Table 4.
Reduced abundance of mitochondrial proteostasis and unfolded protein response (UPRmt) effector proteins in old male HFpEF cardiomyocyte mitochondria. Summary of mitochondrial chaperones, co-chaperones, and proteases identified by DIA proteomics that are significantly reduced in cardiomyocyte mitochondria from old mice with HFD+ L-NAME compared with age-matched RD controls. Proteins are annotated by functional category, sub-mitochondrial localization, log2 fold change (HFpEF vs control), abundance ratio, and false discovery rate (FDR)-adjusted P value.
| Category | Gene | Protein name | Localization | log2FC (HFpEF vs Ctrl) | HFpEF / Ctrl | Adjusted P (FDR) | Interpretation |
|---|---|---|---|---|---|---|---|
| Chaperone | Hspd1 | HSP60 | Matrix | –0.48 | 0.72 | <0.05 | ↓ protein folding capacity |
| Chaperone | Hspe1 | HSP10 | Matrix | –0.52 | 0.70 | <0.05 | ↓ chaperonin cofactor |
| Chaperone | Hspa9 | mtHSP70 / Mortalin | Matrix | –0.58 | 0.67 | <0.05 | ↓ protein import & folding |
| Co-chaperone | Dnaja3 | Tid1 | Matrix/IMM | –0.70 | 0.62 | <0.01 | ↓ co-chaperone activity |
| Protease | ClpP | Caseinolytic peptidase P | Matrix | –0.46 | 0.73 | <0.05 | ↓ UPRmt core protease |
| Protease | Lonp1 | Lon protease | Matrix | –0.48 | 0.72 | <0.05 | ↓ matrix protein quality control |
| Protease | Afg3l2 | m-AAA protease subunit | IMM (matrix-facing) | –0.54 | 0.69 | <0.05 | ↓ IMM proteostasis |