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Volumn 176, Issue 11, 2006, Pages 6512-6522

Function of liver activation-regulated chemokine/CC chemokine ligand 20 is differently affected by cathepsin B and cathepsin D processing

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CHEMOKINE; BETA CHEMOKINE; CALCIUM ION; CATHEPSIN B; CATHEPSIN D; CATHEPSIN H; CCL20 CHEMOKINE; CHEMOKINE; DNA; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; LIGAND; RNA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 33646857762     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.176.11.6512     Document Type: Article
Times cited : (40)

References (59)
  • 1
    • 0842324615 scopus 로고    scopus 로고
    • Chemokines: Multiple levels of leukocyte migration control
    • Moser, B., M. Wolf, A. Walz, and P. Loetscher. 2004. Chemokines: multiple levels of leukocyte migration control. Trends Immunol. 25: 75-84.
    • (2004) Trends Immunol. , vol.25 , pp. 75-84
    • Moser, B.1    Wolf, M.2    Walz, A.3    Loetscher, P.4
  • 2
    • 0035260774 scopus 로고    scopus 로고
    • Dancing to the tune of chemokines
    • Thelen, M. 2001. Dancing to the tune of chemokines. Nat. Immunol. 2: 129-134.
    • (2001) Nat. Immunol. , vol.2 , pp. 129-134
    • Thelen, M.1
  • 3
    • 0034080318 scopus 로고    scopus 로고
    • The biology of chemokines and their receptors
    • Rossi, D., and A. Zlotnik. 2000. The biology of chemokines and their receptors. Annu. Rev. Immunol. 18: 217-242.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 217-242
    • Rossi, D.1    Zlotnik, A.2
  • 4
    • 3042822267 scopus 로고    scopus 로고
    • Cancer and the chemokine network
    • Balkwill, F. 2004. Cancer and the chemokine network. Nat. Rev. Cancer 4: 540-550.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 540-550
    • Balkwill, F.1
  • 7
    • 0037377728 scopus 로고    scopus 로고
    • Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1α, macrophage inflammatory protein-1β, and SLC that are expressed in human breast cancer
    • Wolf, M., I. Clark-Lewis, C. Buri, H. Langen, M. Lis, and L. Mazzucchelli. 2003. Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1α, macrophage inflammatory protein-1β, and SLC that are expressed in human breast cancer. Am. J. Pathol. 162: 1183-1190.
    • (2003) Am. J. Pathol. , vol.162 , pp. 1183-1190
    • Wolf, M.1    Clark-Lewis, I.2    Buri, C.3    Langen, H.4    Lis, M.5    Mazzucchelli, L.6
  • 8
    • 0033547791 scopus 로고    scopus 로고
    • Amino-terminal processing of chemokine ENA-78 regulates biological activity
    • Nufer, O., M. Corbett, and A. Walz. 1999. Amino-terminal processing of chemokine ENA-78 regulates biological activity. Biochemistry 38: 636-642.
    • (1999) Biochemistry , vol.38 , pp. 636-642
    • Nufer, O.1    Corbett, M.2    Walz, A.3
  • 9
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines, M., M. Wolf, A. Walz, and M. Baggiolini. 1994. Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett. 352: 231-235.
    • (1994) FEBS Lett. , vol.352 , pp. 231-235
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 10
    • 0041620473 scopus 로고    scopus 로고
    • Identification of interleukin-8 converting enzyme as cathepsin L
    • Ohashi, K., M. Naruto, T. Nakaki, and E. Sano. 2003. Identification of interleukin-8 converting enzyme as cathepsin L. Biochim. Biophys. Acta 1649: 30-39.
    • (2003) Biochim. Biophys. Acta , vol.1649 , pp. 30-39
    • Ohashi, K.1    Naruto, M.2    Nakaki, T.3    Sano, E.4
  • 11
    • 0025728640 scopus 로고
    • Formation of neutrophil-activating peptide 2 from platelet-derived connective-tissue-activating peptide III by different tissue proteinases
    • Car, B. D., M. Baggiolini, and A. Walz. 1991. Formation of neutrophil-activating peptide 2 from platelet-derived connective-tissue- activating peptide III by different tissue proteinases. Biochem. J. 275: 581-584.
    • (1991) Biochem. J. , vol.275 , pp. 581-584
    • Car, B.D.1    Baggiolini, M.2    Walz, A.3
  • 15
    • 0034682885 scopus 로고    scopus 로고
    • Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3
    • McQuibban, G. A., J. H. Gong, E. M. Tam, C. A. McCulloch, I. Clark-Lewis, and C. M. Overall. 2000. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289: 1202-1206.
    • (2000) Science , vol.289 , pp. 1202-1206
    • McQuibban, G.A.1    Gong, J.H.2    Tam, E.M.3    McCulloch, C.A.4    Clark-Lewis, I.5    Overall, C.M.6
  • 17
    • 0029966513 scopus 로고    scopus 로고
    • Cathepsin D and breast cancer
    • Westley, B. R., and F. E. May. 1996. Cathepsin D and breast cancer. Eur. J. Cancer 32A: 15-24.
    • (1996) Eur. J. Cancer , vol.32 , pp. 15-24
    • Westley, B.R.1    May, F.E.2
  • 19
    • 0032903046 scopus 로고    scopus 로고
    • Prognostic classification of malignant melanomas by combining clinical, histological, and immunohistochemical parameters
    • Otto, F. J., T. Goldmann, B. Biess, A. Lippold, L. Suter, and U. Westhoff. 1999. Prognostic classification of malignant melanomas by combining clinical, histological, and immunohistochemical parameters. Oncology 56: 208-214.
    • (1999) Oncology , vol.56 , pp. 208-214
    • Otto, F.J.1    Goldmann, T.2    Biess, B.3    Lippold, A.4    Suter, L.5    Westhoff, U.6
  • 20
    • 15644369239 scopus 로고    scopus 로고
    • Molecular cloning of a novel human CC chemokine liver and activation-regulated chemokine (LARC) expressed in liver: Chemotactic activity for lymphocytes and gene localization on chromosome 2
    • Hieshima, K., T. Imai, G. Opdenakker, J. Van Damme, J. Kusuda, H. Tei, Y. Sakaki, K. Takatsuki, R. Miura, O. Yoshie, and H. Nomiyama. 1997. Molecular cloning of a novel human CC chemokine liver and activation-regulated chemokine (LARC) expressed in liver: chemotactic activity for lymphocytes and gene localization on chromosome 2. J. Biol. Chem. 272: 5846-5853.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5846-5853
    • Hieshima, K.1    Imai, T.2    Opdenakker, G.3    Van Damme, J.4    Kusuda, J.5    Tei, H.6    Sakaki, Y.7    Takatsuki, K.8    Miura, R.9    Yoshie, O.10    Nomiyama, H.11
  • 21
    • 0033373334 scopus 로고    scopus 로고
    • Macrophage inflammatory protein 3α is involved in the constitutive trafficking of epidermal Langerhans cells
    • Charbonnier, A. S., N. Kohrgruber, E. Kriehuber, G. Stingl, A. Rot, and D. Maurer. 1999. Macrophage inflammatory protein 3α is involved in the constitutive trafficking of epidermal Langerhans cells. J. Exp. Med. 190: 1755-1768.
    • (1999) J. Exp. Med. , vol.190 , pp. 1755-1768
    • Charbonnier, A.S.1    Kohrgruber, N.2    Kriehuber, E.3    Stingl, G.4    Rot, A.5    Maurer, D.6
  • 22
    • 0033065118 scopus 로고    scopus 로고
    • Selective expression of liver and activation-regulated chemokine (LARC) in intestinal epithelium in mice and humans
    • Tanaka, Y., T. Imai, M. Baba, I. Ishikawa, M. Uehira, H. Nomiyama, and O. Yoshie. 1999. Selective expression of liver and activation-regulated chemokine (LARC) in intestinal epithelium in mice and humans. Eur. J. Immunol. 29: 633-642.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 633-642
    • Tanaka, Y.1    Imai, T.2    Baba, M.3    Ishikawa, I.4    Uehira, M.5    Nomiyama, H.6    Yoshie, O.7
  • 23
    • 0034678392 scopus 로고    scopus 로고
    • Localization of distinct Peyer's patch dendritic cell subsets and their recruitment by chemokines macrophage inflammatory protein (MIP)-3α, MIP-3β, and secondary lymphoid organ chemokine
    • Iwasaki, A., and B. L. Kelsall. 2000. Localization of distinct Peyer's patch dendritic cell subsets and their recruitment by chemokines macrophage inflammatory protein (MIP)-3α, MIP-3β, and secondary lymphoid organ chemokine. J. Exp. Med. 191: 1381-1394.
    • (2000) J. Exp. Med. , vol.191 , pp. 1381-1394
    • Iwasaki, A.1    Kelsall, B.L.2
  • 27
    • 0031593822 scopus 로고    scopus 로고
    • MIP-3α, MIP-3β and fractalkine induce the locomotion and the mobilization of intracellular calcium, and activate the heterotrimeric G proteins in human natural killer cells
    • Al-Aoukaty, A., B. Rolstad, A. Giaid, and A. A. Maghazachi. 1998. MIP-3α, MIP-3β and fractalkine induce the locomotion and the mobilization of intracellular calcium, and activate the heterotrimeric G proteins in human natural killer cells. Immunology 95: 618-624.
    • (1998) Immunology , vol.95 , pp. 618-624
    • Al-Aoukaty, A.1    Rolstad, B.2    Giaid, A.3    Maghazachi, A.A.4
  • 30
    • 0032954129 scopus 로고    scopus 로고
    • CC-chemokine receptor 6 is expressed on diverse memory subsets of T cells and determines responsiveness to macrophage inflammatory protein 3α
    • Liao, F., R. L. Rabin, C. S. Smith, G. Sharma, T. B. Nutman, and J. M. Farber. 1999. CC-chemokine receptor 6 is expressed on diverse memory subsets of T cells and determines responsiveness to macrophage inflammatory protein 3α. J. Immunol. 162: 186-194.
    • (1999) J. Immunol. , vol.162 , pp. 186-194
    • Liao, F.1    Rabin, R.L.2    Smith, C.S.3    Sharma, G.4    Nutman, T.B.5    Farber, J.M.6
  • 31
    • 0037093850 scopus 로고    scopus 로고
    • Human B cells become highly responsive to macrophage-inflammatory protein-3α/CC chemokine ligand-20 after cellular activation without changes in CCR6 expression or ligand binding
    • Liao, F., A. K. Shirakawa, J. F. Foley, R. L. Rabin, and J. M. Farber. 2002. Human B cells become highly responsive to macrophage-inflammatory protein-3α/CC chemokine ligand-20 after cellular activation without changes in CCR6 expression or ligand binding. J. Immunol. 168: 4871-4880.
    • (2002) J. Immunol. , vol.168 , pp. 4871-4880
    • Liao, F.1    Shirakawa, A.K.2    Foley, J.F.3    Rabin, R.L.4    Farber, J.M.5
  • 32
    • 0031066574 scopus 로고    scopus 로고
    • Identification through bioinformatics of two new macrophage proinflammatory human chemokines: MIP-3α and MIP-3β
    • Rossi, D. L., A. P. Vicari, K. Franz-Bacon, T. K. McClanahan, and A. Zlotnik. 1997. Identification through bioinformatics of two new macrophage proinflammatory human chemokines: MIP-3α and MIP-3β. J. immunol. 158: 1033-1036.
    • (1997) J. Immunol. , vol.158 , pp. 1033-1036
    • Rossi, D.L.1    Vicari, A.P.2    Franz-Bacon, K.3    McClanahan, T.K.4    Zlotnik, A.5
  • 33
    • 0036782530 scopus 로고    scopus 로고
    • Expression of lymphocyte-specific chemokines in human malignant glioma: Essential role of LARC in cellular immunity of malignant glioma
    • Kimura, T., H. Takeshima, N. Nomiyama, T. Nishi, T. Kino, M. Kochi, J. I. Kuratsu, and Y. Ushio. 2002. Expression of lymphocyte-specific chemokines in human malignant glioma: essential role of LARC in cellular immunity of malignant glioma. Int. J. Oncol. 21: 707-715.
    • (2002) Int. J. Oncol. , vol.21 , pp. 707-715
    • Kimura, T.1    Takeshima, H.2    Nomiyama, N.3    Nishi, T.4    Kino, T.5    Kochi, M.6    Kuratsu, J.I.7    Ushio, Y.8
  • 34
    • 0030629978 scopus 로고    scopus 로고
    • Chemical synthesis, purification, and folding of C-X-C and C-C chemokines
    • Clark-Lewis, I., L. Vo, P. Owen, and J. Anderson. 1997. Chemical synthesis, purification, and folding of C-X-C and C-C chemokines. Methods Enzymol. 287: 233-250.
    • (1997) Methods Enzymol. , vol.287 , pp. 233-250
    • Clark-Lewis, I.1    Vo, L.2    Owen, P.3    Anderson, J.4
  • 36
    • 0022969510 scopus 로고
    • Ion channels in human neutrophils activated by a rise in free cytosolic calcium concentration
    • von Tscharner, V., B. Prod'hom, M. Baggiolini, and H. Reuter. 1986. Ion channels in human neutrophils activated by a rise in free cytosolic calcium concentration. Nature 324: 369-372.
    • (1986) Nature , vol.324 , pp. 369-372
    • Von Tscharner, V.1    Prod'hom, B.2    Baggiolini, M.3    Reuter, H.4
  • 37
    • 0036547965 scopus 로고    scopus 로고
    • Fibroblasts capture cathepsin D secreted by breast cancer cells: Possible role in the regulation of the invasive process
    • Heylen, N., L. M. Vincent, V. Devos, V. Dubois, C. Remade, and A. Trauet. 2002. Fibroblasts capture cathepsin D secreted by breast cancer cells: possible role in the regulation of the invasive process. Int. J. Oncol. 20: 761-767.
    • (2002) Int. J. Oncol. , vol.20 , pp. 761-767
    • Heylen, N.1    Vincent, L.M.2    Devos, V.3    Dubois, V.4    Remade, C.5    Trauet, A.6
  • 38
    • 0037177886 scopus 로고    scopus 로고
    • Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-βL a process initiated by the exocytosis of cathepsin B
    • Guo, M., P. A. Mathieu, B. Linebaugh, B. F. Sloane, and J. J. Reiners, Jr. 2002. Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-βL a process initiated by the exocytosis of cathepsin B. J. Biol. Chem. 277: 14829-14837.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14829-14837
    • Guo, M.1    Mathieu, P.A.2    Linebaugh, B.3    Sloane, B.F.4    Reiners Jr., J.J.5
  • 39
    • 0034606348 scopus 로고    scopus 로고
    • CXC chemokine receptor 5 expression defines follicular homing T cells with B cell helper function
    • Schaerli, P., K. Willimann, A. B. Lang, M. Lipp, P. Loetscher, and B. Moser. 2000. CXC chemokine receptor 5 expression defines follicular homing T cells with B cell helper function. J. Exp. Med. 192: 1553-1562.
    • (2000) J. Exp. Med. , vol.192 , pp. 1553-1562
    • Schaerli, P.1    Willimann, K.2    Lang, A.B.3    Lipp, M.4    Loetscher, P.5    Moser, B.6
  • 40
    • 0037020263 scopus 로고    scopus 로고
    • The structure of human macrophage inflammatory protein-3α/CCL20: Linking antimicrobial and CC chemokine receptor-6-binding activities with human β-defensins
    • Hoover, D. M., C. Boulegue, D. Yang, J. J. Oppenheim, K. Tucker, W. Lu, and J. Lubkowski. 2002. The structure of human macrophage inflammatory protein-3α/CCL20: linking antimicrobial and CC chemokine receptor-6-binding activities with human β-defensins. J. Biol. Chem. 277: 37647-37654.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37647-37654
    • Hoover, D.M.1    Boulegue, C.2    Yang, D.3    Oppenheim, J.J.4    Tucker, K.5    Lu, W.6    Lubkowski, J.7
  • 41
    • 0036547277 scopus 로고    scopus 로고
    • Expression of the C-C chemokine MIP-3α/CCL20 in human epidermis with impaired permeability barrier function
    • Schmuth, M., S. Neyer, C. Rainer, A. Grassegger, P. Fritsch, N. Romani, and C. Heufler. 2002. Expression of the C-C chemokine MIP-3α/CCL20 in human epidermis with impaired permeability barrier function. Exp. Dermatol. 11: 135-142.
    • (2002) Exp. Dermatol. , vol.11 , pp. 135-142
    • Schmuth, M.1    Neyer, S.2    Rainer, C.3    Grassegger, A.4    Fritsch, P.5    Romani, N.6    Heufler, C.7
  • 43
    • 0033613247 scopus 로고    scopus 로고
    • Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses
    • Kuschert, G. S., F. Coulin, C. A. Power, A. E. Proudfoot, R. E. Hubbard, A. J. Hoogewerf, and T. N. Wells. 1999. Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses. Biochemistry 38: 12959-12968.
    • (1999) Biochemistry , vol.38 , pp. 12959-12968
    • Kuschert, G.S.1    Coulin, F.2    Power, C.A.3    Proudfoot, A.E.4    Hubbard, R.E.5    Hoogewerf, A.J.6    Wells, T.N.7
  • 44
    • 0037621716 scopus 로고    scopus 로고
    • Proteoglycans are potent modulators of the biological responses of eosinophils to chemokines
    • Culley, F. J., E. J. Fadlon, A. Kirchem, T. J. Williams, P. J. Jose, and J. E. Pease. 2003. Proteoglycans are potent modulators of the biological responses of eosinophils to chemokines. Eur. J. Immunol. 33: 1302-1310.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 1302-1310
    • Culley, F.J.1    Fadlon, E.J.2    Kirchem, A.3    Williams, T.J.4    Jose, P.J.5    Pease, J.E.6
  • 45
    • 2342444114 scopus 로고    scopus 로고
    • Post-translational and cell type-specific regulation of CXCR4 expression by cytokines
    • Bruhl, H., C. D. Cohen, S. Linder, M. Kretzler, D. Schlondorff, and M. Mack. 2003. Post-translational and cell type-specific regulation of CXCR4 expression by cytokines. Eur. J. Immunol. 33: 3028-3037.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 3028-3037
    • Bruhl, H.1    Cohen, C.D.2    Linder, S.3    Kretzler, M.4    Schlondorff, D.5    Mack, M.6
  • 46
    • 0343340434 scopus 로고    scopus 로고
    • Cathepsin B, a prognostic indicator in lymph node-negative breast carcinoma patients: Comparison with cathepsin D, cathepsin L, and other clinical indicators
    • Lah, T. T., M. Cercek, A. Blejec, J. Kos, E. Gorodetsky, R. Somers, and I. Daskal. 2000. Cathepsin B, a prognostic indicator in lymph node-negative breast carcinoma patients: comparison with cathepsin D, cathepsin L, and other clinical indicators. Clin. Cancer Res. 6: 578-584.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 578-584
    • Lah, T.T.1    Cercek, M.2    Blejec, A.3    Kos, J.4    Gorodetsky, E.5    Somers, R.6    Daskal, I.7
  • 47
    • 0034128337 scopus 로고    scopus 로고
    • Cysteine proteinases and their inhibitors in extracellular fluids: Markers for diagnosis and prognosis in cancer
    • Kos, J., B. Werle, T. Lah, and N. Brunner. 2000. Cysteine proteinases and their inhibitors in extracellular fluids: markers for diagnosis and prognosis in cancer. Int. J. Biol. Markers 15: 84-89.
    • (2000) Int. J. Biol. Markers , vol.15 , pp. 84-89
    • Kos, J.1    Werle, B.2    Lah, T.3    Brunner, N.4
  • 48
    • 0028952217 scopus 로고
    • Limited and defined truncation at the C terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2): Comparison of native and recombinant NAP-2 variants
    • Ehlert, J. E., F. Petersen, M. H. Kubbutat, J. Gerdes, H. D. Flad, and E. Brandt. 1995. Limited and defined truncation at the C terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2): comparison of native and recombinant NAP-2 variants. J. Biol. Chem. 270: 6338-6344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6338-6344
    • Ehlert, J.E.1    Petersen, F.2    Kubbutat, M.H.3    Gerdes, J.4    Flad, H.D.5    Brandt, E.6
  • 49
    • 0032211132 scopus 로고    scopus 로고
    • Novel C-terminally truncated isoforms of the CXC chemokine β-thromboglobulin and their impact on neutrophil functions
    • Ehlert, J. E., J. Gerdes, H. D. Flad, and E. Brandt. 1998. Novel C-terminally truncated isoforms of the CXC chemokine β-thromboglobulin and their impact on neutrophil functions. J. Immunol. 161: 4975-4982.
    • (1998) J. Immunol. , vol.161 , pp. 4975-4982
    • Ehlert, J.E.1    Gerdes, J.2    Flad, H.D.3    Brandt, E.4
  • 51
    • 0034667898 scopus 로고    scopus 로고
    • Regulated production and molecular diversity of human liver and activation-regulated chemokine/macrophage inflammatory protein-3α from normal and transformed cells
    • Schutyser, E., S. Struyf, P. Menten, J. P. Lenaerts, R. Conings, W. Put, A. Wuyts, P. Proost, and J. Van Damme. 2000. Regulated production and molecular diversity of human liver and activation-regulated chemokine/macrophage inflammatory protein-3α from normal and transformed cells. J. Immunol. 165: 4470-4477.
    • (2000) J. Immunol. , vol.165 , pp. 4470-4477
    • Schutyser, E.1    Struyf, S.2    Menten, P.3    Lenaerts, J.P.4    Conings, R.5    Put, W.6    Wuyts, A.7    Proost, P.8    Van Damme, J.9
  • 52
    • 0024379967 scopus 로고
    • Acid pH in tumors and its potential for therapeutic exploitation
    • Tannock, I. F., and D. Rotin. 1989. Acid pH in tumors and its potential for therapeutic exploitation. Cancer Res. 49: 4373-4384.
    • (1989) Cancer Res. , vol.49 , pp. 4373-4384
    • Tannock, I.F.1    Rotin, D.2
  • 53
    • 0023665211 scopus 로고
    • Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B
    • Polgar, L., and C. Csoma. 1987. Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B. J. Biol. Chem. 262: 14448-14453.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14448-14453
    • Polgar, L.1    Csoma, C.2
  • 54
    • 6344284808 scopus 로고    scopus 로고
    • Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV
    • Sadir, R., A. Imberty, F. Baleux, and H. Lortat-Jacob. 2004. Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV. J. Biol. Chem. 279: 43854-43860.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43854-43860
    • Sadir, R.1    Imberty, A.2    Baleux, F.3    Lortat-Jacob, H.4
  • 57
    • 0027509103 scopus 로고
    • T-cell adhesion induced by proteoglycan-immobilized cytokine MIP-1β
    • Tanaka, Y., D. H. Adams, S. Hubscher, H. Hirano, U. Siebenlist, and S. Shaw. 1993. T-cell adhesion induced by proteoglycan-immobilized cytokine MIP-1β. Nature 361: 79-82.
    • (1993) Nature , vol.361 , pp. 79-82
    • Tanaka, Y.1    Adams, D.H.2    Hubscher, S.3    Hirano, H.4    Siebenlist, U.5    Shaw, S.6
  • 58
    • 10544237272 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan on leukemic cells is primarily involved in integrin triggering and its mediated adhesion to endothelial cells
    • Tanaka, Y., K. Kimata, A. Wake, S. Mine, I. Morimoto, N. Yamakawa, H. Habuchi, S. Ashikari, H. Yamamoto, K. Sakurai, et al. 1996. Heparan sulfate proteoglycan on leukemic cells is primarily involved in integrin triggering and its mediated adhesion to endothelial cells. J. Exp. Med. 184: 1987-1997.
    • (1996) J. Exp. Med. , vol.184 , pp. 1987-1997
    • Tanaka, Y.1    Kimata, K.2    Wake, A.3    Mine, S.4    Morimoto, I.5    Yamakawa, N.6    Habuchi, H.7    Ashikari, S.8    Yamamoto, H.9    Sakurai, K.10
  • 59
    • 85039323193 scopus 로고    scopus 로고
    • J. Exp. Med. Vol. 176 No. 11
    • J. Exp. Med. , vol.176 , pp. 11


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