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Volumn 5, Issue , 2015, Pages

Role of Src in vascular hyperpermeability induced by advanced glycation end products

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ADVANCED GLYCATION END PRODUCT; ADVANCED GLYCATION END PRODUCT RECEPTOR; CADHERIN; LEUKOCYTE ANTIGEN; MOESIN; PROTEIN TYROSINE KINASE; VASCULAR ENDOTHELIAL CADHERIN;

EID: 84941922766     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep14090     Document Type: Article
Times cited : (39)

References (50)
  • 2
    • 4043058031 scopus 로고    scopus 로고
    • Advanced glycation end products and vascular inflammation: Implications for accelerated atherosclerosis in diabetes
    • Basta, G., Schmidt, A. M. & De Caterina, R. Advanced glycation end products and vascular inflammation: implications for accelerated atherosclerosis in diabetes. Cardiovasc Res 63, 582-592 (2004).
    • (2004) Cardiovasc Res , vol.63 , pp. 582-592
    • Basta, G.1    Schmidt, A.M.2    De Caterina, R.3
  • 3
    • 80052269118 scopus 로고    scopus 로고
    • Skin autofluorescence is inversely related to HDL anti-oxidative capacity in type 2 diabetes mellitus
    • Mulder, D. J. et al. Skin autofluorescence is inversely related to HDL anti-oxidative capacity in type 2 diabetes mellitus. Atherosclerosis 218, 102-106 (2011).
    • (2011) Atherosclerosis , vol.218 , pp. 102-106
    • Mulder, D.J.1
  • 4
    • 84859788536 scopus 로고    scopus 로고
    • Methylglyoxal promotes oxidative stress and endothelial dysfunction
    • Sena, C. M. et al. Methylglyoxal promotes oxidative stress and endothelial dysfunction. Pharmacol Res 65, 497-506 (2012).
    • (2012) Pharmacol Res , vol.65 , pp. 497-506
    • Sena, C.M.1
  • 5
    • 0026726769 scopus 로고
    • Receptor-mediated interactions of advanced glycosylation end products with cellular components within diabetic tissues
    • Vlassara, H. Receptor-mediated interactions of advanced glycosylation end products with cellular components within diabetic tissues. Diabetes 41 Suppl 2, 52-56 (1992).
    • (1992) Diabetes , vol.41 , pp. 52-56
    • Vlassara, H.1
  • 6
    • 0032861267 scopus 로고    scopus 로고
    • Acute modulation of albumin microvascular leakage by advanced glycation end products in microcirculation of diabetic rats in vivo
    • Bonnardel-Phu, E., Wautier, J. L., Schmidt, A. M., Avila, C. & Vicaut, E. Acute modulation of albumin microvascular leakage by advanced glycation end products in microcirculation of diabetic rats in vivo. Diabetes 48, 2052-2058 (1999).
    • (1999) Diabetes , vol.48 , pp. 2052-2058
    • Bonnardel-Phu, E.1    Wautier, J.L.2    Schmidt, A.M.3    Avila, C.4    Vicaut, E.5
  • 7
    • 67650079692 scopus 로고    scopus 로고
    • ERM protein moesin is phosphorylated by advanced glycation end products and modulates endothelial permeability
    • Guo, X. et al. ERM protein moesin is phosphorylated by advanced glycation end products and modulates endothelial permeability. Am J Physiol Heart Circ Physiol 297, H238-246 (2009).
    • (2009) Am J Physiol Heart Circ Physiol , vol.297 , pp. H238-246
    • Guo, X.1
  • 8
    • 10744223527 scopus 로고    scopus 로고
    • Randomized trial of an inhibitor of formation of advanced glycation end products in diabetic nephropathy
    • Bolton, W. K. et al. Randomized trial of an inhibitor of formation of advanced glycation end products in diabetic nephropathy. Am J Nephrol 24, 32-40 (2004).
    • (2004) Am J Nephrol , vol.24 , pp. 32-40
    • Bolton, W.K.1
  • 9
    • 57749172257 scopus 로고    scopus 로고
    • Src family kinases as mediators of endothelial permeability: Effects on inflammation and metastasis
    • Kim, M. P., Park, S. I., Kopetz, S. & Gallick, G. E. Src family kinases as mediators of endothelial permeability: effects on inflammation and metastasis. Cell Tissue Res 335, 249-259 (2009).
    • (2009) Cell Tissue Res , vol.335 , pp. 249-259
    • Kim, M.P.1    Park, S.I.2    Kopetz, S.3    Gallick, G.E.4
  • 10
    • 38349124475 scopus 로고    scopus 로고
    • Regulation of endothelial permeability by Src kinase signaling: Vascular leakage versus transcellular transport of drugs and macromolecules
    • Hu, G., Place, A. T. & Minshall, R. D. Regulation of endothelial permeability by Src kinase signaling: vascular leakage versus transcellular transport of drugs and macromolecules. Chem Biol Interact 171, 177-189 (2008).
    • (2008) Chem Biol Interact , vol.171 , pp. 177-189
    • Hu, G.1    Place, A.T.2    Minshall, R.D.3
  • 11
    • 0034008116 scopus 로고    scopus 로고
    • Microcirculatory dysfunction in sepsis: A pathogenetic basis for therapy?
    • Lehr, H. A., Bittinger, F. & Kirkpatrick, C. J. Microcirculatory dysfunction in sepsis: a pathogenetic basis for therapy? J Pathol 190, 373-386 (2000).
    • (2000) J Pathol , vol.190 , pp. 373-386
    • Lehr, H.A.1    Bittinger, F.2    Kirkpatrick, C.J.3
  • 12
    • 0037180812 scopus 로고    scopus 로고
    • Points of control in inflammation
    • Nathan, C. Points of control in inflammation. Nature 420, 846-852 (2002).
    • (2002) Nature , vol.420 , pp. 846-852
    • Nathan, C.1
  • 13
    • 33751264889 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation: Modulation of basal and agonist-stimulated venular permeability
    • Yuan, Y., Huang, Q. & Wu, H. M. Myosin light chain phosphorylation: modulation of basal and agonist-stimulated venular permeability. Am J Physiol 272, H1437-1443 (1997).
    • (1997) Am J Physiol , vol.272 , pp. H1437-1443
    • Yuan, Y.1    Huang, Q.2    Wu, H.M.3
  • 14
    • 84891078821 scopus 로고    scopus 로고
    • A critical role for Lyn kinase in strengthening endothelial integrity and barrier function
    • Han, J. et al. A critical role for Lyn kinase in strengthening endothelial integrity and barrier function. Blood 122, 4140-4149 (2013).
    • (2013) Blood , vol.122 , pp. 4140-4149
    • Han, J.1
  • 15
    • 0036889213 scopus 로고    scopus 로고
    • Src-dependent neutrophil-mediated vascular hyperpermeability and betacatenin modification
    • Tinsley, J. H., Ustinova, E. E., Xu, W. & Yuan, S. Y. Src-dependent, neutrophil-mediated vascular hyperpermeability and betacatenin modification. Am J Physiol Cell Physiol 283, C1745-1751 (2002).
    • (2002) Am J Physiol Cell Physiol , vol.283 , pp. C1745-1751
    • Tinsley, J.H.1    Ustinova, E.E.2    Xu, W.3    Yuan, S.Y.4
  • 16
    • 77951212625 scopus 로고    scopus 로고
    • Src-induced tyrosine phosphorylation of VE-cadherin is not sufficient to decrease barrier function of endothelial monolayers
    • Adam, A. P., Sharenko, A. L., Pumiglia, K. & Vincent, P. A. Src-induced tyrosine phosphorylation of VE-cadherin is not sufficient to decrease barrier function of endothelial monolayers. J Biol Chem 285, 7045-7055 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 7045-7055
    • Adam, A.P.1    Sharenko, A.L.2    Pumiglia, K.3    Vincent, P.A.4
  • 17
    • 84870688010 scopus 로고    scopus 로고
    • Phosphorylation of VE-cadherin is modulated by haemodynamic forces and contributes to the regulation of vascular permeability in vivo
    • Orsenigo, F. et al. Phosphorylation of VE-cadherin is modulated by haemodynamic forces and contributes to the regulation of vascular permeability in vivo. Nat Commun 3, 1208 (2012).
    • (2012) Nat Commun , vol.3 , Issue.1208
    • Orsenigo, F.1
  • 18
    • 84924692264 scopus 로고    scopus 로고
    • Advanced glycation end products induce glomerular endothelial cell hyperpermeability by upregulating matrix metalloproteinase activity
    • Luo, P. et al. Advanced glycation end products induce glomerular endothelial cell hyperpermeability by upregulating matrix metalloproteinase activity. Mol Med Rep 11, 4447-4453 (2015).
    • (2015) Mol Med Rep , vol.11 , pp. 4447-4453
    • Luo, P.1
  • 19
    • 84894031118 scopus 로고    scopus 로고
    • Advanced glycation end products activate the miRNA/RhoA/ROCK2 pathway in endothelial cells
    • Wu, X. D. et al. Advanced glycation end products activate the miRNA/RhoA/ROCK2 pathway in endothelial cells. Microcirculation 21, 178-186 (2014).
    • (2014) Microcirculation , vol.21 , pp. 178-186
    • Wu, X.D.1
  • 20
    • 84860124109 scopus 로고    scopus 로고
    • Advanced glycation end products increase permeability of brain microvascular endothelial cells through reactive oxygen species-induced vascular endothelial growth factor expression
    • Niiya, Y., Abumiya, T., Yamagishi, S., Takino, J. & Takeuchi, M. Advanced glycation end products increase permeability of brain microvascular endothelial cells through reactive oxygen species-induced vascular endothelial growth factor expression. J Stroke Cerebrovasc Dis 21, 293-298 (2012).
    • (2012) J Stroke Cerebrovasc Dis , vol.21 , pp. 293-298
    • Niiya, Y.1    Abumiya, T.2    Yamagishi, S.3    Takino, J.4    Takeuchi, M.5
  • 21
    • 77954660494 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor inhibits advanced glycation end products-induced retinal vascular permeability
    • Sheikpranbabu, S., Haribalaganesh, R., Lee, K. J. & Gurunathan, S. Pigment epithelium-derived factor inhibits advanced glycation end products-induced retinal vascular permeability. Biochimie 92, 1040-1051 (2010).
    • (2010) Biochimie , vol.92 , pp. 1040-1051
    • Sheikpranbabu, S.1    Haribalaganesh, R.2    Lee, K.J.3    Gurunathan, S.4
  • 22
    • 34548397756 scopus 로고    scopus 로고
    • Proteolytic degradation of VE-cadherin alters the blood-retinal barrier in diabetes
    • Navaratna, D., McGuire, P. G., Menicucci, G. & Das, A. Proteolytic degradation of VE-cadherin alters the blood-retinal barrier in diabetes. Diabetes 56, 2380-2387 (2007).
    • (2007) Diabetes , vol.56 , pp. 2380-2387
    • Navaratna, D.1    McGuire, P.G.2    Menicucci, G.3    Das, A.4
  • 23
    • 33746019939 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor inhibits advanced glycation end product-induced retinal vascular hyperpermeability by blocking reactive oxygen species-mediated vascular endothelial growth factor expression
    • Yamagishi, S. et al. Pigment epithelium-derived factor inhibits advanced glycation end product-induced retinal vascular hyperpermeability by blocking reactive oxygen species-mediated vascular endothelial growth factor expression. J Biol Chem 281, 20213-20220 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 20213-20220
    • Yamagishi, S.1
  • 24
    • 33746920337 scopus 로고    scopus 로고
    • Advanced glycation end products: Sparking the development of diabetic vascular injury
    • Goldin, A., Beckman, J. A., Schmidt, A. M. & Creager, M. A. Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation 114, 597-605 (2006).
    • (2006) Circulation , vol.114 , pp. 597-605
    • Goldin, A.1    Beckman, J.A.2    Schmidt, A.M.3    Creager, M.A.4
  • 25
    • 56749185425 scopus 로고    scopus 로고
    • Phosphorylated c-Src in the nucleus is associated with improved patient outcome in ER-positive breast cancer
    • Campbell, E. J. et al. Phosphorylated c-Src in the nucleus is associated with improved patient outcome in ER-positive breast cancer. Br J Cancer 99, 1769-1774 (2008).
    • (2008) Br J Cancer , vol.99 , pp. 1769-1774
    • Campbell, E.J.1
  • 26
    • 33744958085 scopus 로고    scopus 로고
    • Key role of Src kinase in S100B-induced activation of the receptor for advanced glycation end products in vascular smooth muscle cells
    • Reddy, M. A. et al. Key role of Src kinase in S100B-induced activation of the receptor for advanced glycation end products in vascular smooth muscle cells. J Biol Chem 281, 13685-13693 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 13685-13693
    • Reddy, M.A.1
  • 27
    • 61349095437 scopus 로고    scopus 로고
    • In skeletal muscle advanced glycation end products (AGEs) inhibit insulin action and induce the formation of multimolecular complexes including the receptor for AGEs
    • Cassese, A. et al. In skeletal muscle advanced glycation end products (AGEs) inhibit insulin action and induce the formation of multimolecular complexes including the receptor for AGEs. J Biol Chem 283, 36088-36099 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 36088-36099
    • Cassese, A.1
  • 28
    • 0036829918 scopus 로고    scopus 로고
    • STAT5 activation induced by diabetic LDL depends on LDL glycation and occurs via src kinase activity
    • Brizzi, M. F. et al. STAT5 activation induced by diabetic LDL depends on LDL glycation and occurs via src kinase activity. Diabetes 51, 3311-3317 (2002).
    • (2002) Diabetes , vol.51 , pp. 3311-3317
    • Brizzi, M.F.1
  • 29
    • 84861098989 scopus 로고    scopus 로고
    • Formin mDia1 mediates vascular remodeling via integration of oxidative and signal transduction pathways
    • Toure, F. et al. Formin mDia1 mediates vascular remodeling via integration of oxidative and signal transduction pathways. Circ Res 110, 1279-1293 (2012).
    • (2012) Circ Res , vol.110 , pp. 1279-1293
    • Toure, F.1
  • 30
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    • Berryman, M., Franck, Z. & Bretscher, A. Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J Cell Sci 105 (Pt 4), 1025-1043 (1993).
    • (1993) J Cell Sci , vol.105 , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 31
    • 30744433331 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin proteins are phosphorylated by TNF-alpha and modulate permeability increases in human pulmonary microvascular endothelial cells
    • Koss, M. et al. Ezrin/radixin/moesin proteins are phosphorylated by TNF-alpha and modulate permeability increases in human pulmonary microvascular endothelial cells. J Immunol 176, 1218-1227 (2006).
    • (2006) J Immunol , vol.176 , pp. 1218-1227
    • Koss, M.1
  • 32
    • 79960733700 scopus 로고    scopus 로고
    • Ezrin, Radixin and Moesin: Key regulators of membrane-cortex interactions and signaling
    • Neisch, A. L. & Fehon, R. G. Ezrin, Radixin and Moesin: key regulators of membrane-cortex interactions and signaling. Curr Opin Cell Biol 23, 377-382 (2011).
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 377-382
    • Neisch, A.L.1    Fehon, R.G.2
  • 33
    • 39049085828 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin: Versatile controllers of signaling molecules and of the cortical cytoskeleton
    • Niggli, V. & Rossy, J. Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton. Int J Biochem Cell Biol 40, 344-349 (2008).
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 344-349
    • Niggli, V.1    Rossy, J.2
  • 34
    • 84861692366 scopus 로고    scopus 로고
    • Advanced glycation end products induce moesin phosphorylation in murine retinal endothelium
    • Wang, L. et al. Advanced glycation end products induce moesin phosphorylation in murine retinal endothelium. Acta Diabetol 49, 47-55 (2012).
    • (2012) Acta Diabetol , vol.49 , pp. 47-55
    • Wang, L.1
  • 35
    • 84855780092 scopus 로고    scopus 로고
    • RhoA/ROCK-dependent moesin phosphorylation regulates AGE-induced endothelial cellular response
    • Wang, J. et al. RhoA/ROCK-dependent moesin phosphorylation regulates AGE-induced endothelial cellular response. Cardiovasc Diabetol 11, 7 (2012).
    • (2012) Cardiovasc Diabetol , vol.11 , Issue.7
    • Wang, J.1
  • 36
    • 48049094159 scopus 로고    scopus 로고
    • The role of adherens junctions and VE-cadherin in the control of vascular permeability
    • Dejana, E., Orsenigo, F. & Lampugnani, M. G. The role of adherens junctions and VE-cadherin in the control of vascular permeability. J Cell Sci 121, 2115-2122 (2008).
    • (2008) J Cell Sci , vol.121 , pp. 2115-2122
    • Dejana, E.1    Orsenigo, F.2    Lampugnani, M.G.3
  • 37
    • 84901495236 scopus 로고    scopus 로고
    • Endothelial permeability and VE-cadherin: A wacky comradeship
    • Gavard, J. Endothelial permeability and VE-cadherin: a wacky comradeship. Cell Adh Migr 8, 158-164 (2014).
    • (2014) Cell Adh Migr , vol.8 , pp. 158-164
    • Gavard, J.1
  • 38
    • 33750529948 scopus 로고    scopus 로고
    • VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin
    • Gavard, J. & Gutkind, J. S. VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin. Nat Cell Biol 8, 1223-1234 (2006).
    • (2006) Nat Cell Biol , vol.8 , pp. 1223-1234
    • Gavard, J.1    Gutkind, J.S.2
  • 39
    • 84866880821 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of DEP-1/CD148 as a mechanism controlling Src kinase activation, endothelial cell permeability, invasion, and capillary formation
    • Spring, K. et al. Tyrosine phosphorylation of DEP-1/CD148 as a mechanism controlling Src kinase activation, endothelial cell permeability, invasion, and capillary formation. Blood 120, 2745-2756 (2012).
    • (2012) Blood , vol.120 , pp. 2745-2756
    • Spring, K.1
  • 40
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb, M. B., Polte, T. R. & Hanks, S. K. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol Cell Biol 15, 954-963 (1995).
    • (1995) Mol Cell Biol , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 41
    • 1842836011 scopus 로고    scopus 로고
    • Src family kinase activity is required for signal tranducer and activator of transcription 3 and focal adhesion kinase phosphorylation and vascular endothelial growth factor signaling in vivo and for anchorage-dependent and -independent growth of human tumor cells
    • Laird, A. D. et al. Src family kinase activity is required for signal tranducer and activator of transcription 3 and focal adhesion kinase phosphorylation and vascular endothelial growth factor signaling in vivo and for anchorage-dependent and -independent growth of human tumor cells. Mol Cancer Ther 2, 461-469 (2003).
    • (2003) Mol Cancer Ther , vol.2 , pp. 461-469
    • Laird, A.D.1
  • 42
    • 0036544562 scopus 로고    scopus 로고
    • Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling
    • Eliceiri, B. P. et al. Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling. J Cell Biol 157, 149-160 (2002).
    • (2002) J Cell Biol , vol.157 , pp. 149-160
    • Eliceiri, B.P.1
  • 43
    • 33846196709 scopus 로고    scopus 로고
    • Resealing of endothelial junctions by focal adhesion kinase
    • Quadri, S. K. & Bhattacharya, J. Resealing of endothelial junctions by focal adhesion kinase. Am J Physiol Lung Cell Mol Physiol 292, L334-342 (2007).
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.292 , pp. L334-342
    • Quadri, S.K.1    Bhattacharya, J.2
  • 44
    • 82955198454 scopus 로고    scopus 로고
    • Role of FAK in S1P-regulated endothelial permeability
    • Belvitch, P. & Dudek, S. M. Role of FAK in S1P-regulated endothelial permeability. Microvasc Res 83, 22-30 (2012).
    • (2012) Microvasc Res , vol.83 , pp. 22-30
    • Belvitch, P.1    Dudek, S.M.2
  • 45
    • 0037088851 scopus 로고    scopus 로고
    • Modulatory role of focal adhesion kinase in regulating human pulmonary arterial endothelial barrier function
    • Mehta, D. et al. Modulatory role of focal adhesion kinase in regulating human pulmonary arterial endothelial barrier function. J Physiol 539, 779-789 (2002).
    • (2002) J Physiol , vol.539 , pp. 779-789
    • Mehta, D.1
  • 46
    • 84862907457 scopus 로고    scopus 로고
    • VEGF-induced vascular permeability is mediated by FAK
    • Chen, X. L. et al. VEGF-induced vascular permeability is mediated by FAK. Dev Cell 22, 146-157 (2012).
    • (2012) Dev Cell , vol.22 , pp. 146-157
    • Chen, X.L.1
  • 47
    • 77953601228 scopus 로고    scopus 로고
    • Role of kinase-independent and -dependent functions of FAK in endothelial cell survival and barrier function during embryonic development
    • Zhao, X., Peng, X., Sun, S., Park, A. Y. & Guan, J. L. Role of kinase-independent and -dependent functions of FAK in endothelial cell survival and barrier function during embryonic development. J Cell Biol 189, 955-965 (2010).
    • (2010) J Cell Biol , vol.189 , pp. 955-965
    • Zhao, X.1    Peng, X.2    Sun, S.3    Park, A.Y.4    Guan, J.L.5
  • 48
    • 48249117901 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-1-dependent neutrophil adhesion to endothelial cells induces caveolae-mediated pulmonary vascular hyperpermeability
    • Hu, G., Vogel, S. M., Schwartz, D. E., Malik, A. B. & Minshall, R. D. Intercellular adhesion molecule-1-dependent neutrophil adhesion to endothelial cells induces caveolae-mediated pulmonary vascular hyperpermeability. Circ Res 102, e120-131 (2008).
    • (2008) Circ Res , vol.102 , pp. e120-131
    • Hu, G.1    Vogel, S.M.2    Schwartz, D.E.3    Malik, A.B.4    Minshall, R.D.5
  • 49
    • 84923381976 scopus 로고    scopus 로고
    • Heat Stress-Induced Disruption of Endothelial Barrier Function Is via PAR1 Signaling and Suppressed by Xuebijing Injection
    • Xu, Q. et al. Heat Stress-Induced Disruption of Endothelial Barrier Function Is via PAR1 Signaling and Suppressed by Xuebijing Injection. PLoS One 10, e0118057 (2015).
    • (2015) PLoS One , vol.10 , pp. e0118057
    • Xu, Q.1
  • 50
    • 0035091569 scopus 로고    scopus 로고
    • Beta(2)-Microglobulin modified with advanced glycation end products delays monocyte apoptosis
    • Hou, F. F. et al. beta(2)-Microglobulin modified with advanced glycation end products delays monocyte apoptosis. Kidney Int 59, 990-1002 (2001).
    • (2001) Kidney Int , vol.59 , pp. 990-1002
    • Hou, F.F.1


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