-26757
    • Riewald, M.1    Schleef, R.R.2
  • 7
    • 0030025631 scopus 로고    scopus 로고
    • Proteinase inhibitor 6 cannot be secreted, which suggests a new type of cellular serpin
    • Scott F. L., Coughlin P. B., Bird C., Cerruti L., Hayman J. A., Bird P. Proteinase inhibitor 6 cannot be secreted, which suggests a new type of cellular serpin. J. Biol. Chem. 271:1996;1605-1612.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1605-1612
    • Scott, F.L.1    Coughlin, P.B.2    Bird, C.3    Cerruti, L.4    Hayman, J.A.5    Bird, P.6
  • 8
    • 0028818516 scopus 로고
    • Thrombin modulates synthesis of plasminogen activator inhibitor 2 (PAI-2) by human peripheral blood monocytes
    • Ritchie H., Jamieson A., Booth N. A. Thrombin modulates synthesis of plasminogen activator inhibitor 2 (PAI-2) by human peripheral blood monocytes. Blood. 86:1995;3428-3435.
    • (1995) Blood , vol.86 , pp. 3428-3435
    • Ritchie, H.1    Jamieson, A.2    Booth, N.A.3
  • 9
    • 0025103776 scopus 로고
    • Plasminogen activator inhibitor type-2 is a major protein induced in human fibroblasts and SK-MEL-109 melanoma cells by tumor necrosis factor
    • Pytel B. A., Peppel K., Baglioni C. Plasminogen activator inhibitor type-2 is a major protein induced in human fibroblasts and SK-MEL-109 melanoma cells by tumor necrosis factor. J. Cell Physiol. 144:1990;416-422.
    • (1990) J. Cell Physiol. , vol.144 , pp. 416-422
    • Pytel, B.A.1    Peppel, K.2    Baglioni, C.3
  • 10
    • 0028902020 scopus 로고
    • Plasminogen activator inhibitor type 2: An intracellular keratinocyte differentiation product that is incorporated into the cornified envelope
    • Jensen P. J., Wu Q., Janowitz P., Ando Y., Schechter N. M. Plasminogen activator inhibitor type 2: an intracellular keratinocyte differentiation product that is incorporated into the cornified envelope. Exp. cell res. 217:1995;65-72.
    • (1995) Exp. Cell Res. , vol.217 , pp. 65-72
    • Jensen, P.J.1    Wu, Q.2    Janowitz, P.3    Ando, Y.4    Schechter, N.M.5
  • 11
    • 0029127095 scopus 로고
    • Plasminogen activator inhibitor type 2 prevents programmed cell death of human macrophages infected withMycobacterium avium
    • Gan H., Newman G. W., Remold H. G. Plasminogen activator inhibitor type 2 prevents programmed cell death of human macrophages infected withMycobacterium avium. J. Immunol. 155:1995;1304-1315.
    • (1995) J. Immunol. , vol.155 , pp. 1304-1315
    • Gan, H.1    Newman, G.W.2    Remold, H.G.3
  • 12
    • 0025746246 scopus 로고
    • Protection from tumor necrosis factor-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2
    • Kumar S., Baglioni C. Protection from tumor necrosis factor-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2. J. Biol. Chem. 266:1991;20960-20964.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20960-20964
    • Kumar, S.1    Baglioni, C.2
  • 13
    • 0028874970 scopus 로고
    • Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor α-induced apoptosis
    • Dickinson J. L., Bates E. J., Ferrante A., Antalis T. Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor α-induced apoptosis. J. Biol. Chem. 270:1995;27894-27904.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27894-27904
    • Dickinson, J.L.1    Bates, E.J.2    Ferrante, A.3    Antalis, T.4
  • 14
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts
    • Martin S. J., Green D. R. Protease activation during apoptosis: Death by a thousand cuts. Cell. 82:1995;349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 15
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme
    • Ray C. A., Black R. A., Kronheim S. R., Greenstreet T. A., Sleath P. R., Salvasen G. S., Pickup D. J. Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme. Cell. 69:1992;597-604.
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvasen, G.S.6    Pickup, D.J.7
  • 17
    • 0028787122 scopus 로고
    • Biological and clinical aspects of plasminogen activator inhibitor type 2
    • Kruithof E. K. O., Baker M. S., Bunn C. L. Biological and clinical aspects of plasminogen activator inhibitor type 2. Blood. 86:1995;4007-4024.
    • (1995) Blood , vol.86 , pp. 4007-4024
    • Kruithof, E.K.O.1    Baker, M.S.2    Bunn, C.L.3
  • 18
    • 0023917559 scopus 로고
    • Increased release of plasminogen activator inhibitor type 2 accompanies the human mononuclear tissue factor response to lipopolysaccharide
    • Schwartz B. S., Monroe M. C., Levin E. G. Increased release of plasminogen activator inhibitor type 2 accompanies the human mononuclear tissue factor response to lipopolysaccharide. Blood. 71:1988;734-741.
    • (1988) Blood , vol.71 , pp. 734-741
    • Schwartz, B.S.1    Monroe, M.C.2    Levin, E.G.3
  • 19
    • 0029617931 scopus 로고
    • Peripheral blood monocyte synthesis of plasminogen activator inhibitor 2 (PAI-2) in response to native and modified LDL
    • Ritchie H., Jamieson A., Booth N. A. Peripheral blood monocyte synthesis of plasminogen activator inhibitor 2 (PAI-2) in response to native and modified LDL. Thromb. Haemost. 74:1995;1521-1527.
    • (1995) Thromb. Haemost. , vol.74 , pp. 1521-1527
    • Ritchie, H.1    Jamieson, A.2    Booth, N.A.3
  • 20
    • 0023857726 scopus 로고
    • A plasminogen activator inhibitor (PAI-2) circulates in two forms during pregnancy
    • Booth N. A., Reith A., Bennett B. A plasminogen activator inhibitor (PAI-2) circulates in two forms during pregnancy. Thromb. Haemost. 59:1988;77-79.
    • (1988) Thromb. Haemost. , vol.59 , pp. 77-79
    • Booth, N.A.1    Reith, A.2    Bennett, B.3
  • 23
    • 0024435761 scopus 로고
    • Functional characteristics of receptor-bound urokinase on human monocytes: Catalytic efficiency and susceptibility to inactivation by plasminogen activator inhibitors
    • Kirchheimer J. C., Remold H. G. Functional characteristics of receptor-bound urokinase on human monocytes: catalytic efficiency and susceptibility to inactivation by plasminogen activator inhibitors. Blood. 74:1989;1396-1402.
    • (1989) Blood , vol.74 , pp. 1396-1402
    • Kirchheimer, J.C.1    Remold, H.G.2
  • 24
    • 0023148141 scopus 로고
    • Phorbol ester induced biosynthesis of glycosylated and non-glycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U937 lymphoma cells
    • Genton C., Kruithof E. K. O., Schleuning W.-D. Phorbol ester induced biosynthesis of glycosylated and non-glycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U937 lymphoma cells. J. Cell Biol. 104:1987;705-712.
    • (1987) J. Cell Biol. , vol.104 , pp. 705-712
    • Genton, C.1    Kruithof, E.K.O.2    Schleuning, W.-D.3
  • 25
    • 0023124557 scopus 로고
    • Plasminogen activator-specific inhibitors produced by human monocytes/macrophages
    • Wohlwend A., Belin D., Vassalli J.-D. Plasminogen activator-specific inhibitors produced by human monocytes/macrophages. J. Exp. Med. 165:1987;320-329.
    • (1987) J. Exp. Med , vol.165 , pp. 320-329
    • Wohlwend, A.1    Belin, D.2    Vassalli, J.-D.3
  • 26
    • 0023932373 scopus 로고
    • Mammalian protein secretion without signal peptide removal: Biosynthesis of PAI-2 in U937 cells
    • Ye R. D., Wun T.-C., Sadler J. E. Mammalian protein secretion without signal peptide removal: Biosynthesis of PAI-2 in U937 cells. J. Biol. Chem. 263:1988;4869-4875.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4869-4875
    • Ye, R.D.1    Wun, T.-C.2    Sadler, J.E.3
  • 27
    • 0024461835 scopus 로고
    • Facultative polypeptide translocation allows a single mRNA to encode the secreted and cytosolic forms of PAI-2
    • Belin D., Wohlwend A., Schleuning W.-D., Kruithof E. K. O., Vassalli J.-D. Facultative polypeptide translocation allows a single mRNA to encode the secreted and cytosolic forms of PAI-2. EMBO J. 8:1989;3287-3294.
    • (1989) EMBO J. , vol.8 , pp. 3287-3294
    • Belin, D.1    Wohlwend, A.2    Schleuning, W.-D.3    Kruithof, E.K.O.4    Vassalli, J.-D.5
  • 28
    • 0025868410 scopus 로고
    • The efficiency of the uncleaved secretion signal in the PAI-2 protein can be enhanced by point mutations that increase its hydrophobicity
    • von Heijne G., Liljestrom P., Mikus P., Andersson H., Ny T. The efficiency of the uncleaved secretion signal in the PAI-2 protein can be enhanced by point mutations that increase its hydrophobicity. J. Biol. Chem. 266:1991;15240-15243.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15240-15243
    • Von Heijne, G.1    Liljestrom, P.2    Mikus, P.3    Andersson, H.4    Ny, T.5
  • 29
    • 0030064680 scopus 로고    scopus 로고
    • A two-step recognition of signal sequences determines the translocation efficiency of proteins
    • Belin D., Bost S., Vassalli J.-D., Strub K. A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J. 15:1996;468-478.
    • (1996) EMBO J. , vol.15 , pp. 468-478
    • Belin, D.1    Bost, S.2    Vassalli, J.-D.3    Strub, K.4
  • 30
    • 0027136633 scopus 로고
    • Plasminogen activator inhibitor type 2 (PAI-2) is a spontaneously polymerizing SERPIN
    • Mikus P., Urano T., Liljestrom P., Ny T. Plasminogen activator inhibitor type 2 (PAI-2) is a spontaneously polymerizing SERPIN. Eur. J. Biochem. 218:1993;1071-1082.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1071-1082
    • Mikus, P.1    Urano, T.2    Liljestrom, P.3    Ny, T.4
  • 31
    • 0029875393 scopus 로고    scopus 로고
    • Intracellular polymerization of the serpin plasminogen activator inhibitor type 2
    • Mikus P., Ny T. Intracellular polymerization of the serpin plasminogen activator inhibitor type 2. J. Biol. Chem. 271:1996;10048-10053.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10048-10053
    • Mikus, P.1    Ny, T.2
  • 33
    • 0027471154 scopus 로고
    • Use of an aqueous soluble tetrazolium formazan assay to measure viability and proliferation of lymphokine-dependent cell lines
    • Buttke T. M., McCubrey J. A., Owen T. C. Use of an aqueous soluble tetrazolium formazan assay to measure viability and proliferation of lymphokine-dependent cell lines. J. Immunol. Methods. 157:1993;233-238.
    • (1993) J. Immunol. Methods , vol.157 , pp. 233-238
    • Buttke, T.M.1    McCubrey, J.A.2    Owen, T.C.3
  • 36
    • 0026577257 scopus 로고
    • Identification of a high affinity binding protein for the regulatory subunit RIIβ of cAMP-dependent protein kinase in Golgi enriched membranes of human lymphoblasts
    • Rios R. M., Celati C., Lohmann S. M., Bornens M., Keryer G. Identification of a high affinity binding protein for the regulatory subunit RIIβ of cAMP-dependent protein kinase in Golgi enriched membranes of human lymphoblasts. EMBO J. 11:1992;1723-1731.
    • (1992) EMBO J. , vol.11 , pp. 1723-1731
    • Rios, R.M.1    Celati, C.2    Lohmann, S.M.3    Bornens, M.4    Keryer, G.5
  • 37
    • 0019513263 scopus 로고
    • Immunohistochemical localization of galactosyltransferase in human fibroblasts and HeLa cells
    • Berger E. G., Mandel T., Schlit U. Immunohistochemical localization of galactosyltransferase in human fibroblasts and HeLa cells. J. Histochem. Cytochem. 29:1981;364-370.
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 364-370
    • Berger, E.G.1    Mandel, T.2    Schlit, U.3
  • 38
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1β, a protein lacking a signal sequence
    • Rubartelli A., Cozzolino F., Talio M., Sitia R. A novel secretory pathway for interleukin-1β, a protein lacking a signal sequence. EMBO J. 9:1990;1503-1510.
    • (1990) EMBO J. , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 39
    • 0025740387 scopus 로고
    • Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland
    • Christmas P., Callaway J., Fallon J., Jones J., Haigler H. T. Selective secretion of annexin 1, a protein without a signal sequence, by the human prostate gland. J. Biol. Chem. 266:1991;2499-2507.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2499-2507
    • Christmas, P.1    Callaway, J.2    Fallon, J.3    Jones, J.4    Haigler, H.T.5
  • 40
    • 0029148162 scopus 로고
    • Glucocorticoid-induced annexin 1 secretion by monocytes and peritoneal leukocytes
    • Comera C., Russo-Marie F. Glucocorticoid-induced annexin 1 secretion by monocytes and peritoneal leukocytes. Br. J. Pharmacol. 115:1995;1043-1047.
    • (1995) Br. J. Pharmacol. , vol.115 , pp. 1043-1047
    • Comera, C.1    Russo-Marie, F.2
  • 41
    • 0025727177 scopus 로고
    • Interleukin 1 β and thioredoxin are secreted through a novel pathway of secretion
    • Rubartelli A., Bajetto A., Allavena G., Wollman E., Sitia R. Interleukin 1 β and thioredoxin are secreted through a novel pathway of secretion. Biochem. Soc. Tran. 19:1991;255-259.
    • (1991) Biochem. Soc. Tran. , vol.19 , pp. 255-259
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 42
    • 0026548976 scopus 로고
    • Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the ER-Golgi complex
    • Mignatti P., Morimoto S., Rifkin D. Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the ER-Golgi complex. J. Cell Physiol. 151:1992;81-93.
    • (1992) J. Cell Physiol. , vol.151 , pp. 81-93
    • Mignatti, P.1    Morimoto, S.2    Rifkin, D.3
  • 44
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory pathway
    • Cooper D. N. W., Barondes S. H. Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory pathway. J. Cell Biol. 110:1990;1681-1691.
    • (1990) J. Cell Biol. , vol.110 , pp. 1681-1691
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 45
    • 0030994878 scopus 로고    scopus 로고
    • Plasma membrane targetting, vesicular budding and release of galactin 3 from the cytoplasm of mammalian cells during secretion
    • Mehul B., Hughes R. C. Plasma membrane targetting, vesicular budding and release of galactin 3 from the cytoplasm of mammalian cells during secretion. J. Cell Sci. 110:1997;1169-1178.
    • (1997) J. Cell Sci. , vol.110 , pp. 1169-1178
    • Mehul, B.1    Hughes, R.C.2
  • 46
    • 0023845961 scopus 로고
    • Interleukin 1β is localized in the cytoplasmic ground substance but is largely absent from the Golgi apparatus and plasma membranes of stimulated human monocytes
    • Singer I. I., Scott S., Hall G. L., Limjuco G., Chin J., Schmidt J. A. Interleukin 1β is localized in the cytoplasmic ground substance but is largely absent from the Golgi apparatus and plasma membranes of stimulated human monocytes. J. Exp. Med. 167:1990;389-409.
    • (1990) J. Exp. Med. , vol.167 , pp. 389-409
    • Singer, I.I.1    Scott, S.2    Hall, G.L.3    Limjuco, G.4    Chin, J.5    Schmidt, J.A.6
  • 47
    • 0030791210 scopus 로고    scopus 로고
    • Regulation, location and activity of plasminogen activator inhibitor 2 (PAI-2) in peripheral blood monocytes, macrophages and foam cells
    • Ritchie H., Jamieson A., Booth N. A. Regulation, location and activity of plasminogen activator inhibitor 2 (PAI-2) in peripheral blood monocytes, macrophages and foam cells. Thromb. Haemost. 77:1997;1168-1173.
    • (1997) Thromb. Haemost. , vol.77 , pp. 1168-1173
    • Ritchie, H.1    Jamieson, A.2    Booth, N.A.3
  • 48
    • 0029861092 scopus 로고    scopus 로고
    • The exon 3 encoded sequence of the intracellular serine proteinase inhibitor plasminogen activator inhibitor 2 is a protein binding domain
    • Jensen P. H., Jensen T. G., Laug W. E., Hager H., Gliemann J., Pepinsky B. The exon 3 encoded sequence of the intracellular serine proteinase inhibitor plasminogen activator inhibitor 2 is a protein binding domain. J. Biol. Chem. 271:1996;26892-26899.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26892-26899
    • Jensen, P.H.1    Jensen, T.G.2    Laug, W.E.3    Hager, H.4    Gliemann, J.5    Pepinsky, B.6
  • 49
    • 0027263591 scopus 로고
    • Type-2 plasminogen activator inhibitor is a substrate for trophoblast transglutaminase and factor XIIIa-transglutaminase-catalyzed cross-linking to cellular and extracellular structures
    • Jensen P. H., Lorand L., Ebbesen P., Gliemann J. Type-2 plasminogen activator inhibitor is a substrate for trophoblast transglutaminase and factor XIIIa-transglutaminase-catalyzed cross-linking to cellular and extracellular structures. Eur. J. Biochem. 214:1993;141-146.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 141-146
    • Jensen, P.H.1    Lorand, L.2    Ebbesen, P.3    Gliemann, J.4
  • 50
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • Aeschlimann D., Paulsson M. Transglutaminases: Protein cross-linking enzymes in tissues and body fluids. Thromb. Haemost. 71:1994;402-415.
    • (1994) Thromb. Haemost. , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.