Apolipoprotein C-II is a novel substrate for matrix metalloproteinases

Se Yeon Kim, Sung Min Park, Seung-Taek Lee

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

We previously reported an efficient proteomic approach to identify matrix metalloproteinase (MMP) substrates from complex protein mixture. Using the proteomic approach, apolipoprotein C-II (apoC-II), which is a cofactor of lipoprotein lipase (LPL) and a component of very-low density lipoprotein and chylomicron, has been identified as a putative MMP-14 substrate. Cleavage of apoC-II, with various MMPs, demonstrated that apoC-II is cleaved most efficiently by MMP-14, and also by MMP-7, among the tested MMPs. The 79-amino acid residue apoC-II was cleaved between Asn35 and Leu36 by MMP-14, and between Phe14 and Leu15 and between Asn35 and Leu36 by MMP-7. Cleavage of apoC-II by MMP-14 markedly decreased LPL activity and would thus impair hydrolysis of triglycerides in plasma and transfer of fatty acids to tissues. Our result suggests that cleavage of apoC-II by MMPs would be important for development of pathophysiological situations of apoC-II deficiency such as atherosclerosis.

Original languageEnglish
Pages (from-to)47-54
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume339
Issue number1
DOIs
Publication statusPublished - 2006 Jan 6

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Apolipoprotein C-II
Matrix Metalloproteinases
Matrix Metalloproteinase 14
Substrates
Matrix Metalloproteinase 7
Lipoprotein Lipase
Proteomics
Hyperlipoproteinemia Type I
Chylomicrons
Lipoprotein(a)
VLDL Lipoproteins
Complex Mixtures
Atherosclerosis
Triglycerides
Hydrolysis
Fatty Acids
Amino Acids
Tissue
Plasmas

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "We previously reported an efficient proteomic approach to identify matrix metalloproteinase (MMP) substrates from complex protein mixture. Using the proteomic approach, apolipoprotein C-II (apoC-II), which is a cofactor of lipoprotein lipase (LPL) and a component of very-low density lipoprotein and chylomicron, has been identified as a putative MMP-14 substrate. Cleavage of apoC-II, with various MMPs, demonstrated that apoC-II is cleaved most efficiently by MMP-14, and also by MMP-7, among the tested MMPs. The 79-amino acid residue apoC-II was cleaved between Asn35 and Leu36 by MMP-14, and between Phe14 and Leu15 and between Asn35 and Leu36 by MMP-7. Cleavage of apoC-II by MMP-14 markedly decreased LPL activity and would thus impair hydrolysis of triglycerides in plasma and transfer of fatty acids to tissues. Our result suggests that cleavage of apoC-II by MMPs would be important for development of pathophysiological situations of apoC-II deficiency such as atherosclerosis.",
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Apolipoprotein C-II is a novel substrate for matrix metalloproteinases. / Kim, Se Yeon; Park, Sung Min; Lee, Seung-Taek.

In: Biochemical and Biophysical Research Communications, Vol. 339, No. 1, 06.01.2006, p. 47-54.

Research output: Contribution to journalArticle

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