Copyright
©The Author(s) 2016.
World J Nephrol. Jan 6, 2016; 5(1): 66-75
Published online Jan 6, 2016. doi: 10.5527/wjn.v5.i1.66
Published online Jan 6, 2016. doi: 10.5527/wjn.v5.i1.66
Table 1 Pathogen associated molecular pattern and damage associated molecular pattern that trigger nod-like receptor protein-3 activation[12]
| Type | Molecule/molecular pattern |
| PAMP | Leptospiral interrogans/glycolipoprotein |
| Influenza | |
| Streptococcus pyogenes/streptolysin O | |
| Staphylococcus aureus/alpha hemolysin | |
| DAMP | ATP |
| Nigericin | |
| Histones | |
| U1snRNP ribonucleoprotein | |
| dsDNA/nucleosomes | |
| MSU crystals | |
| Uromodulin | |
| Biglycan | |
| Silica | |
| Alum | |
| Calcium oxalate | |
| Asbestos | |
| Amyloid-β | |
| Hemazoin | |
| Hyaluronan |
Table 2 Over 30 proteins capable of amyloid formation have been identified
| Immunoglobulin light chains in primary systemic amyloidosis |
| Ig heavy chain |
| Beta2-microglobulin in dialysis-associated arthropathy |
| Amyloid beta protein in alzheimer disease and down syndrome |
| Hereditary forms (including transthyretin, apolipoprotein A-I and A-II, gelsolin, lysozyme, fibrinogen a-alpha chain |
| Amyloid a in secondary amyloidosis |
- Citation: Scarpioni R, Ricardi M, Albertazzi V. Secondary amyloidosis in autoinflammatory diseases and the role of inflammation in renal damage. World J Nephrol 2016; 5(1): 66-75
- URL: https://www.wjgnet.com/2220-6124/full/v5/i1/66.htm
- DOI: https://dx.doi.org/10.5527/wjn.v5.i1.66
