Giulio Gabbiani | Université de Genève (original) (raw)
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Papers by Giulio Gabbiani
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Sep 30, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Mar 18, 2013
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 23, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Oct 5, 2012
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 25, 2011
Wound Repair and Regeneration, Apr 1, 1996
Myofibroblasts are granulation tissue fibroblasts bearing ultrastructural and biochemical feature... more Myofibroblasts are granulation tissue fibroblasts bearing ultrastructural and biochemical features of smooth muscle cells, such as cytoplasmic microfilaments and α‐smooth muscle actin expression. They appear transiently during wound healing and more permanently during several pathologic situations such as fibrotic diseases. Transforming growth factor‐β1 has been suggested to be an important promoter of the myofibroblastic phenotype. Here we show that (1) transforming growth factor‐β2, like transforming growth factor‐β1, induces myofibroblast formation in vivo and in vitro; (2) transforming growth factor‐β3 acts as a negative regulator of the myofibroblastic phenotype in vivo but not in vitro; and (3) in vitro, the three different transforming growth factor‐β isoforms are equally able to induce α‐smooth muscle actin messenger RNA and protein expression in growing and quiescent cultured human and rat subcutaneous tissue fibroblasts. These data confirm that in vitro the behavior of the three different transforming growth factor‐β isoforms is similar, whereas in vivo transforming growth factor‐β isoforms possibly play different but complementary roles in myofibroblast modulation during wound repair.
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Oct 11, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 8, 2011
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Dec 21, 2013
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Sep 7, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Sep 30, 2011
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, May 23, 2012
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Jul 26, 2011
Vascular Pharmacology, Sep 1, 2006
Virchows Archiv, Dec 19, 2000
Hepatology, Mar 1, 1999
Hepatic stellate cells are the major cellular sources of extracellular matrix in chronic liver di... more Hepatic stellate cells are the major cellular sources of extracellular matrix in chronic liver diseases leading to fibrosis. We explored the antifibrogenic effect of two histone deacetylase inhibitors, sodium butyrate and trichostatin A (TSA), on this cell type in vitro. Primary hepatic stellate cells as well as culture activated cells were exposed to butyrate (0.01-1 mmol/L) or TSA (1-100 nmol/L); their effect on collagen types I and III and smooth muscle alpha-actin was examined by quantitative immunoprecipitation and by Northern analysis. Their antiproliferative effect was examined by 3H-thymidine incorporation and cell counting. Hyperacetylation of histones was demonstrated by acid urea/Triton-X-100 (AUT) polyacrylamide gel electrophoresis. Possible cytotoxic effects were judged on stellate cells by evaluating de novo total protein synthesis, and on hepatocytes by measuring lactate dehydrogenase (LDH) leakage, albumin secretion, and epoxide hydrolase and ethoxycoumarin O-deethylase activity. TSA at 100 nmol/L and butyrate at 1 mmol/L retarded the morphological changes characteristic for activation of primary stellate cells. TSA at 100 nmol/L inhibited synthesis of collagen types I and III and smooth muscle alpha-actin by 62%, 70%, and 88%. Butyrate at 1 mmol/L showed a modest inhibitory effect on collagen type III and smooth muscle alpha-actin, but had no effect on collagen type I. Northern analysis suggested that these inhibitory effects on collagen type III and smooth muscle alpha-actin were transcriptional, while the effect on collagen type I was largely posttranscriptional. At 100 nmol/L, TSA strongly suppressed proliferation of primary hepatic stellate cells. Inhibition of activation of stellate cells was preceded by hyperacetylation of histone H4. When tested on cells at day 14 in culture, butyrate had no inhibitory effects on the synthesis of collagens or smooth muscle alpha-actin. One hundred or 10 nmol/L TSA modestly inhibited the synthesis of collagens type I (-24%,-22%) and III (-34%,-22%), and smooth muscle alpha-actin (-27%,-12%). We conclude that TSA inhibits transdifferentiation of stellate cells into myofibroblasts by interfering with the level of acetylation of histone H4.
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 9, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Nov 12, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Sep 30, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Mar 18, 2013
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 23, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Oct 5, 2012
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 25, 2011
Wound Repair and Regeneration, Apr 1, 1996
Myofibroblasts are granulation tissue fibroblasts bearing ultrastructural and biochemical feature... more Myofibroblasts are granulation tissue fibroblasts bearing ultrastructural and biochemical features of smooth muscle cells, such as cytoplasmic microfilaments and α‐smooth muscle actin expression. They appear transiently during wound healing and more permanently during several pathologic situations such as fibrotic diseases. Transforming growth factor‐β1 has been suggested to be an important promoter of the myofibroblastic phenotype. Here we show that (1) transforming growth factor‐β2, like transforming growth factor‐β1, induces myofibroblast formation in vivo and in vitro; (2) transforming growth factor‐β3 acts as a negative regulator of the myofibroblastic phenotype in vivo but not in vitro; and (3) in vitro, the three different transforming growth factor‐β isoforms are equally able to induce α‐smooth muscle actin messenger RNA and protein expression in growing and quiescent cultured human and rat subcutaneous tissue fibroblasts. These data confirm that in vitro the behavior of the three different transforming growth factor‐β isoforms is similar, whereas in vivo transforming growth factor‐β isoforms possibly play different but complementary roles in myofibroblast modulation during wound repair.
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Oct 11, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 8, 2011
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Dec 21, 2013
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Sep 7, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Sep 30, 2011
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, May 23, 2012
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Jul 26, 2011
Vascular Pharmacology, Sep 1, 2006
Virchows Archiv, Dec 19, 2000
Hepatology, Mar 1, 1999
Hepatic stellate cells are the major cellular sources of extracellular matrix in chronic liver di... more Hepatic stellate cells are the major cellular sources of extracellular matrix in chronic liver diseases leading to fibrosis. We explored the antifibrogenic effect of two histone deacetylase inhibitors, sodium butyrate and trichostatin A (TSA), on this cell type in vitro. Primary hepatic stellate cells as well as culture activated cells were exposed to butyrate (0.01-1 mmol/L) or TSA (1-100 nmol/L); their effect on collagen types I and III and smooth muscle alpha-actin was examined by quantitative immunoprecipitation and by Northern analysis. Their antiproliferative effect was examined by 3H-thymidine incorporation and cell counting. Hyperacetylation of histones was demonstrated by acid urea/Triton-X-100 (AUT) polyacrylamide gel electrophoresis. Possible cytotoxic effects were judged on stellate cells by evaluating de novo total protein synthesis, and on hepatocytes by measuring lactate dehydrogenase (LDH) leakage, albumin secretion, and epoxide hydrolase and ethoxycoumarin O-deethylase activity. TSA at 100 nmol/L and butyrate at 1 mmol/L retarded the morphological changes characteristic for activation of primary stellate cells. TSA at 100 nmol/L inhibited synthesis of collagen types I and III and smooth muscle alpha-actin by 62%, 70%, and 88%. Butyrate at 1 mmol/L showed a modest inhibitory effect on collagen type III and smooth muscle alpha-actin, but had no effect on collagen type I. Northern analysis suggested that these inhibitory effects on collagen type III and smooth muscle alpha-actin were transcriptional, while the effect on collagen type I was largely posttranscriptional. At 100 nmol/L, TSA strongly suppressed proliferation of primary hepatic stellate cells. Inhibition of activation of stellate cells was preceded by hyperacetylation of histone H4. When tested on cells at day 14 in culture, butyrate had no inhibitory effects on the synthesis of collagens or smooth muscle alpha-actin. One hundred or 10 nmol/L TSA modestly inhibited the synthesis of collagens type I (-24%,-22%) and III (-34%,-22%), and smooth muscle alpha-actin (-27%,-12%). We conclude that TSA inhibits transdifferentiation of stellate cells into myofibroblasts by interfering with the level of acetylation of histone H4.
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Aug 9, 2010
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, Nov 12, 2010