TABLE 2.
Number of modified amino acid residues in apoA1 of HDL from LDL(−) fractions and native HDL
| Number of Various Amino Acid Residues | |||||
| HDL in LDL(−) Fraction | Native HDL | ||||
| Modification Types | AMI Patient | Healthy Subject | (A) | (B) | (C) |
| Adducts of reactive lipid aldehydes | |||||
| Acrolein addition +38 (K) | 13 | 14 | 10 | 0 | 5 |
| Acrolein addition +56 (K) | 19 | 16 | 9 | 0 | 11 |
| Acrolein addition +76 (K) | 19 | 13 | 8 | 2 | 6 |
| Acrolein addition +94 (K) | 16 | 14 | 7 | 0 | 4 |
| Acrolein addition +112 (K) | 19 | 18 | 8 | 1 | 8 |
| Reduced acrolein addition +58 (K) | 20 | 21 | 13 | 4 | 8 |
| Reduced acrolein addition +96 (K) | 13 | 11 | 6 | 1 | 7 |
| Reduced HNE (H) | 4 | 4 | 3 | 1 | 5 |
| ONE addition +154 (K) | 12 | 16 | 11 | 1 | 10 |
| Hexanoyl addition +98 (K) | 14 | 18 | 7 | 0 | 5 |
| HPNE addition +172 (K) | 12 | 17 | 13 | 0 | 8 |
| MDA adduct +54 (K) | 17 | 18 | 4 | 1 | 4 |
| MDA adduct +62 (K) | 19 | 15 | 11 | 0 | 4 |
| Halogenation/nitration | |||||
| Chloro (Y) | 0 | 1 | 0 | 0 | 0 |
| Nitro (W) | 0 | 1 | 0 | 0 | 0 |
| Nitro (Y) | 4 | 2 | 1 | 2 | 0 |
| Oxidized amino acids | |||||
| Dioxidation (K) | 1 | 1 | 0 | 1 | 0 |
| Dioxidation (P) | 2 | 0 | 1 | 0 | 1 |
| Dioxidation [R] | 4 | 1 | 4 | 0 | 0 |
| Dioxidation (W) | 4 | 4 | 4 | 2 | 3 |
| Dioxidation (Y) | 2 | 1 | 3 | 0 | 1 |
| Oxidation (D) | 7 | 2 | 1 | 1 | 1 |
| Oxidation (F) | 2 | 0 | 1 | 0 | 1 |
| Oxidation (H) | 4 | 2 | 3 | 2 | 1 |
| Oxidation (K) | 8 | 0 | 0 | 0 | 1 |
| Oxidation (N) | 3 | 1 | 0 | 0 | 0 |
| Oxidation (P) | 10 | 5 | 5 | 0 | 5 |
| Oxidation (R) | 4 | 4 | 3 | 0 | 2 |
| Oxidation (W) | 4 | 4 | 4 | 0 | 2 |
| Oxidation (Y) | 5 | 2 | 2 | 2 | 0 |
| Trioxidation (W) | 3 | 4 | 1 | 0 | 0 |
| Trioxidation (Y) | 1 | 0 | 2 | 0 | 1 |
| Others | |||||
| Trp→hydroxykynurenine (W) | 4 | 4 | 2 | 0 | 0 |
| Trp→kynurenine (W) | 4 | 4 | 4 | 0 | 1 |
| Total | 273 | 238 | 151 | 21 | 105 |
LDL(−) upper bands and native HDL bands from three healthy subjects in agarose gel electrophoresis were analyzed by LC-MS/MS to detect modified peptide fragments of apoA1. In total, 34 modification types were identified in the apoA1 sequence. Total sites of the oxidized amino acid modifications were counted for each sample. The name of the original amino acid residue was written in one-letter code; (D), aspartic acid; (F), phenylalanine; (H), histidine; (K), lysine; (N), asparagine; (P), proline; (R), arginine; (W), tryptophan; (Y), tyrosine. The representative data from HDL in LDL(–) fraction from an AMI patient and a healthy subject, and native HDL fraction from three healthy subjects (A, B, C) are indicated. See supplemental Tables S3–S7 for detailed results.