Molecular Vision: Picciani, Mol Vis 2008; 14:871-877. Table 2

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 1^5,7	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.