[P27] 4 Hydroxynonenal modified Bovine Serum Albumin (4 HNE-BSA)40P-HNE-BS102
|Concentration:||1 mg / ml, determined by the Lowry method|
|Source:||Bovine Serum Albumin purchased from Boehringer Mannheim and modified with 4- HNE.|
|Buffer:||In 10 mM PBS, 0.15 M NaCl, 0.5 mM EDTA, 0.01 % NaN3, pH 7.4.|
|Storage:||-20°C for short and long-term storage. Aliquot to avoid repeated freezing and thawing.|
*The products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.
Modifications on lysine residues, with formation of carboxylmethyl-lysine (CML), malondialdehyde (MDA) and hexitol-lysine are advanced glycation end-products (AGE), and the coupling with reactive aldehyde compounds, such as 4-hydroxynonenal (4-HNE) may appear from lipid oxidation (Guichardant et al., 1998). These modifications feature the oxidative byproducts which react with NH2 groups and form Schiff-base adducts (Mark et al., 1996).
LDL treated with HNE or oxidatively modified by Cu++ or by cultured endothelial cells give rise to Michael addition-type HNE adducts that are recognized by HNE-specific antibodies.
Guichardant M, Taibi-Tronche P, Fay LB, Lagarde M. Covalent modifications of aminophospholipids by 4-hydroxynonenal. Free Radic Biol Med. 1998 Dec;25(9):1049-56.
Mark S. Bolgar, Chao-Yuh Yang, and Simon J. Gaskell, First Direct Evidence for Lipid/Protein Conjugation in Oxidized Human Low Density Lipoprotein (LDL), JBC, 271: 27999-28001 (1996).
|[P27]||2017||Grönwall, Caroline; Amara, Khaled; Hardt, Uta; Krishnamurthy, Akilan; Steen, Johanna; Engström, Marianne et al. (2017): Autoreactivity to malondialdehyde-modifications in rheumatoid arthritis is linked to disease activity and synovial pathogenesis. In Journal of autoimmunity 84, pp. 29–45. DOI: 10.1016/j.jaut.2017.06.004.|