Title : Analysis of the acrolein-modified sites of apolipoprotein B-100 in LDL.

Pub. Date : 2021 Jan

PMID : 32919080






9 Functional Relationships(s)
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1 The purpose of this study was to determine which amino acid residues of apoB protein in LDL are conjugated with acrolein. Acrolein apolipoprotein B Homo sapiens
2 Acro-apoB was prepared by incubation of LDL with acrolein (10 to 60 muM) at 37 C for 7 days. Acrolein apolipoprotein B Homo sapiens
3 Identification of acrolein-conjugated amino acid residues in apoB was performed using LC-MS/MS. Acrolein apolipoprotein B Homo sapiens
4 The levels of acrolein-conjugated amino acid residues of apoB as well as crosslinking apoB increased in proportion to acrolein concentration. Acrolein apolipoprotein B Homo sapiens
5 The levels of acrolein-conjugated amino acid residues of apoB as well as crosslinking apoB increased in proportion to acrolein concentration. Acrolein apolipoprotein B Homo sapiens
6 The levels of acrolein-conjugated amino acid residues of apoB as well as crosslinking apoB increased in proportion to acrolein concentration. Acrolein apolipoprotein B Homo sapiens
7 The level of LDL uptake by macrophages was parallel with the acrolein-conjugated monomer apoB. Acrolein apolipoprotein B Homo sapiens
8 Acrolein-conjugated amino acid residues in apoB were C212, K327, K742, K949, K1087, H1923, K2634, K3237 and K3846. Acrolein apolipoprotein B Homo sapiens
9 It is proposed that the rapid uptake of LDL by macrophages is dependent on acrolein conjugation of four amino acids residues at the scavenger receptor recognition site of apoB in LDL. Acrolein apolipoprotein B Homo sapiens