메뉴 건너뛰기




Volumn 250, Issue 1-2, 2007, Pages 14-23

Differentiation of murine B cells induced by chondroitin sulfate B

Author keywords

CD138; Chondroitin sulfate B (CSB); Differentiation; IgM; Murine B cells; Protein kinase C

Indexed keywords

2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; CD45RB ANTIGEN; CHONDROITIN 4 SULFATE; DERMATAN SULFATE; HEPARIN; HYALURONIC ACID; IMMUNOGLOBULIN M; INTERLEUKIN 4; INTERLEUKIN 5; SYNDECAN 1; WORTMANNIN;

EID: 40949158805     PISSN: 00088749     EISSN: 10902163     Source Type: Journal    
DOI: 10.1016/j.cellimm.2007.12.002     Document Type: Article
Times cited : (11)

References (37)
  • 1
    • 0023049693 scopus 로고
    • Proteoglycans in health and disease: structures and functions
    • Poole A.R. Proteoglycans in health and disease: structures and functions. Biochem. J. 236 (1986) 1-14
    • (1986) Biochem. J. , vol.236 , pp. 1-14
    • Poole, A.R.1
  • 2
    • 0026507880 scopus 로고
    • Proteoglycans: many forms and many functions
    • Hardingham T.E., and Fosang A.J. Proteoglycans: many forms and many functions. FASEB J. 6 (1992) 861-870
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 4
    • 0036744549 scopus 로고    scopus 로고
    • Dermatan sulfate: new functions from an old glycosaminoglycan
    • Trowbridge J.M., and Gallo R.L. Dermatan sulfate: new functions from an old glycosaminoglycan. Glycobiology 12 (2002) 117R-125R
    • (2002) Glycobiology , vol.12
    • Trowbridge, J.M.1    Gallo, R.L.2
  • 5
    • 30744451472 scopus 로고    scopus 로고
    • Glycosaminoglycans and their proteoglycans: host-associated molecular patterns for initiation and modulation of inflammation
    • Taylor K.R., and Gallo R.L. Glycosaminoglycans and their proteoglycans: host-associated molecular patterns for initiation and modulation of inflammation. FASEB J. 20 (2006) 9-22
    • (2006) FASEB J. , vol.20 , pp. 9-22
    • Taylor, K.R.1    Gallo, R.L.2
  • 6
    • 0028057914 scopus 로고
    • Zonal distribution of chondroitin-4-sulfate/dermatan sulphate and chondroitin-6-sulfate in normal and diseased human synovium
    • Worral J.G., Wilkinson L.S., Bayliss M.T., and Edwards J.C.W. Zonal distribution of chondroitin-4-sulfate/dermatan sulphate and chondroitin-6-sulfate in normal and diseased human synovium. Ann. Rheum. Dis. 53 (1994) 35-38
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 35-38
    • Worral, J.G.1    Wilkinson, L.S.2    Bayliss, M.T.3    Edwards, J.C.W.4
  • 7
    • 0020580563 scopus 로고
    • Connective tissue activation. XXV. Regulation of proteoglycan synthesis in human synovial cells
    • Castor C.W., Roberts D.J., Hossler P.A., and Bignall M.C. Connective tissue activation. XXV. Regulation of proteoglycan synthesis in human synovial cells. Arthritis Rheum. 26 (1983) 522-527
    • (1983) Arthritis Rheum. , vol.26 , pp. 522-527
    • Castor, C.W.1    Roberts, D.J.2    Hossler, P.A.3    Bignall, M.C.4
  • 8
    • 0019188798 scopus 로고
    • Synovial membrane in rheumatoid arthritis: determination of glycosaminoglycans and age-dependent correlations
    • Kittlick P.D., Bihari-Varga M., Fischer J., Kiss N., Henzgen S., and Raabe G. Synovial membrane in rheumatoid arthritis: determination of glycosaminoglycans and age-dependent correlations. Exp. Pathol. 18 (1980) 197-203
    • (1980) Exp. Pathol. , vol.18 , pp. 197-203
    • Kittlick, P.D.1    Bihari-Varga, M.2    Fischer, J.3    Kiss, N.4    Henzgen, S.5    Raabe, G.6
  • 9
    • 0025343253 scopus 로고
    • Structural and biochemical abnormalities of articular cartilage in rheumatoid arthritis
    • Mitrovic D.R., and Darmon N. Structural and biochemical abnormalities of articular cartilage in rheumatoid arthritis. Rheumatol. Int. 10 (1990) 31-37
    • (1990) Rheumatol. Int. , vol.10 , pp. 31-37
    • Mitrovic, D.R.1    Darmon, N.2
  • 11
    • 33644645844 scopus 로고    scopus 로고
    • Inhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis
    • Chang X., Yamada R., and Yamamoto K. Inhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis. Arthritis Res. Ther. 7 (2005) R268-R273
    • (2005) Arthritis Res. Ther. , vol.7
    • Chang, X.1    Yamada, R.2    Yamamoto, K.3
  • 12
    • 0030453765 scopus 로고    scopus 로고
    • Fibrin degradation in the synovial fluid of rheumatoid arthritis patients: a model for extravascular fibrinolysis
    • Carmassi F., de Negri F., Morale M., Song K.Y., and Chung S.I. Fibrin degradation in the synovial fluid of rheumatoid arthritis patients: a model for extravascular fibrinolysis. Semin. Thromb. Hemost. 22 (1996) 489-496
    • (1996) Semin. Thromb. Hemost. , vol.22 , pp. 489-496
    • Carmassi, F.1    de Negri, F.2    Morale, M.3    Song, K.Y.4    Chung, S.I.5
  • 14
    • 0037195179 scopus 로고    scopus 로고
    • Glycosaminoglycans are a potential cause of rheumatoid arthritis
    • Wang J.Y., and Roehrl M.H. Glycosaminoglycans are a potential cause of rheumatoid arthritis. Proc. Natl. Acad. Sci. USA 99 (2002) 14362-14367
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14362-14367
    • Wang, J.Y.1    Roehrl, M.H.2
  • 15
    • 19344373929 scopus 로고    scopus 로고
    • PKC- and PI3K-dependent but ERK-independent proliferation of murine splenic B cells stimulated by chondroitin sulfate B
    • Aoyama E., Yoshihara R., Tai A., Yamamoto I., and Gohda E. PKC- and PI3K-dependent but ERK-independent proliferation of murine splenic B cells stimulated by chondroitin sulfate B. Immunol. Lett. 99 (2005) 80-84
    • (2005) Immunol. Lett. , vol.99 , pp. 80-84
    • Aoyama, E.1    Yoshihara, R.2    Tai, A.3    Yamamoto, I.4    Gohda, E.5
  • 16
    • 0032126673 scopus 로고    scopus 로고
    • Differential effects of chondroitin sulfates A and B on monocyte and B-cell activation: evidence for B-cell activation via a CD44-dependent pathway
    • Rachmilewitz J., and Tykocinski M.L. Differential effects of chondroitin sulfates A and B on monocyte and B-cell activation: evidence for B-cell activation via a CD44-dependent pathway. Blood 92 (1998) 223-229
    • (1998) Blood , vol.92 , pp. 223-229
    • Rachmilewitz, J.1    Tykocinski, M.L.2
  • 17
    • 0021881521 scopus 로고
    • Activation of human B cells and inhibition of their terminal differentiation by monoclonal anti-μ antibodies
    • Maruyama S., Kubagawa H., and Cooper M.D. Activation of human B cells and inhibition of their terminal differentiation by monoclonal anti-μ antibodies. J. Immunol. 135 (1985) 192-199
    • (1985) J. Immunol. , vol.135 , pp. 192-199
    • Maruyama, S.1    Kubagawa, H.2    Cooper, M.D.3
  • 18
    • 33947716710 scopus 로고    scopus 로고
    • CD138 cross-linking enhances TLR-induced B cell proliferation but decreases IgM plasma cell differentiation
    • Manjarrez-Orduño N., Moreno-García M.E., Fink K., and Santos-Argumedo L. CD138 cross-linking enhances TLR-induced B cell proliferation but decreases IgM plasma cell differentiation. Eur. J. Immunol. 37 (2007) 358-367
    • (2007) Eur. J. Immunol. , vol.37 , pp. 358-367
    • Manjarrez-Orduño, N.1    Moreno-García, M.E.2    Fink, K.3    Santos-Argumedo, L.4
  • 19
    • 0031759388 scopus 로고    scopus 로고
    • SKW 6. 4 cell differentiation induced by interleukin 6 is stimulated by butyrate
    • Kawamoto T., Gohda E., Iji H., Fujiwara M., and Yamamoto I. SKW 6. 4 cell differentiation induced by interleukin 6 is stimulated by butyrate. Immunopharmacology 40 (1998) 119-130
    • (1998) Immunopharmacology , vol.40 , pp. 119-130
    • Kawamoto, T.1    Gohda, E.2    Iji, H.3    Fujiwara, M.4    Yamamoto, I.5
  • 20
    • 0020537688 scopus 로고
    • A solid-phase immunoenzymatic technique for the enumeration of specific antibody-secreting cells
    • Sedgwick J.D., and Holt P.G. A solid-phase immunoenzymatic technique for the enumeration of specific antibody-secreting cells. J. Immunol. Methods 57 (1983) 301-309
    • (1983) J. Immunol. Methods , vol.57 , pp. 301-309
    • Sedgwick, J.D.1    Holt, P.G.2
  • 21
    • 0028054988 scopus 로고
    • B cell differentiation induced by helper T cell membranes: evidence for sequential isotype switching and a requirement for lymphokines during proliferation
    • Hodgkin P.D., Castle B.E., and Kehry M.R. B cell differentiation induced by helper T cell membranes: evidence for sequential isotype switching and a requirement for lymphokines during proliferation. Eur. J. Immunol. 24 (1994) 239-246
    • (1994) Eur. J. Immunol. , vol.24 , pp. 239-246
    • Hodgkin, P.D.1    Castle, B.E.2    Kehry, M.R.3
  • 22
    • 0024755681 scopus 로고
    • B lymphocytes express and lose syndecan at specific stages of differentiation
    • Sanderson R.D., Lalor P., and Bernfield M. B lymphocytes express and lose syndecan at specific stages of differentiation. Cell Regul. 1 (1989) 27-35
    • (1989) Cell Regul. , vol.1 , pp. 27-35
    • Sanderson, R.D.1    Lalor, P.2    Bernfield, M.3
  • 23
    • 0035194463 scopus 로고    scopus 로고
    • Plasma cells: finding new light at the end of B cell development
    • Calame K.L. Plasma cells: finding new light at the end of B cell development. Nat. Immunol. 2 (2001) 1103-1108
    • (2001) Nat. Immunol. , vol.2 , pp. 1103-1108
    • Calame, K.L.1
  • 24
    • 0030989022 scopus 로고    scopus 로고
    • Hyaluronate-CD44 interactions can induce murine B-cell activation
    • Rafi A., Nagarkatti M., and Nagarkatti P.S. Hyaluronate-CD44 interactions can induce murine B-cell activation. Blood 89 (1997) 2901-2908
    • (1997) Blood , vol.89 , pp. 2901-2908
    • Rafi, A.1    Nagarkatti, M.2    Nagarkatti, P.S.3
  • 25
    • 0032561306 scopus 로고    scopus 로고
    • Dermatan sulfate released after injury is a potent promoter of fibroblast growth factor-2 function
    • Penc S.F., Pomahac B., Winkler T., Dorschner R.A., Eriksson E., Herndon M., and Gallo R.L. Dermatan sulfate released after injury is a potent promoter of fibroblast growth factor-2 function. J. Biol. Chem. 273 (1998) 28116-28121
    • (1998) J. Biol. Chem. , vol.273 , pp. 28116-28121
    • Penc, S.F.1    Pomahac, B.2    Winkler, T.3    Dorschner, R.A.4    Eriksson, E.5    Herndon, M.6    Gallo, R.L.7
  • 27
    • 0033555829 scopus 로고    scopus 로고
    • Xid-like immunodeficiency in mice with disruption of the p85α subunit of phosphoinositide 3-kinase
    • Suzuki H., Terauchi Y., Fujiwara M., Aizawa S., Yazaki Y., Kadowaki T., and Koyasu S. Xid-like immunodeficiency in mice with disruption of the p85α subunit of phosphoinositide 3-kinase. Science 283 (1999) 390-392
    • (1999) Science , vol.283 , pp. 390-392
    • Suzuki, H.1    Terauchi, Y.2    Fujiwara, M.3    Aizawa, S.4    Yazaki, Y.5    Kadowaki, T.6    Koyasu, S.7
  • 28
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α
    • Fruman D.A., Snapper S.B., Yballe C.M., Davidson L., Yu J.Y., Alt F.W., et al. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α. Science 283 (1999) 393-397
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1    Snapper, S.B.2    Yballe, C.M.3    Davidson, L.4    Yu, J.Y.5    Alt, F.W.6
  • 29
    • 0037119630 scopus 로고    scopus 로고
    • A crucial role for the p110δ subunit of phosphatidylinositol 3-kinase in B cell development and activation
    • Clayton E., Bardi G., Bell S.E., Chantry D., Downes C.P., Gray A., et al. A crucial role for the p110δ subunit of phosphatidylinositol 3-kinase in B cell development and activation. J. Exp. Med. 196 (2002) 753-763
    • (2002) J. Exp. Med. , vol.196 , pp. 753-763
    • Clayton, E.1    Bardi, G.2    Bell, S.E.3    Chantry, D.4    Downes, C.P.5    Gray, A.6
  • 30
    • 33746054494 scopus 로고    scopus 로고
    • Interleukin-5 regulates genes involved in B-cell terminal maturation
    • Horikawa K., and Takatsu K. Interleukin-5 regulates genes involved in B-cell terminal maturation. Immunology 118 (2006) 497-508
    • (2006) Immunology , vol.118 , pp. 497-508
    • Horikawa, K.1    Takatsu, K.2
  • 31
    • 33749522228 scopus 로고    scopus 로고
    • ERK signaling is a molecular switch integrating opposing inputs from B cell receptor and T cell cytokines to control TLR-driven plasma cell differentiation
    • Rui L., Healy J.I., Blasioli J., and Goodnow C.C. ERK signaling is a molecular switch integrating opposing inputs from B cell receptor and T cell cytokines to control TLR-driven plasma cell differentiation. J. Immunol. 177 (2006) 5337-5346
    • (2006) J. Immunol. , vol.177 , pp. 5337-5346
    • Rui, L.1    Healy, J.I.2    Blasioli, J.3    Goodnow, C.C.4
  • 32
    • 17844410418 scopus 로고    scopus 로고
    • B cell receptor (BCR) cross-talk: IL-4 creates an alternate pathway for BCR-induced ERK activation that is phosphatidylinositol 3-kinase independent
    • Guo B., and Rothstein T.L. B cell receptor (BCR) cross-talk: IL-4 creates an alternate pathway for BCR-induced ERK activation that is phosphatidylinositol 3-kinase independent. J. Immunol. 174 (2005) 5375-5381
    • (2005) J. Immunol. , vol.174 , pp. 5375-5381
    • Guo, B.1    Rothstein, T.L.2
  • 33
    • 0034634577 scopus 로고    scopus 로고
    • Binding of a large chondroitin sulfate/dermatan sulfate proteoglycan, versican, to L-selectin, P-selectin, and CD44
    • Kawashima H., Hirose M., Hirose J., Nagakubo D., Plaas A.H.K., and Miyasaka M. Binding of a large chondroitin sulfate/dermatan sulfate proteoglycan, versican, to L-selectin, P-selectin, and CD44. J. Biol. Chem. 275 (2000) 35448-35456
    • (2000) J. Biol. Chem. , vol.275 , pp. 35448-35456
    • Kawashima, H.1    Hirose, M.2    Hirose, J.3    Nagakubo, D.4    Plaas, A.H.K.5    Miyasaka, M.6
  • 34
    • 0027282460 scopus 로고
    • The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44
    • Naujokas M.F., Morin M., Anderson M.S., Peterson M., and Miller J. The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44. Cell 74 (1993) 257-268
    • (1993) Cell , vol.74 , pp. 257-268
    • Naujokas, M.F.1    Morin, M.2    Anderson, M.S.3    Peterson, M.4    Miller, J.5
  • 35
    • 0028965095 scopus 로고
    • A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation
    • Toyama-Sorimachi N., Sorimachi H., Tobita Y., Kitamura F., Yagita H., Suzuki K., et al. A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation. J. Biol. Chem. 270 (1995) 7437-7444
    • (1995) J. Biol. Chem. , vol.270 , pp. 7437-7444
    • Toyama-Sorimachi, N.1    Sorimachi, H.2    Tobita, Y.3    Kitamura, F.4    Yagita, H.5    Suzuki, K.6
  • 36
    • 0025245009 scopus 로고
    • IL-5 induces a Pgp-1 (CD44) bright B cell subpopulation that is highly enriched in proliferative and Ig secretory activity and binds to hyaluronate
    • Murakami S., Miyake K., June C.H., Kincade P.W., and Hodes R.J. IL-5 induces a Pgp-1 (CD44) bright B cell subpopulation that is highly enriched in proliferative and Ig secretory activity and binds to hyaluronate. J. Immunol. 145 (1990) 3618-3627
    • (1990) J. Immunol. , vol.145 , pp. 3618-3627
    • Murakami, S.1    Miyake, K.2    June, C.H.3    Kincade, P.W.4    Hodes, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.