Abstract

CorrigendumCorrigendumPublished Online:15 Oct 2014https://doi.org/10.1152/ajpcell.zh0-7613-corr.2014Original articleMoreSectionsPDF (663 KB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInEmailWeChat Volume 298, March 1, 2010Volume 67, March 1, 2010Awad AE, Kandalam V, Chakrabarti S, Wang X, Penninger JM, Davidge ST, Oudit GY, Kassiri Z. Tumor necrosis factor induces matrix metalloproteinases in cardiomyocytes and cardiofibroblasts differentially via superoxide production in a PI3Kγ-dependent manner. Am J Physiol Cell Physiol 298: C679–C692, 2010. First published December 9, 2009; doi: 10.1152/ajpcell.00351.2009. In results, Figs. 3, 5, and 8 were incorrect. The zymogram gel loading controls presented in Figs. 3A and 5C have been replaced with Coomassie blue-stained gel loading controls from the same experiments to correct errors identified in the images originally presented. Figure 8A has been revised to declare that the lanes presented are not contiguous. Legends to the figures have been updated to address these changes. The corrections do not alter the conclusions of this study. The corrected figures are shown below. Fig. 3.TNF stimulates expression of matrix metalloproteinase (MMP)9, but not MMP2, in a superoxide-dependent fashion. A: gelatin zymography on cell homogenates and conditioned media from WT cardiomyocyte and cardiofibroblast control, rTNF-, or rTNF + apocynin-treated groups after 1 h (i) or 24 h (ii). Averaged band intensities for MMP9 are presented as bar graphs for control (white), rTNF (black), and rTNF + apocynin (horizontal hatch). Coomassie blue-stained parallel gels, using the same protein samples and dilution as in the zymograms, were used as the loading controls. B: MMP9 mRNA levels measured by Taqman RT-PCR in cardiomyocytes and cardiofibroblasts treated as in A. *P < 0.05 compared with all other groups. #P < 0.05 compared with rTNF-treated group. Ctrl, control; rTNF, recombinant TNF; APO, apocynin; MW, molecular weight. RE, relative expression.Download figureDownload PowerPointFig. 5.TNF-mediated superoxide production and MMP activation is ablated in phosphatidylinositol 3-kinase (PI3K)γ−/− neonatal mouse cardiomyocytes and cardiofibroblasts. A: lucigenin chemiluminescence assay in WT and PI3Kγ−/− cultures before and after 1 h or 24 h of rTNF treatment. Values were normalized to the control within each group. B: representative images of DHE-stained PI3Kγ−/− cultures and the corresponding counterstained nuclei. Bar graphs show averaged superoxide levels for each group (n = 12 fields/group). C: gelatin zymography in PI3Kγ−/− cardiomyocytes (i) and cardiofibroblasts (ii) after 24 h of rTNF treatment. Coomassie blue-stained parallel gels, using the same protein samples and dilution as in the zymograms, were used as the loading controls. D: mRNA expression of MMP9 in WT and PI3Kγ−/− cardiomyocytes and cardiofibroblasts. Values were normalized to the control group within each genotype. E: total collagenase activity in PI3Kγ−/− compared with WT cultures. *P < 0.05 compared with the control group within each genotype. #P < 0.05 compared with WT-rTNF group. MFI, mean fluorescent intensity. RE, relative expression.Download figureDownload PowerPointFig. 8.PI3K activity is suppressed in TNF−/− mice following pressure overload. A: representative Western blots showing PI3Kγ (i) and protein loading controls α-tubulin (ii) and Coomassie blue staining (iii) in WT and TNF−/− mice after sham operation or 10 wk post-TAC. All samples were run on the same gel but lanes were removed for final presentation as indicated by the space inserted at the splice sites. B: averaged PI3Kγ protein levels normalized to corresponding α-tubulin in WT and TNF−/− mice post-TAC (n = 4). C: PI3K activity in WT and TNF−/− mice following TAC (n = 6). *P < 0.05 compared with corresponding sham. #P < 0.05 compared with WT-TAC. AU, arbitrary units.Download figureDownload PowerPointThis article has no references to display. Download PDF Previous Back to Top FiguresReferencesRelatedInformationRelated ArticlesTumor necrosis factor induces matrix metalloproteinases in cardiomyocytes and cardiofibroblasts differentially via superoxide production in a PI3Kγ-dependent manner 01 Mar 2010American Journal of Physiology-Cell Physiology More from this issue > Volume 307Issue 8October 2014Pages C760-C762 Copyright & PermissionsCopyright © 2014 the American Physiological Societyhttps://doi.org/10.1152/ajpcell.zh0-7613-corr.2014History Published online 15 October 2014 Published in print 15 October 2014 Metrics

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.