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

doi:10.1016/j.bbrc.2011.04.105

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

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

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.

Original language	English
Pages (from-to)	58-63
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	409
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2011.04.105
Publication status	Published - 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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.bbrc.2011.04.105

Cite this

@article{de2689e873194683b23d40c2ccea0647,

title = "Analysis of apolipoprotein A-I as a substrate for matrix metalloproteinase-14",

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.",

author = "Park, {Jun Hyoung} and Park, {Sung Min} and Park, {Ki Hoon} and Cho, {Kyung Hyun} and Lee, {Seung Taek}",

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). ",

year = "2011",

month = may,

day = "27",

doi = "10.1016/j.bbrc.2011.04.105",

language = "English",

volume = "409",

pages = "58--63",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Analysis of apolipoprotein A-I as a substrate for matrix metalloproteinase-14

AU - Park, Jun Hyoung

AU - Park, Sung Min

AU - Park, Ki Hoon

AU - Cho, Kyung Hyun

AU - Lee, Seung Taek

N1 - 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).

PY - 2011/5/27

Y1 - 2011/5/27

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=79956213354&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79956213354&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2011.04.105

DO - 10.1016/j.bbrc.2011.04.105

M3 - Article

C2 - 21549099

AN - SCOPUS:79956213354

SN - 0006-291X

VL - 409

SP - 58

EP - 63

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

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

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this