TABLE 2.
Comparative secretion of proteins identified from visceral and subcutaneous adipose tissue–derived preadipocytes
| Description | Signal peptide? | Functional description | Accession |
|---|---|---|---|
| Collagen α-1(I) chain | + | Extracellular matrix | CO1A1_MOUSE |
| Collagen α-2(I) chain | + | Extracellular matrix | CO1A2_MOUSE |
| Collagen α-1(III) chain | + | Extracellular matrix | CO3A1_MOUSE |
| Collagen α-2(V) chain | + | Extracellular matrix | CO5A2_MOUSE |
| Fibronectin | + | Extracellular matrix | FINC_MOUSE |
| Fibulin-2 | + | Extracellular matrix | FBLN2_MOUSE |
| SPARC | + | Angiogenesis inhibitor | SPRC_MOUSE |
| Pigment epithelium-derived factor | + | Angiogenesis inhibitor, role in insulin resistance | PEDF_MOUSE |
| Collagen α-1(V) chain | + | Extracellular matrix | CO5A1_MOUSE |
| Haptoglobin | + | Haem binding protein, acute phase reactant | HPT_MOUSE |
| Cathepsin B | + | Protease activity | CATB_MOUSE |
| Plasma protease C1 inhibitor | + | Inhibits C1s and C1r protease activity | IC1_MOUSE |
| Plasminogen activator inhibitor 1 | + | Serine protease inhibitor, inhibits matrix metalloproteinases, associated with insulin resistance | PAI1_MOUSE |
| Collagen α-1(II) chain | + | Extracellular matrix | CO2A1_MOUSE |
| Metalloproteinase inhibitor 1 | + | Regulation of extracellular matrix | TIMP1_MOUSE |
| Collagen α-1(IV) chain | + | Extracellular matrix | CO4A1_MOUSE |
| Titin | - | Mechanical contraction | TITIN_MOUSE |
| Biglycan | + | Extracellular matrix | PGS1_MOUSE |
| Cathepsin L1 | + | Cysteine protease | CATL1_MOUSE |
| Epidermal growth factor receptor | + | Regulation of growth and proliferation | EGFR_MOUSE |
| Collagen α-2(XI) chain | + | Extracellular matrix | COBA2_MOUSE |
| Follistatin-related protein 1 | + | Growth factor binding | FSTL1_MOUSE |
| A disintegrin and metalloproteinase with thrombospondin motifs 7 | + | Regulation of extracellular matrix | ATS7_MOUSE |
Visceral or subcutaneous WAT-derived preadipocytes were incubated in media containing different isotopes of arginine and lysine. Conditioned media were mixed, subjected to lectin affinity chromatography, and subjected to quantitative mass spectrometry. Peak height ratios of isotope to endogenous (12C) amino acids and ratios between isotopes are shown. Complete dataset available in supplementary data.