메뉴 건너뛰기




Volumn 41, Issue 2, 2011, Pages 437-449

Serglycin inhibits the classical and lectin pathways of complement via its glycosaminoglycan chains: Implications for multiple myeloma

Author keywords

Complement; Multiple myeloma; Serglycin

Indexed keywords

CALCIUM; CHONDROITIN SULFATE; COMPLEMENT COMPONENT C1Q; GLYCOSAMINOGLYCAN; LECTIN; MANNOSE BINDING LECTIN; PROTEOGLYCAN; SERGLYCIN; THYMOCYTE ANTIBODY; UNCLASSIFIED DRUG;

EID: 78851470656     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201040429     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 0022359823 scopus 로고
    • Purification and analysis of the core protein of the protease-resistant intracellular chondroitin sulfate E proteoglycan from the interleukin 3-dependent mouse mast cell
    • Stevens, R. L., Otsu, K. and Austen, K. F., Purification and analysis of the core protein of the protease-resistant intracellular chondroitin sulfate E proteoglycan from the interleukin 3-dependent mouse mast cell. J. Biol. Chem. 1985. 260: 14194-14200.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14194-14200
    • Stevens, R.L.1    Otsu, K.2    Austen, K.F.3
  • 2
    • 42449101298 scopus 로고    scopus 로고
    • Serglycin - structure and biology
    • Kolset, S. O. and Tveit, H., Serglycin - structure and biology. Cell. Mol. Life Sci. 2008. 65: 1073-1085.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1073-1085
    • Kolset, S.O.1    Tveit, H.2
  • 3
    • 2342447936 scopus 로고    scopus 로고
    • Intracellular proteoglycans
    • Kolset, S. O., Prydz, K. and Pejler, G., Intracellular proteoglycans. Biochem. J. 2004. 379: 217-227.
    • (2004) Biochem. J. , vol.379 , pp. 217-227
    • Kolset, S.O.1    Prydz, K.2    Pejler, G.3
  • 5
    • 0024467227 scopus 로고
    • Modulation of the expression of chondroitin sulfate proteoglycan in stimulated human monocytes
    • Uhlin-Hansen, L., Eskeland, T. and Kolset, S. O., Modulation of the expression of chondroitin sulfate proteoglycan in stimulated human monocytes. J. Biol. Chem. 1989. 264: 14916-14922.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14916-14922
    • Uhlin-Hansen, L.1    Eskeland, T.2    Kolset, S.O.3
  • 6
    • 33748741953 scopus 로고    scopus 로고
    • Serglycin is the major secreted proteoglycan in macrophages and has a role in the regulation of macrophage tumor necrosis factor-alpha secretion in response to lipopolysaccharide
    • Zernichow, L., Abrink, M., Hallgren, J., Grujic, M., Pejler, G. and Kolset, S. O., Serglycin is the major secreted proteoglycan in macrophages and has a role in the regulation of macrophage tumor necrosis factor-alpha secretion in response to lipopolysaccharide. J. Biol. Chem. 2006. 281: 26792-26801.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26792-26801
    • Zernichow, L.1    Abrink, M.2    Hallgren, J.3    Grujic, M.4    Pejler, G.5    Kolset, S.O.6
  • 7
    • 4644322014 scopus 로고    scopus 로고
    • Serglycin is essential for maturation of mast cell secretory granule
    • Abrink, M., Grujic, M. and Pejler, G., Serglycin is essential for maturation of mast cell secretory granule. J. Biol. Chem. 2004. 279: 40897-40905.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40897-40905
    • Abrink, M.1    Grujic, M.2    Pejler, G.3
  • 8
    • 25844486023 scopus 로고    scopus 로고
    • Serglycin-deficient cytotoxic T lymphocytes display defective secretory granule maturation and granzyme B storage
    • Grujic, M., Braga, T., Lukinius, A., Eloranta, M. L., Knight, S. D., Pejler, G. and Abrink, M., Serglycin-deficient cytotoxic T lymphocytes display defective secretory granule maturation and granzyme B storage. J. Biol. Chem. 2005. 280: 33411-33418.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33411-33418
    • Grujic, M.1    Braga, T.2    Lukinius, A.3    Eloranta, M.L.4    Knight, S.D.5    Pejler, G.6    Abrink, M.7
  • 9
    • 20144380101 scopus 로고    scopus 로고
    • A novel mechanism for protein delivery: granzyme B undergoes electrostatic exchange from serglycin to target cells
    • Raja, S. M., Metkar, S. S., Honing, S., Wang, B., Russin, W. A., Pipalia, N. H., Menaa, C. et al., A novel mechanism for protein delivery: granzyme B undergoes electrostatic exchange from serglycin to target cells. J. Biol. Chem. 2005. 280: 20752-20761.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20752-20761
    • Raja, S.M.1    Metkar, S.S.2    Honing, S.3    Wang, B.4    Russin, W.A.5    Pipalia, N.H.6    Menaa, C.7
  • 10
    • 33845925571 scopus 로고    scopus 로고
    • Serglycin constitutively secreted by myeloma plasma cells is a potent inhibitor of bone mineralization in vitro
    • Theocharis, A. D., Seidel, C., Borset, M., Dobra, K., Baykov, V., Labropoulou, V., Kanakis, I. et al., Serglycin constitutively secreted by myeloma plasma cells is a potent inhibitor of bone mineralization in vitro. J. Biol. Chem. 2006. 281: 35116-35128.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35116-35128
    • Theocharis, A.D.1    Seidel, C.2    Borset, M.3    Dobra, K.4    Baykov, V.5    Labropoulou, V.6    Kanakis, I.7
  • 11
    • 34547677725 scopus 로고    scopus 로고
    • Immunodeficiency and immunotherapy in multiple myeloma
    • Pratt, G., Goodyear, O. and Moss, P., Immunodeficiency and immunotherapy in multiple myeloma. Br. J. Haematol. 2007. 138: 563-579.
    • (2007) Br. J. Haematol. , vol.138 , pp. 563-579
    • Pratt, G.1    Goodyear, O.2    Moss, P.3
  • 12
    • 0019842492 scopus 로고
    • Alternative pathway of complement in multiple myeloma
    • Kraut, E. H. and Sagone, A. L., Jr., Alternative pathway of complement in multiple myeloma. Am. J. Hematol. 1981. 11: 335-345.
    • (1981) Am. J. Hematol. , vol.11 , pp. 335-345
    • Kraut, E.H.1    Sagone Jr, A.L.2
  • 13
    • 0024452295 scopus 로고
    • Complement abnormalities in multiple myeloma
    • Zurlo, J. J., Schechter, G. P. and Fries, L. F., Complement abnormalities in multiple myeloma. Am. J. Med. 1989. 87: 411-420.
    • (1989) Am. J. Med. , vol.87 , pp. 411-420
    • Zurlo, J.J.1    Schechter, G.P.2    Fries, L.F.3
  • 16
    • 37349079469 scopus 로고    scopus 로고
    • Role of complement and complement regulators in the removal of apoptotic cells
    • Trouw, L. A., Blom, A. M. and Gasque, P., Role of complement and complement regulators in the removal of apoptotic cells. Mol. Immunol. 2008. 45: 1199-1207.
    • (2008) Mol. Immunol. , vol.45 , pp. 1199-1207
    • Trouw, L.A.1    Blom, A.M.2    Gasque, P.3
  • 17
    • 0035810399 scopus 로고    scopus 로고
    • Complement. First of two parts
    • Walport, M. J., Complement. First of two parts. N. Engl. J. Med. 2001. 344: 1058-1066.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 18
    • 0035849176 scopus 로고    scopus 로고
    • Complement. Second of two parts
    • Walport, M. J., Complement. Second of two parts. N. Engl. J. Med. 2001. 344: 1140-1144.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1140-1144
    • Walport, M.J.1
  • 19
    • 0029927303 scopus 로고    scopus 로고
    • CRP-mediated activation of complement in vivo: assessment by measuring circulating complement-C-reactive protein complexes
    • Wolbink, G. J., Brouwer, M. C., Buysmann, S., ten Berge, I. J. and Hack, C. E., CRP-mediated activation of complement in vivo: assessment by measuring circulating complement-C-reactive protein complexes. J. Immunol. 1996. 157: 473-479.
    • (1996) J. Immunol. , vol.157 , pp. 473-479
    • Wolbink, G.J.1    Brouwer, M.C.2    Buysmann, S.3    ten Berge, I.J.4    Hack, C.E.5
  • 20
    • 25444482114 scopus 로고    scopus 로고
    • The extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q
    • Sjöberg, A., Önnerfjord, P., Mörgelin, M., Heinegård, D. and Blom, A. M., The extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q. J. Biol. Chem. 2005. 280: 32301-32308.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32301-32308
    • Sjöberg, A.1    Önnerfjord, P.2    Mörgelin, M.3    Heinegård, D.4    Blom, A.M.5
  • 21
    • 59249103181 scopus 로고    scopus 로고
    • Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation
    • Sjöberg, A. P., Manderson, G. A., Mörgelin, M., Day, A. J., Heinegård, D. and Blom, A. M., Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation. Mol. Immunol. 2009. 46: 830-839.
    • (2009) Mol. Immunol. , vol.46 , pp. 830-839
    • Sjöberg, A.P.1    Manderson, G.A.2    Mörgelin, M.3    Day, A.J.4    Heinegård, D.5    Blom, A.M.6
  • 22
    • 60349127531 scopus 로고    scopus 로고
    • Complement activation and inhibition: a delicate balance
    • Sjöberg, A. P., Trouw, L. A. and Blom, A. M., Complement activation and inhibition: a delicate balance. Trends Immunol. 2009. 30: 83-90.
    • (2009) Trends Immunol. , vol.30 , pp. 83-90
    • Sjöberg, A.P.1    Trouw, L.A.2    Blom, A.M.3
  • 24
    • 0031065202 scopus 로고    scopus 로고
    • Secreted chondroitin sulfate proteoglycan of human B cell lines binds to the complement protein C1q and inhibits complex formation of C1
    • Kirschfink, M., Blase, L., Engelmann, S. and Schwartz-Albiez, R., Secreted chondroitin sulfate proteoglycan of human B cell lines binds to the complement protein C1q and inhibits complex formation of C1. J. Immunol. 1997. 158: 1324-1331.
    • (1997) J. Immunol. , vol.158 , pp. 1324-1331
    • Kirschfink, M.1    Blase, L.2    Engelmann, S.3    Schwartz-Albiez, R.4
  • 26
    • 0036464657 scopus 로고    scopus 로고
    • Limiting transplantation-related mortality following unrelated donor stem cell transplantation by using a nonmyeloablative conditioning regimen
    • Chakraverty, R., Peggs, K., Chopra, R., Milligan, D. W., Kottaridis, P. D., Verfuerth, S., Geary, J. et al., Limiting transplantation-related mortality following unrelated donor stem cell transplantation by using a nonmyeloablative conditioning regimen. Blood 2002. 99: 1071-1078.
    • (2002) Blood , vol.99 , pp. 1071-1078
    • Chakraverty, R.1    Peggs, K.2    Chopra, R.3    Milligan, D.W.4    Kottaridis, P.D.5    Verfuerth, S.6    Geary, J.7
  • 27
    • 0036682491 scopus 로고    scopus 로고
    • Autologous stem cell transplantation followed by a dose-reduced allograft induces high complete remission rate in multiple myeloma
    • Kroger, N., Schwerdtfeger, R., Kiehl, M., Sayer, H. G., Renges, H., Zabelina, T., Fehse, B. et al., Autologous stem cell transplantation followed by a dose-reduced allograft induces high complete remission rate in multiple myeloma. Blood 2002. 100: 755-760.
    • (2002) Blood , vol.100 , pp. 755-760
    • Kroger, N.1    Schwerdtfeger, R.2    Kiehl, M.3    Sayer, H.G.4    Renges, H.5    Zabelina, T.6    Fehse, B.7
  • 28
    • 28844482290 scopus 로고    scopus 로고
    • Antithymocyte globulin induces complement-dependent cell lysis and caspase-dependent apoptosis in myeloma cells
    • Ayuk, F. A., Fang, L., Fehse, B., Zander, A. R. and Kroger, N., Antithymocyte globulin induces complement-dependent cell lysis and caspase-dependent apoptosis in myeloma cells. Exp. Hematol. 2005. 33: 1531-1536.
    • (2005) Exp. Hematol. , vol.33 , pp. 1531-1536
    • Ayuk, F.A.1    Fang, L.2    Fehse, B.3    Zander, A.R.4    Kroger, N.5
  • 29
    • 75749113883 scopus 로고    scopus 로고
    • Non-collagenous Glycoproteins in the Extracellular Matrix, with Particular Reference to Cartilage and Bone
    • Wiley, New York .
    • Heinegård D., Franzén, A., Lorenzo, P., Non-collagenous Glycoproteins in the Extracellular Matrix, with Particular Reference to Cartilage and Bone. Wiley, New York 2002.
    • (2002)
    • Heinegård, D.1    Franzén, A.2    Lorenzo, P.3
  • 30
    • 0023025001 scopus 로고
    • Two novel matrix proteins isolated from articular cartilage show wide distributions among connective tissues
    • Heinegård, D., Larsson, T., Sommarin, Y., Franzen, A., Paulsson, M. and Hedbom, E., Two novel matrix proteins isolated from articular cartilage show wide distributions among connective tissues. J. Biol. Chem. 1986. 261: 13866-13872.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13866-13872
    • Heinegård, D.1    Larsson, T.2    Sommarin, Y.3    Franzen, A.4    Paulsson, M.5    Hedbom, E.6
  • 31
    • 0019472804 scopus 로고
    • Purification and radiolabeling of human C1q
    • Tenner, A. J., Lesavre, P. H. and Cooper, N. R., Purification and radiolabeling of human C1q. J. Immunol. 1981. 127: 648-653.
    • (1981) J. Immunol. , vol.127 , pp. 648-653
    • Tenner, A.J.1    Lesavre, P.H.2    Cooper, N.R.3
  • 32
    • 0028787494 scopus 로고
    • Serum amyloid P component binding to C4b-binding protein
    • Garcia de Frutos, P., Härdig, Y. and Dahlbäck, B., Serum amyloid P component binding to C4b-binding protein. J. Biol. Chem. 1995. 270: 26950-26955.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26950-26955
    • Garcia de Frutos, P.1    Härdig, Y.2    Dahlbäck, B.3
  • 33
    • 0037210218 scopus 로고    scopus 로고
    • CCP1-4 of the C4b-binding protein alpha-chain are required for factor I mediated cleavage of complement factor C3b
    • Blom, A. M., Kask, L. and Dahlbäck, B., CCP1-4 of the C4b-binding protein alpha-chain are required for factor I mediated cleavage of complement factor C3b. Mol. Immunol. 2003. 39: 547-556.
    • (2003) Mol. Immunol. , vol.39 , pp. 547-556
    • Blom, A.M.1    Kask, L.2    Dahlbäck, B.3
  • 34
    • 0018387528 scopus 로고
    • Isolation of the globular region of the subcomponent q of the C1 component of complement
    • Paques, E. P., Huber, R., Priess, H. and Wright, J. K., Isolation of the globular region of the subcomponent q of the C1 component of complement. Hoppe Seylers Z. Physiol. Chem. 1979. 360: 177-183.
    • (1979) Hoppe Seylers Z. Physiol. Chem. , vol.360 , pp. 177-183
    • Paques, E.P.1    Huber, R.2    Priess, H.3    Wright, J.K.4
  • 35
    • 0017228027 scopus 로고
    • Subunit composition and structure of subcomponent C1q of the first component of human complement
    • Reid, K. B. and Porter, R. R., Subunit composition and structure of subcomponent C1q of the first component of human complement. Biochem. J. 1976. 155: 19-23.
    • (1976) Biochem. J. , vol.155 , pp. 19-23
    • Reid, K.B.1    Porter, R.R.2
  • 36
    • 0037145715 scopus 로고    scopus 로고
    • Human colon adenocarcinoma is associated with specific post-translational modifications of versican and decorin
    • Theocharis, A. D., Human colon adenocarcinoma is associated with specific post-translational modifications of versican and decorin. Biochim. Biophys. Acta 2002. 1588: 165-172.
    • (2002) Biochim. Biophys. Acta , vol.1588 , pp. 165-172
    • Theocharis, A.D.1
  • 37
    • 0022359849 scopus 로고
    • The core proteins of large and small interstitial proteoglycans from various connective tissues form distinct subgroups
    • Heinegård, D., Björne-Persson, A., Coster, L., Franzen, A., Gardell, S., Malmström, A., Paulsson, M. et al., The core proteins of large and small interstitial proteoglycans from various connective tissues form distinct subgroups. Biochem. J. 1985. 230: 181-194.
    • (1985) Biochem. J. , vol.230 , pp. 181-194
    • Heinegård, D.1    Björne-Persson, A.2    Coster, L.3    Franzen, A.4    Gardell, S.5    Malmström, A.6    Paulsson, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.