1,028
Views
4
CrossRef citations to date
0
Altmetric
Biochemistry & Molecular Biology

Identification of pyridinoline, a collagen crosslink, as a novel intrinsic ligand for the receptor for advanced glycation end-products (RAGE)

, , , , , & show all
Pages 1508-1514 | Received 20 Apr 2018, Accepted 07 May 2018, Published online: 26 May 2018

References

  • Hayase F. Recent development of 3-deoxyosone related Maillard reaction products. Food Sci Technol Res. 2000;6:79–86.
  • Neeper M, Schmidt AM, Brett J, et al Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. J Biol Chem. 1992;267:14998–15004.
  • Ott C, Jacobs K, Haucke E, et al Role of advanced glycation end products in cellular signaling. Redox Biol. 2014;2:411–429.
  • Kierdorf K, Fritz G. RAGE regulation and signaling in inflammation and beyond. J Leukoc Biol. 2013;94:55–68.
  • Srikanth V, Maczurek A, Phan T, et al Advanced glycation endproducts and their receptor RAGE in Alzheimer’s disease. Neurobiol Aging. 2011;32:763–777.
  • Hori O, Brett J, Slattery T, et al The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system. J Biol Chem. 1995;270:25752–25761.
  • Hofmann MA, Drury S, Fu C, et al RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell. 1999;97:889–901.
  • Chen GY, Nuñez G. Sterile inflammation: sensing and reacting to damage. Nat Rev Immunol. 2010;10:826–837.
  • Takeuchi M, Bucala R, Suzuki T, et al Neurotoxicity of advanced glycation end-products for cultured cortical neurons. J Neuropathol Exp Neurol. 2000;59:1094–1105.
  • Sato T, Iwaki M, Shimogaito N, et al TAGE (toxic AGEs) theory in diabetic complications. Curr Mol Med. 2006;6:351–358.
  • Takeuchi M, Yamagishi S. Involvement of toxic AGEs (TAGE) in the pathogenesis of diabetic vascular complications and Alzheimer’s disease. J Alzheimers Dis. 2009;16:845–858.
  • Usui T, Hayase F. Isolation and identification of the 3-hydroxy-5-hydroxymethyl-pyridinium compound as a novel advanced glycation end product on glyceraldehyde-related Maillard reaction. Biosci Biotechnol Biochem. 2003;67:930–932.
  • Nagai R, Hayashi CM, Xia L, et al Identification in human atherosclerotic lesions of GA-pyridine, a novel structure derived from glycolaldehyde-modified proteins. J Biol Chem. 2002;277:48905–48912.
  • Murakami Y, Fujino T, Hasegawa T, et al Receptor for advanced glycation end products (RAGE)-mediated cytotoxicity of 3-hydroxypyridinium derivatives. Biosci Biotechnol Biochem. 2018;82:312–319.
  • Fujimoto D, Akiba K-Y, Nakamura N. Isolation and characterization of a fluorescent material in bovine achilles tendon collagen. Biochem Biophys Res Commun. 1977;76:1124–1129.
  • Saito M, Marumo K. Effects of collagen crosslinking on bone material properties in health and disease. Calcif Tissue Int. 2015;97:242–261.
  • Robins SP, Stewart P, Astbury C, et al Measurement of the cross linking compound, pyridinoline, in urine as an index of collagen degradation in joint disease. Ann Rheum Dis. 1986;45:969–973.
  • Delmas PD, Schlemmer A, Gineyts E, et al Urinary excretion of pyridinoline crosslinks correlates with bone turnover measured on iliac crest biopsy in patients with vertebral osteoporosis. J Bone Miner Res. 1991;6:639–644.
  • Risteli J, Elomaa I, Niemi S, et al Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation. Clin Chem. 1993;39:635–640.
  • Robins SP, Duncan A, Wilson N, et al Standardization of pyridinium crosslinks, pyridinoline and deoxypyridinoline, for use as biochemical markers of collagen degradation. Clin Chem. 1996;42:1621–1626.
  • Strober W. Trypan blue exclusion test of cell viability. Curr Protoc Immunol. 2001;21:A3B1–A3B2.
  • Santilli F, Vazzana N, Bucciarelli LG, et al Soluble forms of RAGE in human diseases: clinical and therapeutical implications. Curr Med Chem. 2009;16:940–952.
  • Thomas J, Elsden DF, Partridge SM. Degradation products from elastin: partial structure of two major degradation products from the cross-linkages in elastin. Nature. 1963;200:651–652.
  • Siegel RC, Fu JC, Uto N, et al Collagen cross-linking: lysyl oxidase dependent synthesis of pyridinoline in vitro: confirmation that pyridinoline is derived from collagen. Biochem Biophys Res Commun. 1982;108:1546–1550.
  • Barber M, Bordoli RS, Elliott GJ, et al The structure(s) of pyridinoline(s). Biochem Biophys Res Commun. 1982;109:1041–1046.
  • Daffu G, del Pozo CH, O’Shea KM, et al Radical roles for RAGE in the pathogenesis of oxidative stress in cardiovascular diseases and beyond. Int J Mol Sci. 2013;14:19891–19910.
  • Usui T, Shimohira K, Watanabe H, et al Detection and determination of glyceraldehyde-derived pyridinium-type advanced glycation end product in streptozotocin-induced diabetic rats. Biosci Biotechnol Biochem. 2007;71:442–448.
  • James I, Crowley C, Perrett D. Assay of pyridinium crosslinks in serum using narrow-bore ion-paired reversed-phase high-performance liquid chromatography. J Chromatogr. 1993;612:41–48.
  • Abbiati G, Rigoldi M, Frignani S, et al Determination of pyridinium crosslinks in plasma and serum by high-performance liquid chromatography. J Chromatogr B Biomed Appl. 1994;656:303–310.
  • Kaczmarek A, Vandenabeele P, Krysko DV. Necroptosis: the release of damage-associated molecular patterns and its physiological relevance. Immunity. 2013;38:209–223.
  • Termeer C, Benedix F, Sleeman J, et al Oligosaccharides of Hyaluronan activate dendritic cells via toll-like receptor 4. J Exp Med. 2002;195:99–111.
  • Scheibner KA, Lutz MA, Boodoo S, et al Hyaluronan fragments act as an endogenous danger signal by engaging TLR2. J Immunol. 2006;177:1272–1281.
  • Okamura Y, Watari M, Jerud ES, et al The extra domain A of fibronectin activates Toll-like receptor 4. J Biol Chem. 2001;276:10229–10233.
  • Hwang HS, Park SJ, Cheon EJ, et al Fibronectin fragment-induced expression of matrix metalloproteinases is mediated by MyD88-dependent TLR-2 signaling pathway in human chondrocytes. Arthritis Res Ther. 2015;17:320.
  • Harrington DJ. Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease. Infect Immun. 1996;64:1885–1891.
  • Watanabe K. Collagenolytic proteases from bacteria. Appl Microbiol Biotechnol. 2004;63:520–526.
  • Tchetverikov I, Lohmander LS, Verzijl N, et al MMP protein and activity levels in synovial fluid from patients with joint injury, inflammatory arthritis, and osteoarthritis. Ann Rheum Dis. 2005;64:694–698.
  • Burrage PS, Mix KS, Brinckerhoff CE. Matrix metalloproteinases: role in arthritis. Front Biosci. 2006;11:529–543.
  • Oldfield MD, Bach LA, Forbes JM, et al Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE). J Clin Invest. 2001;108:1853–1863.
  • Simonson MS. Phenotypic transitions and fibrosis in diabetic nephropathy. Kidney Int. 2007;71:846–854.
  • Raghavan CT, Nagaraj RH. AGE-RAGE interaction in the TGFβ2-mediated epithelial to mesenchymal transition of human lens epithelial cells. Glycoconj J. 2016;33:631–643.
  • Nam MH, Nagaraj RH. Matrix-bound AGEs enhance TGFβ2-mediated mesenchymal transition of lens epithelial cells via the noncanonical pathway: implications for secondary cataract formation. Biochem J. 2018;475:1427–1440.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.