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Molecular Mechanism of Transcriptional Regulation of Matrix Metalloproteinase-9 in Diabetic Retinopathy.

Abstract Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary cell apoptosis, a phenomenon which precedes the development of diabetic retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional factors, including two for activator protein 1 (AP-1). The binding of AP-1, a heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to investigate the molecular mechanism of MMP-9 transcriptional regulation in diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1 acetylation were analyzed in retinal endothelial cells incubated in normal or high glucose by chromatin-immunoprecipitation and co-immunoprecipitation respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results were validated in the retina from diabetic mice overexpressing Sirt1, and in the retinal microvessels from human donors with diabetic retinopathy. In experimental models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 promoter, and similar phenomenon was confirmed in the retinal microvessels from human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated, which increases its binding at MMP-9 promoter, and hence, activation of Sirt1 could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. ? 2015 Wiley Periodicals, Inc.
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Authors

Mayor MeshTerms
Keywords
Journal Title journal of cellular physiology
Publication Year Start
%A Mishra, Manish; Flaga, Jadwiga; Kowluru, Renu A.
%T Molecular Mechanism of Transcriptional Regulation of Matrix Metalloproteinase-9 in Diabetic Retinopathy.
%J Journal of cellular physiology, vol. 231, no. 8, pp. 1709-1718
%D 08/2016
%V 231
%N 8
%M eng
%B Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary cell apoptosis, a phenomenon which precedes the development of diabetic retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional factors, including two for activator protein 1 (AP-1). The binding of AP-1, a heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to investigate the molecular mechanism of MMP-9 transcriptional regulation in diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1 acetylation were analyzed in retinal endothelial cells incubated in normal or high glucose by chromatin-immunoprecipitation and co-immunoprecipitation respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results were validated in the retina from diabetic mice overexpressing Sirt1, and in the retinal microvessels from human donors with diabetic retinopathy. In experimental models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 promoter, and similar phenomenon was confirmed in the retinal microvessels from human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated, which increases its binding at MMP-9 promoter, and hence, activation of Sirt1 could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. ? 2015 Wiley Periodicals, Inc.
%P 1709
%L 1718
%Y 10.1002/jcp.25268
%W PHY
%G AUTHOR
%R 2016......231.1709M

@Article{Mishra2016,
author="Mishra, Manish
and Flaga, Jadwiga
and Kowluru, Renu A.",
title="Molecular Mechanism of Transcriptional Regulation of Matrix Metalloproteinase-9 in Diabetic Retinopathy.",
journal="Journal of cellular physiology",
year="2016",
month="Aug",
day="22",
volume="231",
number="8",
pages="1709--1718",
abstract="Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary cell apoptosis, a phenomenon which precedes the development of diabetic retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional factors, including two for activator protein 1 (AP-1). The binding of AP-1, a heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to investigate the molecular mechanism of MMP-9 transcriptional regulation in diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1 acetylation were analyzed in retinal endothelial cells incubated in normal or high glucose by chromatin-immunoprecipitation and co-immunoprecipitation respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results were validated in the retina from diabetic mice overexpressing Sirt1, and in the retinal microvessels from human donors with diabetic retinopathy. In experimental models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 promoter, and similar phenomenon was confirmed in the retinal microvessels from human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated, which increases its binding at MMP-9 promoter, and hence, activation of Sirt1 could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. {\textcopyright} 2015 Wiley Periodicals, Inc.",
issn="1097-4652",
doi="10.1002/jcp.25268",
url="http://www.ncbi.nlm.nih.gov/pubmed/26599598",
language="eng"
}

%0 Journal Article
%T Molecular Mechanism of Transcriptional Regulation of Matrix Metalloproteinase-9 in Diabetic Retinopathy.
%A Mishra, Manish
%A Flaga, Jadwiga
%A Kowluru, Renu A.
%J Journal of cellular physiology
%D 2016
%8 Aug 22
%V 231
%N 8
%@ 1097-4652
%G eng
%F Mishra2016
%X Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary cell apoptosis, a phenomenon which precedes the development of diabetic retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional factors, including two for activator protein 1 (AP-1). The binding of AP-1, a heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to investigate the molecular mechanism of MMP-9 transcriptional regulation in diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1 acetylation were analyzed in retinal endothelial cells incubated in normal or high glucose by chromatin-immunoprecipitation and co-immunoprecipitation respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results were validated in the retina from diabetic mice overexpressing Sirt1, and in the retinal microvessels from human donors with diabetic retinopathy. In experimental models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 promoter, and similar phenomenon was confirmed in the retinal microvessels from human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated, which increases its binding at MMP-9 promoter, and hence, activation of Sirt1 could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. ? 2015 Wiley Periodicals, Inc.
%U http://dx.doi.org/10.1002/jcp.25268
%U http://www.ncbi.nlm.nih.gov/pubmed/26599598
%P 1709-1718

PT Journal
AU Mishra, M
   Flaga, J
   Kowluru, RA
TI Molecular Mechanism of Transcriptional Regulation of Matrix Metalloproteinase-9 in Diabetic Retinopathy.
SO Journal of cellular physiology
JI J. Cell. Physiol.
PD Aug
PY 2016
BP 1709
EP 1718
VL 231
IS 8
DI 10.1002/jcp.25268
LA eng
AB Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary cell apoptosis, a phenomenon which precedes the development of diabetic retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional factors, including two for activator protein 1 (AP-1). The binding of AP-1, a heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to investigate the molecular mechanism of MMP-9 transcriptional regulation in diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1 acetylation were analyzed in retinal endothelial cells incubated in normal or high glucose by chromatin-immunoprecipitation and co-immunoprecipitation respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results were validated in the retina from diabetic mice overexpressing Sirt1, and in the retinal microvessels from human donors with diabetic retinopathy. In experimental models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 promoter, and similar phenomenon was confirmed in the retinal microvessels from human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated, which increases its binding at MMP-9 promoter, and hence, activation of Sirt1 could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. ? 2015 Wiley Periodicals, Inc.
ER

PMID- 26599598
OWN - NLM
STAT- In-Data-Review
DA  - 20160419
IS  - 1097-4652 (Electronic)
IS  - 0021-9541 (Linking)
VI  - 231
IP  - 8
DP  - 2016 Aug
TI  - Molecular Mechanism of Transcriptional Regulation of Matrix Metalloproteinase-9
      in Diabetic Retinopathy.
PG  - 1709-18
LID - 10.1002/jcp.25268 [doi]
AB  - Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary
      cell apoptosis, a phenomenon which precedes the development of diabetic
      retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional
      factors, including two for activator protein 1 (AP-1). The binding of AP-1, a
      heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, 
      and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to
      investigate the molecular mechanism of MMP-9 transcriptional regulation in
      diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1
      acetylation were analyzed in retinal endothelial cells incubated in normal or
      high glucose by chromatin-immunoprecipitation and co-immunoprecipitation
      respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos
      siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results
      were validated in the retina from diabetic mice overexpressing Sirt1, and in the 
      retinal microvessels from human donors with diabetic retinopathy. In experimental
      models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 
      promoter, and similar phenomenon was confirmed in the retinal microvessels from
      human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of
      Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell
      apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated,
      which increases its binding at MMP-9 promoter, and hence, activation of Sirt1
      could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated 
      mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. (c) 2015 Wiley
      Periodicals, Inc.
CI  - (c) 2015 Wiley Periodicals, Inc.
FAU - Mishra, Manish
AU  - Mishra M
AD  - Department of Ophthalmology, Kresge Eye Institute, Wayne State University,
      Detroit, Michigan.
FAU - Flaga, Jadwiga
AU  - Flaga J
AD  - Department of Ophthalmology, Kresge Eye Institute, Wayne State University,
      Detroit, Michigan.
FAU - Kowluru, Renu A
AU  - Kowluru RA
AD  - Department of Ophthalmology, Kresge Eye Institute, Wayne State University,
      Detroit, Michigan.
LA  - eng
PT  - Journal Article
DEP - 20151222
PL  - United States
TA  - J Cell Physiol
JT  - Journal of cellular physiology
JID - 0050222
SB  - IM
EDAT- 2015/11/26 06:00
MHDA- 2015/11/26 06:00
CRDT- 2015/11/25 06:00
PHST- 2015/07/22 [received]
PHST- 2015/11/23 [accepted]
PHST- 2015/12/22 [aheadofprint]
AID - 10.1002/jcp.25268 [doi]
PST - ppublish
SO  - J Cell Physiol. 2016 Aug;231(8):1709-18. doi: 10.1002/jcp.25268. Epub 2015 Dec
      22.
TY  - JOUR
AU  - Mishra, Manish
AU  - Flaga, Jadwiga
AU  - Kowluru, Renu A.
PY  - 2016/Aug/22
TI  - Molecular Mechanism of Transcriptional Regulation of Matrix Metalloproteinase-9 in Diabetic Retinopathy.
T2  - J. Cell. Physiol.
JO  - Journal of cellular physiology
SP  - 1709
EP  - 1718
VL  - 231
IS  - 8
N2  - Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary cell apoptosis, a phenomenon which precedes the development of diabetic retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional factors, including two for activator protein 1 (AP-1). The binding of AP-1, a heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to investigate the molecular mechanism of MMP-9 transcriptional regulation in diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1 acetylation were analyzed in retinal endothelial cells incubated in normal or high glucose by chromatin-immunoprecipitation and co-immunoprecipitation respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results were validated in the retina from diabetic mice overexpressing Sirt1, and in the retinal microvessels from human donors with diabetic retinopathy. In experimental models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 promoter, and similar phenomenon was confirmed in the retinal microvessels from human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated, which increases its binding at MMP-9 promoter, and hence, activation of Sirt1 could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. ? 2015 Wiley Periodicals, Inc.
SN  - 1097-4652
UR  - http://dx.doi.org/10.1002/jcp.25268
UR  - http://www.ncbi.nlm.nih.gov/pubmed/26599598
ID  - Mishra2016
ER  - 
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<b:Comments>Increase in matrix metalloproteinase-9 (MMP-9) is implicated in retinal capillary cell apoptosis, a phenomenon which precedes the development of diabetic retinopathy. MMP-9 promoter has multiple sites for binding the transcriptional factors, including two for activator protein 1 (AP-1). The binding of AP-1, a heterodimer of c-Jun and c-Fos, is regulated by posttranslational modifications, and in diabetes, deacetylating enzyme, Sirt1, is inhibited. Our aim, is to investigate the molecular mechanism of MMP-9 transcriptional regulation in diabetes. Binding of AP-1 (c-Jun, c-Fos) at the MMP-9 promoter, and AP-1 acetylation were analyzed in retinal endothelial cells incubated in normal or high glucose by chromatin-immunoprecipitation and co-immunoprecipitation respectively. Role of AP-1 in MMP-9 regulation was confirmed by c-Jun or c-Fos siRNAs, and that of its acetylation, by Sirt1 overexpression. In vitro results were validated in the retina from diabetic mice overexpressing Sirt1, and in the retinal microvessels from human donors with diabetic retinopathy. In experimental models, AP-1 binding was increased at the proximal and distal sites of the MMP-9 promoter, and similar phenomenon was confirmed in the retinal microvessels from human donors with diabetic retinopathy. Silencing of AP-1, or overexpression of Sirt1 ameliorated glucose-induced increase in MMP-9 expression and cell apoptosis. Thus, in diabetes, due to Sirt1 inhibition, AP-1 is hyperacetylated, which increases its binding at MMP-9 promoter, and hence, activation of Sirt1 could inhibit the development of diabetic retinopathy by impeding MMP-9-mediated mitochondrial damage. J. Cell. Physiol. 231: 1709-1718, 2016. &#169; 2015 Wiley Periodicals, Inc.</b:Comments>
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