期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 20, 期 3, 页码 1205-1209出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2009.11.132
关键词
alpha(1)-Acid glycoprotein; Acute-phase proteins; Drug binding; Chaperone; Thermal aggregation
资金
- OTKA [K69213]
In vitro chaperone-like activity of the acute-phase component and plasma drug transporter human alpha(1)-acid glycoprotein (AAG) has been shown for the first time. AAG suppressed thermal aggregation of a variety of unrelated enzymatic (e. g., aldolase, catalase, enolase, carbonic anhydrase) and non-enzymatic proteins (beta-lactoglobulin, ovotransferrin) and it also prevented dithiothreitol induced aggregation of insulin. The anti-aggregation ability of AAG was abolished/reduced upon drug binding suggesting that protein protein interactions established between the lipocalin beta-barrel fold of AAG and hydrophobic surfaces of the stressed proteins are involved in the chaperone-like activity. The results shed some light on the possible biological function of this enigmatic protein and suggest that besides haptoglobin, clusterin, fibrinogen and alpha(2)-macroglobulin AAG can be considered as a novel member of the extracellular molecular chaperones found in human body fluids. (C) 2009 Elsevier Ltd. All rights reserved.
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