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Electrophilic fatty acids regulate matrix metalloproteinase activity and expression

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Electrophilic fatty acids regulate matrix metalloproteinase activity and expression. / Bonacci, Gustavo; Schopfer, Francisco J; Batthyany, Carlos I; Rudolph, Tanja K; Rudolph, Volker; Khoo, Nicholas K H; Kelley, Eric E; Freeman, Bruce A.

In: J BIOL CHEM, Vol. 286, No. 18, 06.05.2011, p. 16074-16081.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Bonacci, G, Schopfer, FJ, Batthyany, CI, Rudolph, TK, Rudolph, V, Khoo, NKH, Kelley, EE & Freeman, BA 2011, 'Electrophilic fatty acids regulate matrix metalloproteinase activity and expression', J BIOL CHEM, vol. 286, no. 18, pp. 16074-16081. https://doi.org/10.1074/jbc.M111.225029

APA

Bonacci, G., Schopfer, F. J., Batthyany, C. I., Rudolph, T. K., Rudolph, V., Khoo, N. K. H., Kelley, E. E., & Freeman, B. A. (2011). Electrophilic fatty acids regulate matrix metalloproteinase activity and expression. J BIOL CHEM, 286(18), 16074-16081. https://doi.org/10.1074/jbc.M111.225029

Vancouver

Bonacci G, Schopfer FJ, Batthyany CI, Rudolph TK, Rudolph V, Khoo NKH et al. Electrophilic fatty acids regulate matrix metalloproteinase activity and expression. J BIOL CHEM. 2011 May 6;286(18):16074-16081. https://doi.org/10.1074/jbc.M111.225029

Bibtex

@article{b8f662dd35a24588aaa38f6d745b4f57,
title = "Electrophilic fatty acids regulate matrix metalloproteinase activity and expression",
abstract = "Nitro-fatty acids (NO(2)-FA) are electrophilic signaling mediators formed by reactions of nitric oxide and nitrite. NO(2)-FA exert anti-inflammatory signaling actions through post-translational protein modifications. We report that nitro-oleic acid (OA-NO(2)) stimulates proMMP-7 and proMMP-9 proteolytic activity via adduction of the conserved cysteine switch domain thiolate. Biotin-labeled OA-NO(2) showed this adduction occurs preferentially with latent forms of MMP, confirming a role for thiol alkylation by OA-NO(2) in MMP activation. In addition to regulating pro-MMP activation, MMP expression was modulated by OA-NO(2) via activation of peroxisome proliferator-activated receptor-γ. MMP-9 transcription was decreased in phorbol 12-myristate 13-acetate-stimulated THP-1 macrophages to an extent similar to that induced by the peroxisome proliferator-activated receptor-γ agonist Rosiglitazone. This was affirmed using a murine model of atherosclerosis, ApoE(-/-) mice, where in vivo OA-NO(2) administration suppressed MMP expression in atherosclerotic lesions. These findings reveal that electrophilic fatty acid derivatives can serve as effectors during inflammation, first by activating pro-MMP proteolytic activity via alkylation of the cysteine switch domain, and then by transcriptionally inhibiting MMP expression, thereby limiting the further progression of inflammatory processes.",
keywords = "Animals, Carcinogens/pharmacology, Cell Line, Enzyme Activation/drug effects, Enzyme Precursors/biosynthesis, Gene Expression Regulation, Enzymologic, Humans, Hypoglycemic Agents/pharmacology, Inflammation/enzymology, Matrix Metalloproteinase 9/biosynthesis, Metalloendopeptidases/biosynthesis, Mice, Mice, Knockout, Oleic Acids/metabolism, PPAR gamma/antagonists & inhibitors, Protein Structure, Tertiary, Rosiglitazone, Tetradecanoylphorbol Acetate/pharmacology, Thiazolidinediones/pharmacology, Transcription, Genetic/drug effects",
author = "Gustavo Bonacci and Schopfer, {Francisco J} and Batthyany, {Carlos I} and Rudolph, {Tanja K} and Volker Rudolph and Khoo, {Nicholas K H} and Kelley, {Eric E} and Freeman, {Bruce A}",
year = "2011",
month = may,
day = "6",
doi = "10.1074/jbc.M111.225029",
language = "English",
volume = "286",
pages = "16074--16081",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "18",

}

RIS

TY - JOUR

T1 - Electrophilic fatty acids regulate matrix metalloproteinase activity and expression

AU - Bonacci, Gustavo

AU - Schopfer, Francisco J

AU - Batthyany, Carlos I

AU - Rudolph, Tanja K

AU - Rudolph, Volker

AU - Khoo, Nicholas K H

AU - Kelley, Eric E

AU - Freeman, Bruce A

PY - 2011/5/6

Y1 - 2011/5/6

N2 - Nitro-fatty acids (NO(2)-FA) are electrophilic signaling mediators formed by reactions of nitric oxide and nitrite. NO(2)-FA exert anti-inflammatory signaling actions through post-translational protein modifications. We report that nitro-oleic acid (OA-NO(2)) stimulates proMMP-7 and proMMP-9 proteolytic activity via adduction of the conserved cysteine switch domain thiolate. Biotin-labeled OA-NO(2) showed this adduction occurs preferentially with latent forms of MMP, confirming a role for thiol alkylation by OA-NO(2) in MMP activation. In addition to regulating pro-MMP activation, MMP expression was modulated by OA-NO(2) via activation of peroxisome proliferator-activated receptor-γ. MMP-9 transcription was decreased in phorbol 12-myristate 13-acetate-stimulated THP-1 macrophages to an extent similar to that induced by the peroxisome proliferator-activated receptor-γ agonist Rosiglitazone. This was affirmed using a murine model of atherosclerosis, ApoE(-/-) mice, where in vivo OA-NO(2) administration suppressed MMP expression in atherosclerotic lesions. These findings reveal that electrophilic fatty acid derivatives can serve as effectors during inflammation, first by activating pro-MMP proteolytic activity via alkylation of the cysteine switch domain, and then by transcriptionally inhibiting MMP expression, thereby limiting the further progression of inflammatory processes.

AB - Nitro-fatty acids (NO(2)-FA) are electrophilic signaling mediators formed by reactions of nitric oxide and nitrite. NO(2)-FA exert anti-inflammatory signaling actions through post-translational protein modifications. We report that nitro-oleic acid (OA-NO(2)) stimulates proMMP-7 and proMMP-9 proteolytic activity via adduction of the conserved cysteine switch domain thiolate. Biotin-labeled OA-NO(2) showed this adduction occurs preferentially with latent forms of MMP, confirming a role for thiol alkylation by OA-NO(2) in MMP activation. In addition to regulating pro-MMP activation, MMP expression was modulated by OA-NO(2) via activation of peroxisome proliferator-activated receptor-γ. MMP-9 transcription was decreased in phorbol 12-myristate 13-acetate-stimulated THP-1 macrophages to an extent similar to that induced by the peroxisome proliferator-activated receptor-γ agonist Rosiglitazone. This was affirmed using a murine model of atherosclerosis, ApoE(-/-) mice, where in vivo OA-NO(2) administration suppressed MMP expression in atherosclerotic lesions. These findings reveal that electrophilic fatty acid derivatives can serve as effectors during inflammation, first by activating pro-MMP proteolytic activity via alkylation of the cysteine switch domain, and then by transcriptionally inhibiting MMP expression, thereby limiting the further progression of inflammatory processes.

KW - Animals

KW - Carcinogens/pharmacology

KW - Cell Line

KW - Enzyme Activation/drug effects

KW - Enzyme Precursors/biosynthesis

KW - Gene Expression Regulation, Enzymologic

KW - Humans

KW - Hypoglycemic Agents/pharmacology

KW - Inflammation/enzymology

KW - Matrix Metalloproteinase 9/biosynthesis

KW - Metalloendopeptidases/biosynthesis

KW - Mice

KW - Mice, Knockout

KW - Oleic Acids/metabolism

KW - PPAR gamma/antagonists & inhibitors

KW - Protein Structure, Tertiary

KW - Rosiglitazone

KW - Tetradecanoylphorbol Acetate/pharmacology

KW - Thiazolidinediones/pharmacology

KW - Transcription, Genetic/drug effects

U2 - 10.1074/jbc.M111.225029

DO - 10.1074/jbc.M111.225029

M3 - SCORING: Journal article

C2 - 21454668

VL - 286

SP - 16074

EP - 16081

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 18

ER -