From: Proteomic profiling of endorepellin angiostatic activity on human endothelial cells
Spot number (see Fig. 2) | Protein ID | Gene name | NCBI Accession Number | Mr (kDa) | pI | Response to endorepellin (mean fold change) | p-value | Reported functions a |
---|---|---|---|---|---|---|---|---|
1 | Calreticulin | CALR | 4757900 | 48 | 4.14 | ↓ Downregulated, 0.642 | 0.0881 | Molecular calcium binding and chaperone protein |
2 | β-actin | ACTB | 4501885 | 42 | 5.18 | ↓ Downregulated, 0.403 | 0.0023 | Cellular structure, motility and integrity |
3 | Chaperonin/Hsp60 | HSPD1 | 31542947 | 61 | 5.59 | ↓ Downregulated, 0.714 | 0.1262 | Mitochondrial protein assembly, prevention of misfolding, produced under stress within the mitochondrial matrix |
4 | Vimentin | VIM | 4507895 | 54 | 4.91 | ↑ Upregulated, 3.178 | 0.0276 | Class III intermediate filament, cytoskeletal crosstalk, intracellular communication, influence cell shape, adhesion and migration, signalling events |
5 | Prolyl 4-hydroxylase, β subunit | P4HB | 20070125 | 57 | 4.61 | ↑ Absent from Controlb | - | Key subunit of prolyl 4-hydroxylase enzyme, identical to protein disulfide isomerase |