Analysis of apolipoprotein A-I as a substrate for matrix metalloproteinase-14

Title
Analysis of apolipoprotein A-I as a substrate for matrix metalloproteinase-14
Author(s)
조경현박기훈박준형[박준형]박성민[박성민]이승택[이승택]
Keywords
HIGH-DENSITY-LIPOPROTEIN; PLASMA; ACTIVATION; SENESCENCE; EXPRESSION; TRUNCATION; CLEAVAGE; PROTEIN; CELLS; GENE
Issue Date
201105
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.409, no.1, pp.58 - 63
Abstract
Substrates for matrix metalloproteinase (MMP)-14 were previously identified in human plasma using proteomic techniques. One putative MMP-14 substrate was apolipoprotein A-I (apoA-I), a major component of high-density lipoprotein (HDL). In vitro cleavage assays showed that lipid-free apoA-I is a more accessible substrate for MMP-14 compared to lipid-bound apoA-I, and that MMP-14 is more prone to digest apoA-I than MMP-3. The 28-kDa apoA-I was cleaved into smaller fragments of 27, 26, 25, 22, and 14-kDa by MMP-14. ApoA-I sites cleaved by MMP-14 were determined by isotope labeling of C-termini derived from the cleavage and analysis of the labeled peptides by mass spectrometry, along with N-terminal sequencing of the fragments. Cleavage of apoA-I by MMP-14 resulted in a loss of ability to form HDL Our results suggest that cleavage of lipid-free apoA-I by MMP-14 may contribute to reduced HDL formation, and this may be occurring during the development of various vascular diseases as lipid metabolism is disrupted. (C) 2011 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/25225http://dx.doi.org/10.1016/j.bbrc.2011.04.105
ISSN
0006-291X
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