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Apolipoprotein A-IV is a novel substrate for matrix metalloproteinases

Title
Apolipoprotein A-IV is a novel substrate for matrix metalloproteinases
Authors
Park J.Y.Park J.H.Jang W.Hwang I.-K.Kim I.J.Kim H.-J.Cho K.-H.Lee S.-T.
Ewha Authors
김화정
SCOPUS Author ID
김화정scopus
Issue Date
2012
Journal Title
Journal of Biochemistry
ISSN
0021-924XJCR Link
Citation
vol. 151, no. 3, pp. 291 - 298
Indexed
SCI; SCIE; SCOPUS WOS scopus
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. © 2011 The Authors.
DOI
10.1093/jb/mvr137
Appears in Collections:
약학대학 > 약학과 > Journal papers
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