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. 2008 May 14;14:871–877.

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.