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Volumn 35, Issue 6, 2007, Pages 947-956

Adiponectin binds to chemokines via the globular head and modulates interactions between chemokines and heparan sulfates

Author keywords

[No Author keywords available]

Indexed keywords

ADIPONECTIN; CHEMOKINE; HEPARAN SULFATE; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; MONOCYTE CHEMOTACTIC PROTEIN 1; PROTEIN CCF 18; RANTES; STROMAL CELL DERIVED FACTOR 1; UNCLASSIFIED DRUG;

EID: 34249031836     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exphem.2007.03.010     Document Type: Article
Times cited : (42)

References (32)
  • 1
    • 0033515761 scopus 로고    scopus 로고
    • Paradoxical decrease of an adipose-specific protein, adiponectin, in obesity
    • Arita Y., Kihara S., Ouchi N., et al. Paradoxical decrease of an adipose-specific protein, adiponectin, in obesity. Biochem Biophys Res Commun 257 (1999) 79-83
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 79-83
    • Arita, Y.1    Kihara, S.2    Ouchi, N.3
  • 2
    • 0029980285 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)
    • Maeda K., Okubo K., Shimomura I., Funahashi T., Matsuzawa Y., and Matsubara K. cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1). Biochem Biophys Res Commun 221 (1996) 286-289
    • (1996) Biochem Biophys Res Commun , vol.221 , pp. 286-289
    • Maeda, K.1    Okubo, K.2    Shimomura, I.3    Funahashi, T.4    Matsuzawa, Y.5    Matsubara, K.6
  • 3
    • 0032510463 scopus 로고    scopus 로고
    • The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor
    • Shapiro L., and Scherer P.E. The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr Biol 8 (1998) 335-338
    • (1998) Curr Biol , vol.8 , pp. 335-338
    • Shapiro, L.1    Scherer, P.E.2
  • 4
    • 0034096988 scopus 로고    scopus 로고
    • Plasma concentrations of a novel, adipose-specific protein, adiponectin, in type2 diabetic patients
    • Hotta K., Funahashi T., Arita Y., et al. Plasma concentrations of a novel, adipose-specific protein, adiponectin, in type2 diabetic patients. Arterioscler Thromb Vasc Biol 20 (2000) 1595-1599
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1595-1599
    • Hotta, K.1    Funahashi, T.2    Arita, Y.3
  • 5
    • 0033613545 scopus 로고    scopus 로고
    • Novel modulator for endothelial adhesion molecules
    • Ouchi N., Kihara S., Arita Y., et al. Novel modulator for endothelial adhesion molecules. Circulation 100 (1999) 2473-2476
    • (1999) Circulation , vol.100 , pp. 2473-2476
    • Ouchi, N.1    Kihara, S.2    Arita, Y.3
  • 6
    • 0036063777 scopus 로고    scopus 로고
    • Diet-induced insulin resistance in mice lacking adiponectin/ACRP30
    • Maeda N., Shimomura I., Kishida K., et al. Diet-induced insulin resistance in mice lacking adiponectin/ACRP30. Nat Med 8 (2002) 731-737
    • (2002) Nat Med , vol.8 , pp. 731-737
    • Maeda, N.1    Shimomura, I.2    Kishida, K.3
  • 7
    • 0037020170 scopus 로고    scopus 로고
    • Role of adiponectin in preventing vascular stenosis. The missing link of adipo-vascular axis
    • Matsuda M., Shimomura I., Sata M., et al. Role of adiponectin in preventing vascular stenosis. The missing link of adipo-vascular axis. J Biol Chem 277 (2002) 37487-37491
    • (2002) J Biol Chem , vol.277 , pp. 37487-37491
    • Matsuda, M.1    Shimomura, I.2    Sata, M.3
  • 8
    • 0037180472 scopus 로고    scopus 로고
    • Adiponectin reduces atherosclerosis in apolipoprotein E-deficient mice
    • Okamoto Y., Kihara S., Ouchi N., et al. Adiponectin reduces atherosclerosis in apolipoprotein E-deficient mice. Circulation 106 (2002) 2767-2770
    • (2002) Circulation , vol.106 , pp. 2767-2770
    • Okamoto, Y.1    Kihara, S.2    Ouchi, N.3
  • 9
    • 0034284038 scopus 로고    scopus 로고
    • Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages
    • Yokota T., Oritani K., Takahashi I., et al. Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages. Blood 96 (2000) 1723-1732
    • (2000) Blood , vol.96 , pp. 1723-1732
    • Yokota, T.1    Oritani, K.2    Takahashi, I.3
  • 10
    • 10744223271 scopus 로고    scopus 로고
    • Adiponectin, a fat cell product, influences the earliest lymphocyte precursors in bone marrow cultures by activation of the cyclooxygenase-prostaglandin pathway in stromal cells
    • Yokota T., Meka C.S.R., Kouro T., et al. Adiponectin, a fat cell product, influences the earliest lymphocyte precursors in bone marrow cultures by activation of the cyclooxygenase-prostaglandin pathway in stromal cells. J Immunol 171 (2003) 5091-5099
    • (2003) J Immunol , vol.171 , pp. 5091-5099
    • Yokota, T.1    Meka, C.S.R.2    Kouro, T.3
  • 11
    • 0037494960 scopus 로고    scopus 로고
    • Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
    • Yamauchi T., Kamon J., Ito Y., et al. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 423 (2003) 762-769
    • (2003) Nature , vol.423 , pp. 762-769
    • Yamauchi, T.1    Kamon, J.2    Ito, Y.3
  • 12
    • 24044538551 scopus 로고    scopus 로고
    • Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner
    • Wang Y., Lam K.S.L., Xu J.Y., et al. Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner. J Biol Chem 280 (2005) 18341-18347
    • (2005) J Biol Chem , vol.280 , pp. 18341-18347
    • Wang, Y.1    Lam, K.S.L.2    Xu, J.Y.3
  • 13
    • 3142761477 scopus 로고    scopus 로고
    • T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin
    • Hug C., Wang J., Ahmad N.S., Bogan J.S., Tsao T.S., and Lodish H.F. T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin. Proc Natl Acad Sci 101 (2004) 10308-10313
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 10308-10313
    • Hug, C.1    Wang, J.2    Ahmad, N.S.3    Bogan, J.S.4    Tsao, T.S.5    Lodish, H.F.6
  • 14
    • 0029739948 scopus 로고    scopus 로고
    • Identification of stromal cell products that interact with Pre-B cells
    • Oritani K., and Kincade P.W. Identification of stromal cell products that interact with Pre-B cells. J Cell Biol 134 (1996) 771-782
    • (1996) J Cell Biol , vol.134 , pp. 771-782
    • Oritani, K.1    Kincade, P.W.2
  • 15
    • 0028324454 scopus 로고
    • Molecular cloning and structure of a pre-B-cell growth-stimulating factor
    • Nagasawa T., Kikutani H., and Kishimoto T. Molecular cloning and structure of a pre-B-cell growth-stimulating factor. Proc Natl Acad Sci USA 91 (1994) 2305-2309
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2305-2309
    • Nagasawa, T.1    Kikutani, H.2    Kishimoto, T.3
  • 16
    • 0028784508 scopus 로고
    • Molecular cloning and functional characterization of a novel member of the C-C chemokine family
    • Hara T., Bacon K.B., Cho L.C., et al. Molecular cloning and functional characterization of a novel member of the C-C chemokine family. J Immunol 155 (1995) 5352-5358
    • (1995) J Immunol , vol.155 , pp. 5352-5358
    • Hara, T.1    Bacon, K.B.2    Cho, L.C.3
  • 17
    • 0037438505 scopus 로고    scopus 로고
    • Role of the intracellular domains of CXCR4 in SDF-1-mediated signaling
    • Roland J., Murphy B.J., Ahr B., et al. Role of the intracellular domains of CXCR4 in SDF-1-mediated signaling. Blood 101 (2003) 399-406
    • (2003) Blood , vol.101 , pp. 399-406
    • Roland, J.1    Murphy, B.J.2    Ahr, B.3
  • 18
    • 33646863047 scopus 로고    scopus 로고
    • The shedding of syndecan-4 and syndecan-1 from Hela cells and human primary macrophages is accelerated by SDF-1/CXCL12 and mediated by the matrix metalloproteinase-9
    • Brule S., Charnaux N., Sutton A., et al. The shedding of syndecan-4 and syndecan-1 from Hela cells and human primary macrophages is accelerated by SDF-1/CXCL12 and mediated by the matrix metalloproteinase-9. Glycobiology 16 (2006) 488-501
    • (2006) Glycobiology , vol.16 , pp. 488-501
    • Brule, S.1    Charnaux, N.2    Sutton, A.3
  • 19
    • 0034014647 scopus 로고    scopus 로고
    • An adipocyte-derived plasma protein, adiponectin, adheres to injured vascular walls
    • Okamoto Y., Arita Y., Nishida M., et al. An adipocyte-derived plasma protein, adiponectin, adheres to injured vascular walls. Horm Metab Res 32 (2000) 47-50
    • (2000) Horm Metab Res , vol.32 , pp. 47-50
    • Okamoto, Y.1    Arita, Y.2    Nishida, M.3
  • 20
    • 0036105778 scopus 로고    scopus 로고
    • Paracrine regulation of fat cell formation in bone marrow cultures via adiponectin and prostaglandins
    • Yokota T., Meka C.S.R., Medina K.L., et al. Paracrine regulation of fat cell formation in bone marrow cultures via adiponectin and prostaglandins. J Clin Invest 109 (2002) 1303-1310
    • (2002) J Clin Invest , vol.109 , pp. 1303-1310
    • Yokota, T.1    Meka, C.S.R.2    Medina, K.L.3
  • 21
    • 0037452728 scopus 로고    scopus 로고
    • Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines
    • Proudfoot A.E.I., Handel T.M., Johnson Z., et al. Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines. Proc Natl Acad Sci U S A 100 (2003) 1885-1890
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 1885-1890
    • Proudfoot, A.E.I.1    Handel, T.M.2    Johnson, Z.3
  • 22
    • 0031026475 scopus 로고    scopus 로고
    • The chemokine SDF-1 is a chemoattractant for human CD34+ hematopoietic progenitor cells and provides a new mechanism to explain the mobilization of CD34+ progenitors to peripheral blood
    • Aiuti A., Webb I.J., Bleul C., et al. The chemokine SDF-1 is a chemoattractant for human CD34+ hematopoietic progenitor cells and provides a new mechanism to explain the mobilization of CD34+ progenitors to peripheral blood. J Exp Med 185 (1997) 111-120
    • (1997) J Exp Med , vol.185 , pp. 111-120
    • Aiuti, A.1    Webb, I.J.2    Bleul, C.3
  • 23
    • 0030683638 scopus 로고    scopus 로고
    • Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1
    • Crump M.P., Gong J.H., Loetscher P., et al. Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1. EMBO J 16 (1997) 6996-7007
    • (1997) EMBO J , vol.16 , pp. 6996-7007
    • Crump, M.P.1    Gong, J.H.2    Loetscher, P.3
  • 24
    • 0033588220 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1 alpha associates with heparan sulfates through the first beta-strand of the chemokine
    • Amara A., Lorthioir O., Valenzuela A., et al. Stromal cell-derived factor-1 alpha associates with heparan sulfates through the first beta-strand of the chemokine. J Biol Chem 274 (1999) 23916-23925
    • (1999) J Biol Chem , vol.274 , pp. 23916-23925
    • Amara, A.1    Lorthioir, O.2    Valenzuela, A.3
  • 25
    • 2542498611 scopus 로고    scopus 로고
    • Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo
    • Lau E.K., Paavola C.D., Johnson Z., et al. Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo. J Biol Chem 279 (2004) 22294-22305
    • (2004) J Biol Chem , vol.279 , pp. 22294-22305
    • Lau, E.K.1    Paavola, C.D.2    Johnson, Z.3
  • 26
    • 0032491615 scopus 로고    scopus 로고
    • Lysine 58 and histidine 66 at the C-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding
    • Chakravarty L., Rogers L., Quach T., Breckenridge S., and Kolattukudy P.E. Lysine 58 and histidine 66 at the C-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding. J Biol Chem 273 (1998) 29641-29647
    • (1998) J Biol Chem , vol.273 , pp. 29641-29647
    • Chakravarty, L.1    Rogers, L.2    Quach, T.3    Breckenridge, S.4    Kolattukudy, P.E.5
  • 27
    • 0030892080 scopus 로고    scopus 로고
    • Identification of a glycosaminoglycan-binding site in chemokine macrophage inflammatory protein-1 alpha
    • Koopmann W., and Krangel M.S. Identification of a glycosaminoglycan-binding site in chemokine macrophage inflammatory protein-1 alpha. J Biol Chem 272 (1997) 10103-10109
    • (1997) J Biol Chem , vol.272 , pp. 10103-10109
    • Koopmann, W.1    Krangel, M.S.2
  • 28
    • 0030810177 scopus 로고    scopus 로고
    • Glycosaminoglycans mediate cell surface oligomerization of chemokines
    • Hoogewerf A.J., Kuschert G.S.V., Proudfoot A.E.I., et al. Glycosaminoglycans mediate cell surface oligomerization of chemokines. Biochemistry 36 (1997) 13570-13578
    • (1997) Biochemistry , vol.36 , pp. 13570-13578
    • Hoogewerf, A.J.1    Kuschert, G.S.V.2    Proudfoot, A.E.I.3
  • 29
    • 0034641647 scopus 로고    scopus 로고
    • Adiponectin, an-adipocyte-derived plasma protein, inhibits endothelial NF-kB signaling through a cAMP-dependent pathway
    • Ouchi N., Kihara S., Arita Y., et al. Adiponectin, an-adipocyte-derived plasma protein, inhibits endothelial NF-kB signaling through a cAMP-dependent pathway. Circulation 102 (2000) 1296-1301
    • (2000) Circulation , vol.102 , pp. 1296-1301
    • Ouchi, N.1    Kihara, S.2    Arita, Y.3
  • 30
    • 2442464884 scopus 로고    scopus 로고
    • Adiponectin specifically increased tissue inhibitor of matelloproteinase-1 through interleukin-10 expression in human macrophages
    • Kumada M., Kihara S., Ouchi N., et al. Adiponectin specifically increased tissue inhibitor of matelloproteinase-1 through interleukin-10 expression in human macrophages. Circulation 109 (2004) 2046-2049
    • (2004) Circulation , vol.109 , pp. 2046-2049
    • Kumada, M.1    Kihara, S.2    Ouchi, N.3
  • 31
    • 0037432152 scopus 로고    scopus 로고
    • Reciprocal association of C-reactive protein with adiponectin in blood stream and adipose tissue
    • Ouchi N., Kihara S., Funahashi T., et al. Reciprocal association of C-reactive protein with adiponectin in blood stream and adipose tissue. Circulation 107 (2003) 671-674
    • (2003) Circulation , vol.107 , pp. 671-674
    • Ouchi, N.1    Kihara, S.2    Funahashi, T.3
  • 32
    • 12244301213 scopus 로고    scopus 로고
    • Changes in the distribution pattern of gelatin-binding protein of 28 kDa (adiponectin) in myocardial remodelling after ischaemic injury
    • Ishikawa Y., Akasaka Y., Ishii T., et al. Changes in the distribution pattern of gelatin-binding protein of 28 kDa (adiponectin) in myocardial remodelling after ischaemic injury. Histopathology 42 (2003) 43-52
    • (2003) Histopathology , vol.42 , pp. 43-52
    • Ishikawa, Y.1    Akasaka, Y.2    Ishii, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.