Partial list of proteins with oxidation-sensitive methionine residues
Target protein . | Oxidation-sensitive methionine(s)* . | Effect of MetSO on protein function† . | Reference(s) . |
---|---|---|---|
Proteins relevant to cardiovascular biology | |||
CaMKII | Met281, Met282 | ↑ | 31,32 |
Apolipoprotein A-I | Met86, Met112, Met148 | ↓ | 43,45,46 |
Actin | Met46, Met49 | ↓ | 21,93 |
IκBα | Met45 | ↑ | 94,95 |
p53 | Met340 | ↓ | 96 |
S100A9 | Met63, Met83 | ↓ | 92 |
Proteins involved in hemostasis and thrombosis | |||
Thrombomodulin | Met388 | ↓ | 57,60 |
Activated protein C | Met59 | ↓ | 67 |
VWF | Met1606 | ↑ | 75,76 |
ADAMTS13 | Met249, Met331, Met496 | ↓ | 80 |
Fibrinogen | Met78, Met367, Met476 | ↔ | 84,85 |
α-2-Antiplasmin | 10 Met residues | ND | 90 |
Antithrombin III | Met314, Met315 | ND | 90,91 |
Factor VII | Met298, Met306 | ↓ | 89 |
Plasminogen activator inhibitor-1 | Met347 | ─ | 87,88 |
Tissue plasminogen activator | Met207 | ─ | 86 |
Target protein . | Oxidation-sensitive methionine(s)* . | Effect of MetSO on protein function† . | Reference(s) . |
---|---|---|---|
Proteins relevant to cardiovascular biology | |||
CaMKII | Met281, Met282 | ↑ | 31,32 |
Apolipoprotein A-I | Met86, Met112, Met148 | ↓ | 43,45,46 |
Actin | Met46, Met49 | ↓ | 21,93 |
IκBα | Met45 | ↑ | 94,95 |
p53 | Met340 | ↓ | 96 |
S100A9 | Met63, Met83 | ↓ | 92 |
Proteins involved in hemostasis and thrombosis | |||
Thrombomodulin | Met388 | ↓ | 57,60 |
Activated protein C | Met59 | ↓ | 67 |
VWF | Met1606 | ↑ | 75,76 |
ADAMTS13 | Met249, Met331, Met496 | ↓ | 80 |
Fibrinogen | Met78, Met367, Met476 | ↔ | 84,85 |
α-2-Antiplasmin | 10 Met residues | ND | 90 |
Antithrombin III | Met314, Met315 | ND | 90,91 |
Factor VII | Met298, Met306 | ↓ | 89 |
Plasminogen activator inhibitor-1 | Met347 | ─ | 87,88 |
Tissue plasminogen activator | Met207 | ─ | 86 |
The listed proteins have been characterized by the presence of ≥1 methionine residue with a potential regulatory role or pathologic effect in cardiovascular biology or thrombosis.
The numbering scheme of the oxidation-sensitive methionine residues is based on the species and isoform of the proteins studied in the cited references.
The relative change in function as a consequence of methionine oxidation is indicated as follows: ↑, enhanced; ↓, suppressed; ↔, altered structure; ─, no effect; ND, not determined.