Apolipoprotein A-IV is a novel substrate for matrix metalloproteinases

Title
Apolipoprotein A-IV is a novel substrate for matrix metalloproteinases
Author(s)
조경현이승택[이승택]장욱주박지윤[박지윤]박준형[박준형]황인관[황인관]김인자[김인자]김화정[김화정]
Keywords
HIGH-DENSITY-LIPOPROTEIN; HUMAN PLASMA; N-TERMINI; C-TERMINI; CLEAVAGE; ACTIVATION; MATRILYSIN; BINDING; GROWTH; CANCER
Issue Date
201203
Publisher
OXFORD UNIV PRESS
Citation
JOURNAL OF BIOCHEMISTRY, v.151, no.3, pp.291 - 298
Abstract
Screening of matrix metalloproteinase (MMP)-14 substrates in human plasma using a proteomics approach previously identified apolipoprotein A-IV (apoA-IV) as a novel substrate for MMP-14. Here, we show that among the tested MMPs, purified apoA-IV is most susceptible to cleavage by MMP-7, and that apoA-IV in plasma can be cleaved more efficiently by MMP-7 than MMP-14. Purified recombinant apoA-IV (44-kDa) was cleaved by MMP-7 into several fragments of 41, 32, 29, 27, 24, 22 and 19 kDa. N-terminal sequencing of the fragments identified two internal cleavage sites for MMP-7 in the apoA-IV sequence, between Glu(185) and Leu(186), and between Glu(262) and Leu(263). The cleavage of lipid-bound apoA-IV by MMP-7 was less efficient than that of lipid-free apoA-IV. Further, MMP-7-mediated cleavage of apoA-IV resulted in a rapid loss of its intrinsic anti-oxidant activity. Based on the fact that apoA-IV plays important roles in lipid metabolism and possesses anti-oxidant activity, we suggest that cleavage of lipid-free apoA-IV by MMP-7 has pathological implications in the development of hyperlipidemia and atherosclerosis.
URI
http://hdl.handle.net/YU.REPOSITORY/29595http://dx.doi.org/10.1093/jb/mvr137
ISSN
0021-924X
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