| First Author | Kaur I | Year | 2011 |
| Journal | FEBS Lett | Volume | 585 |
| Issue | 6 | Pages | 829-33 |
| PubMed ID | 21320498 | Mgi Jnum | J:170331 |
| Mgi Id | MGI:4946330 | Doi | 10.1016/j.febslet.2011.02.008 |
| Citation | Kaur I, et al. (2011) Modification of mouse A2M B (620-792) and A2M N (168-230) by malondialdehyde and acetaldehyde attenuates the proteinase and TGF-beta1 binding ability of A2MB. FEBS Lett 585(6):829-33 |
| abstractText | Acetaldehyde and malondialdehyde react covalently with cellular proteins forming protein-malondialdehyde-acetaldehyde adducts thus modulating their biochemical functions. Alpha-2 macroglobulin, an acute phase protein produced by liver binds to cytokines, growth factors and neutralizes proteinases. In this study we examined the formation of MAA adducts of N-terminal and bait region of mouse A2M and their effect on modulating its proteinase and TGF-beta1 binding activities. Adduct formation abrogated the binding of bait region with TGF-beta1, trypsin, and elastase. TGF-beta1 induced NO production was also suppressed. Acetaldehyde and MDA adduction of A2M may have physiological consequences in alcoholic patients. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: TGF Beta1binds to A2M by enzyme linked immunosorbent assay (View interaction). |
