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Analysis of Apolipoprotein A-I as a Substrate for Matrix metalloproteinase-14

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

Biochem Biophys Res Commun. 2011 May 27;409(1):58-63.

PMID: 21549099

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241292	MMP 14 (Stomelysin-3) Substrate			Price

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