Shotgun proteomics implicates protease inhibition and complement activation in the antiinflammatory properties of HDL
J. Clin. Invest. Tomas Vaisar, et al. 117:746 doi:10.1172/JCI26206 [
Go to this article.]
Figure 1Global view of biological processes and molecular functions of HDL proteins. Proteins in total HDL and HDL
3 were identified using LC-ESI-MS/MS (Table
2). Proteins detected in HDL were associated with biological functions using GO process annotations. This approach demonstrated significant overrepresentation of proteins involved in several categories, including lipid metabolism (
P = 2 × 10
–27), the acute-phase response (
P = 1 × 10
–18), protease inhibitor activity (
P = 2 × 10
–6), and complement regulation (
P = 5 × 10
–5). apoH, β-2-glycoprotein I; AGT, angiotensinogen; AHSG, α-2-HS-glycoprotein; AMP, bikunin; FGA, fibrinogen; HRP, haptoglobin-related protein; HPX, hemopexin; ITIH4, inter-α-trypsin inhibitor heavy chain H4; KNG1, kininogen-1; LCAT, lecithin-cholesterol acyltransferase; ORM2, α-1-acid glycoprotein 2; PLTP, phospholipid transfer protein; RBP4, retinol binding protein; SERA1, α-1-antitrypsin; SERF1, serpin peptidase inhibitor (clade F, member 1); SERF2, α-2-antiplasmin; TF, transferrin; TTR, transthyretin; VTN, vitronectin.
