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

Jun Hyoung Park, Sung Min Park, Ki Hoon Park, Kyung Hyun Cho, Seung Taek Lee

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10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)58-63
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2011 May 27

Bibliographical note

Funding Information:
This work was supported by Grants from the Korea Science and Engineering Foundation through the project for Studies on Ubiquitome Functions ( 2005-2001143 to S.-T.L.) and the Mid-Career Researcher Program ( 2010-0026103 to S.-T.L.), and from the 2011 Yonsei University Research Fund. Jun Hyoung Park was a pre-doctoral trainee of the Brain Korea 21 program (Ministry of Education, Science, and Technology, Republic of Korea).

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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