The Experts below are selected from a list of 39 Experts worldwide ranked by ideXlab platform
Suresh C Tyagi - One of the best experts on this subject based on the ideXlab platform.
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extracellular matrix regulation of metalloproteinase and antiproteinase in human Heart Fibroblast cells
Journal of Cellular Physiology, 1996Co-Authors: Suresh C Tyagi, Suresh G Kumar, Srinivasa R Alla, Hanumanth K Reddy, Donald J Voelker, Joseph S JanickiAbstract:Following myocardial infarction, extracellular matrix (ECM) is disrupted, which leads to the generation of collagen- and elastin-derived peptides (CDPs and EDPs, respectively). To investigate whether ECM-derived peptides (i.e., CDPs and EDPs) induce extracellular proteinases in human Heart Fibroblast (HHF) cells, we isolated CDP and EDP using gelfiltration and antibody affinity column chromatography. The CDP and EDP were characterized by their intrinsic fluorescence due to cross-link structure (pyridinoline and desmosine, respectively) and by immunoblot analysis using anti-desmosine antibody. Neutrophil elastase and cathepsin G were identified using selective chromogenic substrates and by their specific inhibition with α1-proteinase inhibitor and α1-antichymotrypsin, respectively. Elastase and cathepsin G were elevated in the infarcted tissue. Selective inhibition of matrix metalloproteinase (MMP) by a higher concentration of tetracycline or doxycycline in zymographic gels elicited an inhibition constant (IC50) of 278 ± 10 μM and indicated that majority of MMP in the infarcted tissue is from Fibroblast cells. The HHF proliferation was measured using an acid-phosphatase assay. The EDP and CDP induce HHF cell proliferation. After EDP treatment phenotypic (formation of pseudopodia) changes were observed in HHF cells. To measure whether phenotypic changes by EDP or CDP are associated with MMP and tissue inhibitor of metalloproteinase (TIMP) expression in HHF cells, we measured MMP and TIMP expression by zymographic and Northern blot (mRNA) analyses. The expression of MMP and TIMP were upregulated at both the protein and gene transcription levels. These results suggested that during ischemic cardiomyopathy, initially neutrophil proteinase activates latent myocardial MMP which can degrade ECM, which continuously degrades if not controlled by TIMP, leading to ventricular dilatation and dysfunction. © 1996 Wiley-Liss, Inc.
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induction of tissue inhibitor and matrix metalloproteinase by serum in human Heart derived Fibroblast and endomyocardial endothelial cells
Journal of Cellular Biochemistry, 1995Co-Authors: Suresh C Tyagi, Suresh G Kumar, Geraldine GloverAbstract:To understand the regulatory mechanisms of extracellular matrix (ECM) turnover and proteinase expression in human cardiovascular tissue, we have isolated and characterized human Heart Fibroblast (HHF) and human Heart endothelial (HHE) cells from endomyocardial biopsy specimens. HHE cell in culture exhibited the typical cobblestone growth pattern and positive immunofluorescent staining for factor Vlll related antigen. HHF demonstrated the typical spindle shape during culture and were positive for vimentin. Both cell types were negative for a-actin, indicating that these cells were of nonmuscle origin. Cell growth studies revealed significant growth when maintained in limiting serum concentration, suggesting mitogenic activity of these cells, and demonstrated growth inhibitory activity when grown in serum-free medium. Serum-dependent matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) expression was measured by zymography, immunoblot, and Northern blot analysis. Results indicated that serum induces both the MMP and TlMP expression at the mRNA and protein levels in a dose-dependent manner. This induction was inhibited by actinomycin D and cycloheximide, suggesting transcriptional and translational regulation of MMP and TIMP. Indirect immunofluorescence labeling indicated expression of MMP and TlMP in HHF and HHE cells. These results suggested that the serum induces proliferation as well as expression of MMP and TlMP in HHE and HHF cells. The growth inhibitory activity of these cell cultures will enable us to explore further the nature of this response and compare this phenomenon with other growth inhibitors and growth promoters identified in other normal and transformed cells.
Joseph S Janicki - One of the best experts on this subject based on the ideXlab platform.
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Effects of mast cells on the behavior of isolated Heart Fibroblasts: modulation of collagen remodeling and gene expression.
Journal of Cellular Physiology, 2002Co-Authors: Angela De Almeida, Joseph S Janicki, Deanna Mustin, Mary F. Forman, Gregory L. Brower, Wayne CarverAbstract:The extracellular matrix plays a critical role in the development and maintenance of the vertebrate Heart. Changes in the accumulation, composition, or organization of the extracellular matrix are known to deleteriously affect Heart function. Mast cells are thought to stimulate collagen expression and Fibroblast proliferation accompanying fibrosis in some organs; however, the effects of mast cells on the Heart interstitium are largely unexplored. The present studies were carried out to determine the effects of mast cells on isolated Heart Fibroblasts. Several in vitro assays were used including collagen gel contraction to examine the effects of mast cells on the function of isolated Fibroblasts. Neonatal Heart Fibroblasts were cultured either with mast cells, mast cell-conditioned medium, or mast cell extracts, and their ability to contract collagen gels measured. Results from these experiments indicated that mast cells inhibit Heart Fibroblast migration and contraction of 3-dimensional collagen gels. Further experiments indicated that incubation of neonatal Heart Fibroblasts with extracts of mast cells altered the expression of collagen, matrix metalloproteases, and matrix receptors of the integrin family. These studies suggest that mast cells play an important role in the regulation of the cardiac interstitial matrix. Further studies are warranted to determine the mechanisms whereby mast cells modulate Fibroblast activity. J. Cell. Physiol. 191: 51–59, 2002. © 2002 Wiley-Liss, Inc.
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extracellular matrix regulation of metalloproteinase and antiproteinase in human Heart Fibroblast cells
Journal of Cellular Physiology, 1996Co-Authors: Suresh C Tyagi, Suresh G Kumar, Srinivasa R Alla, Hanumanth K Reddy, Donald J Voelker, Joseph S JanickiAbstract:Following myocardial infarction, extracellular matrix (ECM) is disrupted, which leads to the generation of collagen- and elastin-derived peptides (CDPs and EDPs, respectively). To investigate whether ECM-derived peptides (i.e., CDPs and EDPs) induce extracellular proteinases in human Heart Fibroblast (HHF) cells, we isolated CDP and EDP using gelfiltration and antibody affinity column chromatography. The CDP and EDP were characterized by their intrinsic fluorescence due to cross-link structure (pyridinoline and desmosine, respectively) and by immunoblot analysis using anti-desmosine antibody. Neutrophil elastase and cathepsin G were identified using selective chromogenic substrates and by their specific inhibition with α1-proteinase inhibitor and α1-antichymotrypsin, respectively. Elastase and cathepsin G were elevated in the infarcted tissue. Selective inhibition of matrix metalloproteinase (MMP) by a higher concentration of tetracycline or doxycycline in zymographic gels elicited an inhibition constant (IC50) of 278 ± 10 μM and indicated that majority of MMP in the infarcted tissue is from Fibroblast cells. The HHF proliferation was measured using an acid-phosphatase assay. The EDP and CDP induce HHF cell proliferation. After EDP treatment phenotypic (formation of pseudopodia) changes were observed in HHF cells. To measure whether phenotypic changes by EDP or CDP are associated with MMP and tissue inhibitor of metalloproteinase (TIMP) expression in HHF cells, we measured MMP and TIMP expression by zymographic and Northern blot (mRNA) analyses. The expression of MMP and TIMP were upregulated at both the protein and gene transcription levels. These results suggested that during ischemic cardiomyopathy, initially neutrophil proteinase activates latent myocardial MMP which can degrade ECM, which continuously degrades if not controlled by TIMP, leading to ventricular dilatation and dysfunction. © 1996 Wiley-Liss, Inc.
Suresh G Kumar - One of the best experts on this subject based on the ideXlab platform.
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extracellular matrix regulation of metalloproteinase and antiproteinase in human Heart Fibroblast cells
Journal of Cellular Physiology, 1996Co-Authors: Suresh C Tyagi, Suresh G Kumar, Srinivasa R Alla, Hanumanth K Reddy, Donald J Voelker, Joseph S JanickiAbstract:Following myocardial infarction, extracellular matrix (ECM) is disrupted, which leads to the generation of collagen- and elastin-derived peptides (CDPs and EDPs, respectively). To investigate whether ECM-derived peptides (i.e., CDPs and EDPs) induce extracellular proteinases in human Heart Fibroblast (HHF) cells, we isolated CDP and EDP using gelfiltration and antibody affinity column chromatography. The CDP and EDP were characterized by their intrinsic fluorescence due to cross-link structure (pyridinoline and desmosine, respectively) and by immunoblot analysis using anti-desmosine antibody. Neutrophil elastase and cathepsin G were identified using selective chromogenic substrates and by their specific inhibition with α1-proteinase inhibitor and α1-antichymotrypsin, respectively. Elastase and cathepsin G were elevated in the infarcted tissue. Selective inhibition of matrix metalloproteinase (MMP) by a higher concentration of tetracycline or doxycycline in zymographic gels elicited an inhibition constant (IC50) of 278 ± 10 μM and indicated that majority of MMP in the infarcted tissue is from Fibroblast cells. The HHF proliferation was measured using an acid-phosphatase assay. The EDP and CDP induce HHF cell proliferation. After EDP treatment phenotypic (formation of pseudopodia) changes were observed in HHF cells. To measure whether phenotypic changes by EDP or CDP are associated with MMP and tissue inhibitor of metalloproteinase (TIMP) expression in HHF cells, we measured MMP and TIMP expression by zymographic and Northern blot (mRNA) analyses. The expression of MMP and TIMP were upregulated at both the protein and gene transcription levels. These results suggested that during ischemic cardiomyopathy, initially neutrophil proteinase activates latent myocardial MMP which can degrade ECM, which continuously degrades if not controlled by TIMP, leading to ventricular dilatation and dysfunction. © 1996 Wiley-Liss, Inc.
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induction of tissue inhibitor and matrix metalloproteinase by serum in human Heart derived Fibroblast and endomyocardial endothelial cells
Journal of Cellular Biochemistry, 1995Co-Authors: Suresh C Tyagi, Suresh G Kumar, Geraldine GloverAbstract:To understand the regulatory mechanisms of extracellular matrix (ECM) turnover and proteinase expression in human cardiovascular tissue, we have isolated and characterized human Heart Fibroblast (HHF) and human Heart endothelial (HHE) cells from endomyocardial biopsy specimens. HHE cell in culture exhibited the typical cobblestone growth pattern and positive immunofluorescent staining for factor Vlll related antigen. HHF demonstrated the typical spindle shape during culture and were positive for vimentin. Both cell types were negative for a-actin, indicating that these cells were of nonmuscle origin. Cell growth studies revealed significant growth when maintained in limiting serum concentration, suggesting mitogenic activity of these cells, and demonstrated growth inhibitory activity when grown in serum-free medium. Serum-dependent matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) expression was measured by zymography, immunoblot, and Northern blot analysis. Results indicated that serum induces both the MMP and TlMP expression at the mRNA and protein levels in a dose-dependent manner. This induction was inhibited by actinomycin D and cycloheximide, suggesting transcriptional and translational regulation of MMP and TIMP. Indirect immunofluorescence labeling indicated expression of MMP and TlMP in HHF and HHE cells. These results suggested that the serum induces proliferation as well as expression of MMP and TlMP in HHE and HHF cells. The growth inhibitory activity of these cell cultures will enable us to explore further the nature of this response and compare this phenomenon with other growth inhibitors and growth promoters identified in other normal and transformed cells.
Geraldine Glover - One of the best experts on this subject based on the ideXlab platform.
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induction of tissue inhibitor and matrix metalloproteinase by serum in human Heart derived Fibroblast and endomyocardial endothelial cells
Journal of Cellular Biochemistry, 1995Co-Authors: Suresh C Tyagi, Suresh G Kumar, Geraldine GloverAbstract:To understand the regulatory mechanisms of extracellular matrix (ECM) turnover and proteinase expression in human cardiovascular tissue, we have isolated and characterized human Heart Fibroblast (HHF) and human Heart endothelial (HHE) cells from endomyocardial biopsy specimens. HHE cell in culture exhibited the typical cobblestone growth pattern and positive immunofluorescent staining for factor Vlll related antigen. HHF demonstrated the typical spindle shape during culture and were positive for vimentin. Both cell types were negative for a-actin, indicating that these cells were of nonmuscle origin. Cell growth studies revealed significant growth when maintained in limiting serum concentration, suggesting mitogenic activity of these cells, and demonstrated growth inhibitory activity when grown in serum-free medium. Serum-dependent matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) expression was measured by zymography, immunoblot, and Northern blot analysis. Results indicated that serum induces both the MMP and TlMP expression at the mRNA and protein levels in a dose-dependent manner. This induction was inhibited by actinomycin D and cycloheximide, suggesting transcriptional and translational regulation of MMP and TIMP. Indirect immunofluorescence labeling indicated expression of MMP and TlMP in HHF and HHE cells. These results suggested that the serum induces proliferation as well as expression of MMP and TlMP in HHE and HHF cells. The growth inhibitory activity of these cell cultures will enable us to explore further the nature of this response and compare this phenomenon with other growth inhibitors and growth promoters identified in other normal and transformed cells.
Jose M Perezpomares - One of the best experts on this subject based on the ideXlab platform.
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characterization of epicardial derived cardiac interstitial cells differentiation and mobilization of Heart Fibroblast progenitors
PLOS ONE, 2013Co-Authors: Adrian Ruizvillalba, Algirdas Ziogas, Martin Ehrbar, Jose M PerezpomaresAbstract:The non-muscular cells that populate the space found between cardiomyocyte fibers are known as ‘cardiac interstitial cells’ (CICs). CICs are heterogeneous in nature and include different cardiac progenitor/stem cells, cardiac Fibroblasts and other cell types. Upon Heart damage CICs soon respond by initiating a reparative response that transforms with time into extensive fibrosis and Heart failure. Despite the biomedical relevance of CICs, controversy remains on the ontogenetic relationship existing between the different cell kinds homing at the cardiac interstitium, as well as on the molecular signals that regulate their differentiation, maturation, mutual interaction and role in adult cardiac homeostasis and disease. Our work focuses on the analysis of epicardial-derived cells, the first cell type that colonizes the cardiac interstitium. We present here a characterization and an experimental analysis of the differentiation potential and mobilization properties of a new cell line derived from mouse embryonic epicardium (EPIC). Our results indicate that these cells express some markers associated with cardiovascular stemness and retain part of the multipotent properties of embryonic epicardial derivatives, spontaneously differentiating into smooth muscle, and Fibroblast/myoFibroblast-like cells. Epicardium-derived cells are also shown to initiate a characteristic response to different growth factors, to display a characteristic proteolytic expression profile and to degrade biological matrices in 3D in vitro assays. Taken together, these data indicate that EPICs are relevant to the analysis of epicardial-derived CICs, and are a god model for the research on cardiac Fibroblasts and the role these cells play in ventricular remodeling in both ischemic or non/ischemic myocardial disease.
