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Volumn 1043, Issue , 2005, Pages 637-643

Significance of proximal tubular metabolism of advanced glycation end products in kidney diseases

Author keywords

Advanced glycation end product; Chronic renal failure; Diabetic nephropathy; Megalin; Proximal tubule

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ADVANCED GLYCATION END PRODUCT RECEPTOR; CARBOHYDRATE DERIVATIVE; CARBONYL DERIVATIVE; CARRIER PROTEIN; MEGALIN; PROTEIN; UREMIC TOXIN;

EID: 23744506885     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1196/annals.1333.072     Document Type: Conference Paper
Times cited : (44)

References (38)
  • 1
    • 0035668462 scopus 로고    scopus 로고
    • The AGE-receptor in the pathogenesis of diabetic complications
    • VLASSARA, H. 2001. The AGE-receptor in the pathogenesis of diabetic complications. Diabetes Metab. Res. Rev. 17: 436-443.
    • (2001) Diabetes Metab. Res. Rev. , vol.17 , pp. 436-443
    • Vlassara, H.1
  • 2
    • 0030031177 scopus 로고    scopus 로고
    • Renal fate of circulating advanced glycated end products (AGE): Evidence for reabsorption and catabolism of AGE-peptides by renal proximal tubular cells
    • GUGLIUCCI, A. & M. BENDAYAN. 1996. Renal fate of circulating advanced glycated end products (AGE): evidence for reabsorption and catabolism of AGE-peptides by renal proximal tubular cells. Diabetologia 39: 149-160.
    • (1996) Diabetologia , vol.39 , pp. 149-160
    • Gugliucci, A.1    Bendayan, M.2
  • 3
    • 0031930853 scopus 로고    scopus 로고
    • Renal catabolism of advanced glycation end products: The fate of pentosidine
    • MIYATA, T., Y. UEDA, K. HORIE, et al. 1998. Renal catabolism of advanced glycation end products: the fate of pentosidine. Kidney Int. 53: 416-422.
    • (1998) Kidney Int. , vol.53 , pp. 416-422
    • Miyata, T.1    Ueda, Y.2    Horie, K.3
  • 4
    • 0032731318 scopus 로고    scopus 로고
    • The tubulointerstitium in progressive diabetic kidney disease: More than an aftermath of glomerular injury?
    • GILBERT, R.E. & M.E. COOPER. 1999. The tubulointerstitium in progressive diabetic kidney disease: more than an aftermath of glomerular injury? Kidney Int. 56: 1627-1637.
    • (1999) Kidney Int. , vol.56 , pp. 1627-1637
    • Gilbert, R.E.1    Cooper, M.E.2
  • 5
    • 0343416902 scopus 로고    scopus 로고
    • Advanced glycation endproducts stimulate the MAP-kinase pathway in tubulus cell line LLC-PK1
    • SIMM, A., G. MUNCH, F. SEIF, et al. 1997. Advanced glycation endproducts stimulate the MAP-kinase pathway in tubulus cell line LLC-PK1. FEBS Lett. 410: 481-484.
    • (1997) FEBS Lett. , vol.410 , pp. 481-484
    • Simm, A.1    Munch, G.2    Seif, F.3
  • 6
    • 0003461658 scopus 로고    scopus 로고
    • Advanced glycated albumin impairs protein degradation in the kidney proximal tubules cell line LLC-PK1
    • SEBEKOVA, K., R. SCHINZEL, H. LING, et al. 1998. Advanced glycated albumin impairs protein degradation in the kidney proximal tubules cell line LLC-PK1. Cell. Mol. Biol. 44: 1051-1060.
    • (1998) Cell. Mol. Biol. , vol.44 , pp. 1051-1060
    • Sebekova, K.1    Schinzel, R.2    Ling, H.3
  • 7
    • 0034670095 scopus 로고    scopus 로고
    • Inhibition of nitric oxide synthase activity by early and advanced glycation end products in cultured rabbit proximal tubular epithelial cells
    • VERBEKE, P., M. PERICHON, B. FRIGUET, et al. 2000. Inhibition of nitric oxide synthase activity by early and advanced glycation end products in cultured rabbit proximal tubular epithelial cells. Biochim. Biophys. Acta 1502: 481-494.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 481-494
    • Verbeke, P.1    Perichon, M.2    Friguet, B.3
  • 8
    • 0036895708 scopus 로고    scopus 로고
    • Activation of tubular epithelial cells in diabetic nephropathy
    • MORCOS, M., A.A. SAYED, A. BIERHAUS, et al. 2002. Activation of tubular epithelial cells in diabetic nephropathy. Diabetes 51: 3532-3544.
    • (2002) Diabetes , vol.51 , pp. 3532-3544
    • Morcos, M.1    Sayed, A.A.2    Bierhaus, A.3
  • 9
    • 0037246065 scopus 로고    scopus 로고
    • Advanced glycation end products inhibit de novo protein synthesis and induce TGF-β overexpression in proximal tubular cells
    • YAMAGISHI, S., Y. INAGAKI, T. OKAMOTO, et al. 2003. Advanced glycation end products inhibit de novo protein synthesis and induce TGF-β overexpression in proximal tubular cells. Kidney Int. 63: 464-473.
    • (2003) Kidney Int. , vol.63 , pp. 464-473
    • Yamagishi, S.1    Inagaki, Y.2    Okamoto, T.3
  • 10
    • 0035661067 scopus 로고    scopus 로고
    • Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE)
    • OLDFIELD, M.D., L.A. BACH, J.M. FORBES, et al. 2001. Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE). J. Clin. Invest. 108: 1853-1863.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1853-1863
    • Oldfield, M.D.1    Bach, L.A.2    Forbes, J.M.3
  • 11
    • 0037406905 scopus 로고    scopus 로고
    • Glucose, glycation, and RAGE: Implications for amplification of cellular dysfunction in diabetic nephropathy
    • WENDT, T., N. TANJI, J. GUO, et al. 2003. Glucose, glycation, and RAGE: implications for amplification of cellular dysfunction in diabetic nephropathy. J. Am. Soc. Nephrol. 14: 1383-1395.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , pp. 1383-1395
    • Wendt, T.1    Tanji, N.2    Guo, J.3
  • 12
    • 18144433542 scopus 로고    scopus 로고
    • The AGE-RAGE system and diabetic nephropathy
    • SAKURAI, S., H. YONEKURA, Y. YAMAMOTO, et al. 2003. The AGE-RAGE system and diabetic nephropathy. J. Am. Soc. Nephrol. 14(Suppl. 3): S259-S263.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , Issue.SUPPL. 3
    • Sakurai, S.1    Yonekura, H.2    Yamamoto, Y.3
  • 13
    • 0033848466 scopus 로고    scopus 로고
    • Expression of advanced glycation end products and their cellular receptor RAGE in diabetic nephropathy and nondiabetic renal disease
    • TANJI, N., G.S. MARKOWITZ, C. FU, et al. 2000. Expression of advanced glycation end products and their cellular receptor RAGE in diabetic nephropathy and nondiabetic renal disease. J. Am. Soc. Nephrol. 11: 1656-1666.
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 1656-1666
    • Tanji, N.1    Markowitz, G.S.2    Fu, C.3
  • 14
    • 0029366113 scopus 로고
    • Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): A new member of the AGE-receptor complex
    • VLASSARA, H., Y.M. LI, F. IMANI, et al. 1995. Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex. Mol. Med. 1: 634-646.
    • (1995) Mol. Med. , vol.1 , pp. 634-646
    • Vlassara, H.1    Li, Y.M.2    Imani, F.3
  • 15
    • 0029020336 scopus 로고
    • Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end products of the Maillard reaction
    • ARAKI, N., T. HIGASHI, T. MORI, et al. 1995. Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end products of the Maillard reaction. Eur. J. Biochem. 230: 408-415.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 408-415
    • Araki, N.1    Higashi, T.2    Mori, T.3
  • 16
    • 0030895048 scopus 로고    scopus 로고
    • A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection
    • SUZUKI, H., Y. KURIHARA, M. TAKEYA, et al. 1997. A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection. Nature 386: 292-296.
    • (1997) Nature , vol.386 , pp. 292-296
    • Suzuki, H.1    Kurihara, Y.2    Takeya, M.3
  • 17
    • 0035793602 scopus 로고    scopus 로고
    • CD36, a member of the class B scavenger receptor family, as a receptor for advanced glycation end products
    • OHGAMI, N., R. NAGAI, M. IKEMOTO, et al. 2001. CD36, a member of the class B scavenger receptor family, as a receptor for advanced glycation end products. J. Biol. Chem. 276: 3195-3202.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3195-3202
    • Ohgami, N.1    Nagai, R.2    Ikemoto, M.3
  • 18
    • 0035918193 scopus 로고    scopus 로고
    • Scavenger receptor class B type I-mediated reverse cholesterol transport is inhibited by advanced glycation end products
    • OHGAMI, N., R. NAGAI, A. MIYAZAKI, et al. 2001. Scavenger receptor class B type I-mediated reverse cholesterol transport is inhibited by advanced glycation end products. J. Biol. Chem. 276: 13348-13355.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13348-13355
    • Ohgami, N.1    Nagai, R.2    Miyazaki, A.3
  • 19
    • 0348048493 scopus 로고    scopus 로고
    • Advanced glycation end products in uremia
    • HENLE, T. & T. MIYATA. 2003. Advanced glycation end products in uremia. Adv. Ren. Replace. Ther. 10:321-331.
    • (2003) Adv. Ren. Replace. Ther. , vol.10 , pp. 321-331
    • Henle, T.1    Miyata, T.2
  • 20
    • 0033997047 scopus 로고    scopus 로고
    • Carbonyl stress' and dialysis-related amyloidosis
    • MIYATA, T., Y. UEDA, A. SAITO, et al. 2000. 'Carbonyl stress' and dialysis-related amyloidosis. Nephrol. Dial. Transplant. 15 (Suppl. 1): 25-28.
    • (2000) Nephrol. Dial. Transplant. , vol.15 , Issue.SUPPL. 1 , pp. 25-28
    • Miyata, T.1    Ueda, Y.2    Saito, A.3
  • 21
    • 0025938891 scopus 로고
    • Advanced glycosylation end products in patients with diabetic nephropathy
    • MAKITA, Z., S. RADOFF, E.J. RAYFIELD, et al. 1991. Advanced glycosylation end products in patients with diabetic nephropathy. N. Engl. J. Med. 325: 836-842.
    • (1991) N. Engl. J. Med. , vol.325 , pp. 836-842
    • Makita, Z.1    Radoff, S.2    Rayfield, E.J.3
  • 22
    • 0028286374 scopus 로고
    • Reactive glycosylation endproducts in diabetic uraemia and treatment of renal failure
    • MAKITA, Z., R. BUCALA, E.J. RAYFIELD, et al. 1994. Reactive glycosylation endproducts in diabetic uraemia and treatment of renal failure. Lancet 343: 1519-1522.
    • (1994) Lancet , vol.343 , pp. 1519-1522
    • Makita, Z.1    Bucala, R.2    Rayfield, E.J.3
  • 23
    • 0031785582 scopus 로고    scopus 로고
    • Accumulation of carbonyls accelerates the formation of pentosidine, an advanced glycation end product: Carbonyl stress in uremia
    • MIYATA, T., Y. UEDA, Y. YAMADA, et al. 1998. Accumulation of carbonyls accelerates the formation of pentosidine, an advanced glycation end product: carbonyl stress in uremia. J. Am. Soc. Nephrol. 9: 2349-2356.
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 2349-2356
    • Miyata, T.1    Ueda, Y.2    Yamada, Y.3
  • 24
    • 0024853285 scopus 로고
    • Profile of drug-metabolizing enzymes in the cortex and medulla of the human kidney
    • PACIFICI, G.M., A. VIANI, M. FRANCHI, et al. 1989. Profile of drug-metabolizing enzymes in the cortex and medulla of the human kidney. Pharmacology 39: 299-308.
    • (1989) Pharmacology , vol.39 , pp. 299-308
    • Pacifici, G.M.1    Viani, A.2    Franchi, M.3
  • 25
    • 0028019068 scopus 로고
    • Complete cloning and sequencing of rat gp330/"megalin," a distinctive member of the low density lipoprotein receptor gene family
    • SAITO, A., S. PIETROMONACO, A.K. LOO, et al. 1994. Complete cloning and sequencing of rat gp330/"megalin," a distinctive member of the low density lipoprotein receptor gene family. Proc. Natl. Acad. Sci. USA 91: 9725-9729.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9725-9729
    • Saito, A.1    Pietromonaco, S.2    Loo, A.K.3
  • 26
    • 84984766757 scopus 로고    scopus 로고
    • Megalin and cubilin: Multifunctional endocytic receptors
    • CHRISTENSEN, E.I. & H. BIRN. 2002. Megalin and cubilin: multifunctional endocytic receptors. Nat. Rev. Mol. Cell. Biol. 3: 256-266.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 256-266
    • Christensen, E.I.1    Birn, H.2
  • 27
    • 3843055696 scopus 로고    scopus 로고
    • Evidence indicating that renal tubular metabolism of leptin is mediated by megalin but not by the leptin receptors
    • HAMA, H., A. SAITO, T. TAKEDA, et al. 2004. Evidence indicating that renal tubular metabolism of leptin is mediated by megalin but not by the leptin receptors. Endocrinology 145: 3935-3940.
    • (2004) Endocrinology , vol.145 , pp. 3935-3940
    • Hama, H.1    Saito, A.2    Takeda, T.3
  • 28
    • 0035031562 scopus 로고    scopus 로고
    • Cubilin, a multifunctional epithelial receptor: An overview
    • KOZYRAKI, R. 2001. Cubilin, a multifunctional epithelial receptor: an overview. J. Mol. Med. 79: 161-167.
    • (2001) J. Mol. Med. , vol.79 , pp. 161-167
    • Kozyraki, R.1
  • 31
    • 0034193309 scopus 로고    scopus 로고
    • Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin
    • OLEINIKOV, A.V., J. ZHAO, S.P. MAKKER, et al. 2000. Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin. Biochem. J. 347(Pt. 3): 613-621.
    • (2000) Biochem. J. , vol.347 , Issue.PART 3 , pp. 613-621
    • Oleinikov, A.V.1    Zhao, J.2    Makker, S.P.3
  • 32
    • 0033673093 scopus 로고    scopus 로고
    • Characterization of ANKRA, a novel ankyrin repeat protein that interacts with the cytoplasmic domain of megalin
    • RADER, K., R.A. ORLANDO, X. LOU, et al. 2000. Characterization of ANKRA, a novel ankyrin repeat protein that interacts with the cytoplasmic domain of megalin. J. Am. Soc. Nephrol. 11: 2167-2178.
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 2167-2178
    • Rader, K.1    Orlando, R.A.2    Lou, X.3
  • 33
    • 0035082651 scopus 로고    scopus 로고
    • The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes
    • PATRIE, K.M., A.J. DRESCHER, M. GOYAL, et al. 2001. The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes. J. Am. Soc. Nephrol. 12: 667-677.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 667-677
    • Patrie, K.M.1    Drescher, A.J.2    Goyal, M.3
  • 34
    • 0036009682 scopus 로고    scopus 로고
    • GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: Putative role in regulating megalin's function
    • LOU, X., T. MCQUISTAN, R.A. ORLANDO, et al. 2002. GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function. J. Am. Soc. Nephrol. 13: 918-927.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 918-927
    • Lou, X.1    Mcquistan, T.2    Orlando, R.A.3
  • 35
    • 0037328934 scopus 로고    scopus 로고
    • Functional interaction of megalin with the megalin binding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule
    • PETERSEN, H.H., J. HILPERT, D. MILITZ, et al. 2003. Functional interaction of megalin with the megalin binding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule. J. Cell. Sci. 116: 453-461.
    • (2003) J. Cell. Sci. , vol.116 , pp. 453-461
    • Petersen, H.H.1    Hilpert, J.2    Militz, D.3
  • 36
    • 0344875494 scopus 로고    scopus 로고
    • The adaptor protein ARH escorts megalin to and through endosomes
    • NAGAI, M., T. MEERLOO, T. TAKEDA, et al. 2003. The adaptor protein ARH escorts megalin to and through endosomes. Mol. Biol. Cell 14: 4984-4996.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4984-4996
    • Nagai, M.1    Meerloo, T.2    Takeda, T.3
  • 37
    • 0345352651 scopus 로고    scopus 로고
    • Role of megalin in endocytosis of advanced glycation end products: Implications for a novel protein binding to both megalin and advanced glycation end products
    • SAITO, A., R. NAGAI, A. TANUMA, et al. 2003. Role of megalin in endocytosis of advanced glycation end products: implications for a novel protein binding to both megalin and advanced glycation end products. J. Am. Soc. Nephrol. 14: 1123-1131.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , pp. 1123-1131
    • Saito, A.1    Nagai, R.2    Tanuma, A.3
  • 38
    • 0041842628 scopus 로고    scopus 로고
    • Bioerigineered implantation of megalin-expressing cells: A potential intracorporeal therapeutic model for uremic toxin protein clearance in renal failure
    • SAITO, A., J.J. KAZAMA, N. IINO, et al. 2003. Bioerigineered implantation of megalin-expressing cells: a potential intracorporeal therapeutic model for uremic toxin protein clearance in renal failure. J. Am. Soc. Nephrol. 14: 2025-2032.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , pp. 2025-2032
    • Saito, A.1    Kazama, J.J.2    Iino, N.3


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