Table 2. Select proteases and proteins identified from normal trabecular meshwork.
Protein |
Accession number 1 |
Peptide matches2 |
Peptide matches3 |
Donors3 |
Alpha-1-antichymotrypsin precursor 4 |
P01011 |
4 |
5 |
6 |
Alpha-1-antitrypsin precursor4 |
P01009 |
4 |
14 |
6 |
Antithrombin-III precursor4 |
P01008 |
3 |
2 |
3 |
Calpactin I light chain5 |
P08206 |
7 |
1 |
1 |
Calpain 1, large [catalytic] subunit |
P07384 |
7 |
6 |
3 |
Calponin H1, smooth muscle5 |
P51911 |
3 |
1 |
2 |
Caspase-14 precursor |
P31944 |
6 |
2 |
3 |
Cathepsin D6 |
P07339 |
6 |
2 |
2 |
Ceruloplasmin precursor5 |
P00450 |
5 |
5 |
4 |
Coagulation factor XIII A chain5 |
P00488 |
2 |
1 |
1 |
Complement C37 |
P01024 |
4 |
3 |
3 |
Complement C4 precursor7 |
P01028 |
4 |
1 |
2 |
Complement component 15,7 |
Q07021 |
3 |
2 |
1 |
Complement factor B precursor7 |
P00751 |
3 |
2 |
1 |
Complement factor H precursor7 |
P08603 |
3 |
2 |
1 |
Endoplasmin5 |
P14625 |
3 |
2 |
3 |
Neurolysin, mitochondrial |
Q9BYT8 |
2 |
1 |
2 |
Prothrombin precursor |
P00734 |
2 |
1 |
3 |
Puromycin-sensitive aminopeptidase |
P55786 |
3 |
1 |
1 |
Tripeptidyl-peptidase II | P29144 | 3 | 1 | 1 |
The proteins that mostly proteases identified by LC MS/MS of protein extracts were derived from the TM of a 55-year-old male Caucasian donor after enrichment on an immobilized immunocolumn and SDS–PAGE fractionation as described in Methods. 1Swiss-Prot database entries are shown; 2peptide matches in current mass spectrometric analyses; 3peptide matches and number of donors from our previous TM proteomic analyses [17] without affinity enrichment; 4identified protease inhibitors; 5identified proteins that are not proteases; 6cathepsin D has been identified as bovine and human protein in our previous and current TM proteomic analysis, here human protein accession number has been provided; 7not all complement components possess proteolytic activity; however, they act as a complex which results in proteolytic activity, here we have placed them in the protease category.