View : 25 Download: 0
Apolipoprotein A-IV is a novel substrate for matrix metalloproteinases
- Apolipoprotein A-IV is a novel substrate for matrix metalloproteinases
- 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
- SCOPUS Author ID
- Issue Date
- Journal Title
- Journal of Biochemistry
- vol. 151, no. 3, pp. 291 - 298
- SCI; SCIE; SCOPUS
- 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.
- Appears in Collections:
- 약학대학 > 약학과 > Journal papers
- Files in This Item:
There are no files associated with this item.
- RIS (EndNote)
- XLS (Excel)
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.