Affiliation: The Hebrew University
- Towards elucidating the role of SirT1 in osteoarthritisMona Dvir-Ginzberg
Head Laboratory of Cartilage Biology, Institute of Dental Sciences, Faculty of Dental Medicine, Hebrew University Hadassah Ein Kerem P O Box 12272, Jerusalem 91120, Israel
Front Biosci (Landmark Ed) 18:343-55. 2013....
- Tumor necrosis factor α-mediated cleavage and inactivation of SirT1 in human osteoarthritic chondrocytesMona Dvir-Ginzberg
National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH, Bethesda, Maryland, USA
Arthritis Rheum 63:2363-73. 2011..This study was undertaken to test the hypothesis that SirT1 is adversely affected by TNFα, resulting in altered gene expression...
- Sirt1-deficient mice exhibit an altered cartilage phenotypeOdile Gabay
Cartilage Biology and Orthopedic Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, 50 South Drive, Bethesda, MD, USA Electronic address
Joint Bone Spine 80:613-20. 2013..We previously demonstrated that Sirt1 regulates apoptosis in cartilage in vitro. Here we attempt to examine in vivo cartilage homeostasis, using Sirt1 total body knockout (KO) mice...
- SirT1 enhances survival of human osteoarthritic chondrocytes by repressing protein tyrosine phosphatase 1B and activating the insulin-like growth factor receptor pathwayViktoria Gagarina
National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH, Bethesda, Maryland 20892, USA
Arthritis Rheum 62:1383-92. 2010..We undertook the present study to assess the role of SirT1 in the survival of osteoarthritic (OA) chondrocytes in humans...
- Sirtuin 1 enzymatic activity is required for cartilage homeostasis in vivo in a mouse modelOdile Gabay
Cartilage Biology and Orthopedic Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIH, Bethesda, Maryland 20892, USA
Arthritis Rheum 65:159-66. 2013..This study was undertaken to determine if SIRT-1 enzymatic activity plays a protective role in cartilage homeostasis in vivo, by investigating mice with SIRT-1 mutations to characterize their cartilage...
- Regulation of cartilage-specific gene expression in human chondrocytes by SirT1 and nicotinamide phosphoribosyltransferaseMona Dvir-Ginzberg
Cartilage Molecular Genetics Group, Cartilage Biology and Orthopaedics Branch, NIAMS, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 283:36300-10. 2008..SirT1, nicotinamide phosphoribosyltransferase, and NAD may, therefore, provide a positive function in human cartilage by elevating expression of genes encoding cartilage extracellular matrix...
- 75-kd sirtuin 1 blocks tumor necrosis factor α-mediated apoptosis in human osteoarthritic chondrocytesHanna Oppenheimer
Laboratory of Cartilage Biology, Institute of Dental Sciences, Faculty of Dental Medicine, Hebrew University, Hadassah Ein Kerem, Jerusalem, Israel
Arthritis Rheum 64:718-28. 2012..Because 75SirT1 is resistant to further degradation, we hypothesized that it has a distinct role in OA, and the present study was undertaken to identify this role...
- Increased apoptotic chondrocytes in articular cartilage from adult heterozygous SirT1 miceOdile Gabay
Cartilage Molecular Genetics Group, Cartilage Biology and Orthopedics Branch, National Institute of Arthritis, Musculoskeletal and Skin Disease, Bethesda, Maryland, USA
Ann Rheum Dis 71:613-6. 2012..A growing body of evidence indicates that the protein deacetylase, SirT1, affects chondrocyte biology and survival. This report aims to evaluate in vivo attributes of SirT1 in cartilage biology of 129/J murine strains...
- Set7/9 impacts COL2A1 expression through binding and repression of SirT1 histone deacetylationHanna Oppenheimer
Laboratory of Cartilage Biology, Institute of Dental Sciences, Hebrew University of Jerusalem, Jerusalem, Israel
J Bone Miner Res 29:348-60. 2014..Our study indicates that Set7/9 prevents the histone deacetylase activity of SirT1, potentiating euchromatin formation on the promoter site of COL2A1 and resulting in morphology-dependent COL2A1 gene transactivation...