The Experts below are selected from a list of 283182 Experts worldwide ranked by ideXlab platform
G I Goldberg - One of the best experts on this subject based on the ideXlab platform.
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expression of 92 kd type iv collagenase gelatinase gelatinase b in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1
Journal of Clinical Investigation, 1993Co-Authors: Masaaki Mohtai, N I Hutchinson, Y Tsuji, William G Stetlerstevenson, Frank M Torti, David J Schurman, R. L. Smith, G I GoldbergAbstract:: We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from normal cartilage also exhibited mRNA for 72-kD type IV collagenase/gelatinase (gelatinase A), tissue collagenase, and stromelysin-1, and these mRNAs were increased in osteoarthritic cartilage. Regional analysis of osteoarthritic cartilage samples from four individuals revealed that gelatinase B mRNA was expressed in grossly fibrillated areas; two of four nonfibrillated cartilage samples failed to exhibit the mRNA, but did have increased levels of mRNA for other neutral metalloproteinases. IL-1 alpha treatment of normal human cartilage explants or isolated chondrocytes induced increased levels of gelatinase B and increased mRNA for tissue collagenase and stromelysin-1. Under identical conditions, mRNA levels for gelatinase A were not increased indicating that regulation of this enzyme in human articular chondrocytes is distinct from that of other metalloproteinases. Our data showing expression of gelatinase B in fibrillated cartilage suggest that it is a marker of progressive articular cartilage degradation in Osteoarthritis.
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Expression of 92-kD type IV collagenase/gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1.
Journal of Clinical Investigation, 1993Co-Authors: Masaaki Mohtai, William G. Stetler-stevenson, N I Hutchinson, Y Tsuji, Frank M Torti, David J Schurman, R. L. Smith, G I GoldbergAbstract:: We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from normal cartilage also exhibited mRNA for 72-kD type IV collagenase/gelatinase (gelatinase A), tissue collagenase, and stromelysin-1, and these mRNAs were increased in osteoarthritic cartilage. Regional analysis of osteoarthritic cartilage samples from four individuals revealed that gelatinase B mRNA was expressed in grossly fibrillated areas; two of four nonfibrillated cartilage samples failed to exhibit the mRNA, but did have increased levels of mRNA for other neutral metalloproteinases. IL-1 alpha treatment of normal human cartilage explants or isolated chondrocytes induced increased levels of gelatinase B and increased mRNA for tissue collagenase and stromelysin-1. Under identical conditions, mRNA levels for gelatinase A were not increased indicating that regulation of this enzyme in human articular chondrocytes is distinct from that of other metalloproteinases. Our data showing expression of gelatinase B in fibrillated cartilage suggest that it is a marker of progressive articular cartilage degradation in Osteoarthritis.
Toshifumi Ozaki - One of the best experts on this subject based on the ideXlab platform.
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Transtibial pullout repair of medial meniscus posterior root tears: effects on the meniscus healing score and ICRS grade among patients with mild Osteoarthritis of the knee
Knee Surgery Sports Traumatology Arthroscopy, 2020Co-Authors: Yuya Kodama, Takayuki Furumatsu, Yuki Okazaki, Shota Takihira, Takaaki Hiranaka, Shinichi Miyazawa, Yusuke Kamatsuki, Toshifumi OzakiAbstract:Purpose To assess the effects of transtibial pullout repair for medial meniscus posterior root tears (MMPRTs) among patients with early Osteoarthritis of the knee as measured by the meniscus healing score and to determine whether the meniscus healing score correlates with the International Cartilage Repair Society (ICRS) grade progression. Methods Forty-seven patients with mild osteoarthritic knees (Kellgren–Lawrence grade ≤ 2 and varus alignment
Masaaki Mohtai - One of the best experts on this subject based on the ideXlab platform.
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expression of 92 kd type iv collagenase gelatinase gelatinase b in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1
Journal of Clinical Investigation, 1993Co-Authors: Masaaki Mohtai, N I Hutchinson, Y Tsuji, William G Stetlerstevenson, Frank M Torti, David J Schurman, R. L. Smith, G I GoldbergAbstract:: We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from normal cartilage also exhibited mRNA for 72-kD type IV collagenase/gelatinase (gelatinase A), tissue collagenase, and stromelysin-1, and these mRNAs were increased in osteoarthritic cartilage. Regional analysis of osteoarthritic cartilage samples from four individuals revealed that gelatinase B mRNA was expressed in grossly fibrillated areas; two of four nonfibrillated cartilage samples failed to exhibit the mRNA, but did have increased levels of mRNA for other neutral metalloproteinases. IL-1 alpha treatment of normal human cartilage explants or isolated chondrocytes induced increased levels of gelatinase B and increased mRNA for tissue collagenase and stromelysin-1. Under identical conditions, mRNA levels for gelatinase A were not increased indicating that regulation of this enzyme in human articular chondrocytes is distinct from that of other metalloproteinases. Our data showing expression of gelatinase B in fibrillated cartilage suggest that it is a marker of progressive articular cartilage degradation in Osteoarthritis.
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Expression of 92-kD type IV collagenase/gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1.
Journal of Clinical Investigation, 1993Co-Authors: Masaaki Mohtai, William G. Stetler-stevenson, N I Hutchinson, Y Tsuji, Frank M Torti, David J Schurman, R. L. Smith, G I GoldbergAbstract:: We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from normal cartilage also exhibited mRNA for 72-kD type IV collagenase/gelatinase (gelatinase A), tissue collagenase, and stromelysin-1, and these mRNAs were increased in osteoarthritic cartilage. Regional analysis of osteoarthritic cartilage samples from four individuals revealed that gelatinase B mRNA was expressed in grossly fibrillated areas; two of four nonfibrillated cartilage samples failed to exhibit the mRNA, but did have increased levels of mRNA for other neutral metalloproteinases. IL-1 alpha treatment of normal human cartilage explants or isolated chondrocytes induced increased levels of gelatinase B and increased mRNA for tissue collagenase and stromelysin-1. Under identical conditions, mRNA levels for gelatinase A were not increased indicating that regulation of this enzyme in human articular chondrocytes is distinct from that of other metalloproteinases. Our data showing expression of gelatinase B in fibrillated cartilage suggest that it is a marker of progressive articular cartilage degradation in Osteoarthritis.
Yuya Kodama - One of the best experts on this subject based on the ideXlab platform.
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Transtibial pullout repair of medial meniscus posterior root tears: effects on the meniscus healing score and ICRS grade among patients with mild Osteoarthritis of the knee
Knee Surgery Sports Traumatology Arthroscopy, 2020Co-Authors: Yuya Kodama, Takayuki Furumatsu, Yuki Okazaki, Shota Takihira, Takaaki Hiranaka, Shinichi Miyazawa, Yusuke Kamatsuki, Toshifumi OzakiAbstract:Purpose To assess the effects of transtibial pullout repair for medial meniscus posterior root tears (MMPRTs) among patients with early Osteoarthritis of the knee as measured by the meniscus healing score and to determine whether the meniscus healing score correlates with the International Cartilage Repair Society (ICRS) grade progression. Methods Forty-seven patients with mild osteoarthritic knees (Kellgren–Lawrence grade ≤ 2 and varus alignment
Frank M Torti - One of the best experts on this subject based on the ideXlab platform.
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expression of 92 kd type iv collagenase gelatinase gelatinase b in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1
Journal of Clinical Investigation, 1993Co-Authors: Masaaki Mohtai, N I Hutchinson, Y Tsuji, William G Stetlerstevenson, Frank M Torti, David J Schurman, R. L. Smith, G I GoldbergAbstract:: We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from normal cartilage also exhibited mRNA for 72-kD type IV collagenase/gelatinase (gelatinase A), tissue collagenase, and stromelysin-1, and these mRNAs were increased in osteoarthritic cartilage. Regional analysis of osteoarthritic cartilage samples from four individuals revealed that gelatinase B mRNA was expressed in grossly fibrillated areas; two of four nonfibrillated cartilage samples failed to exhibit the mRNA, but did have increased levels of mRNA for other neutral metalloproteinases. IL-1 alpha treatment of normal human cartilage explants or isolated chondrocytes induced increased levels of gelatinase B and increased mRNA for tissue collagenase and stromelysin-1. Under identical conditions, mRNA levels for gelatinase A were not increased indicating that regulation of this enzyme in human articular chondrocytes is distinct from that of other metalloproteinases. Our data showing expression of gelatinase B in fibrillated cartilage suggest that it is a marker of progressive articular cartilage degradation in Osteoarthritis.
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Expression of 92-kD type IV collagenase/gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1.
Journal of Clinical Investigation, 1993Co-Authors: Masaaki Mohtai, William G. Stetler-stevenson, N I Hutchinson, Y Tsuji, Frank M Torti, David J Schurman, R. L. Smith, G I GoldbergAbstract:: We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from normal cartilage also exhibited mRNA for 72-kD type IV collagenase/gelatinase (gelatinase A), tissue collagenase, and stromelysin-1, and these mRNAs were increased in osteoarthritic cartilage. Regional analysis of osteoarthritic cartilage samples from four individuals revealed that gelatinase B mRNA was expressed in grossly fibrillated areas; two of four nonfibrillated cartilage samples failed to exhibit the mRNA, but did have increased levels of mRNA for other neutral metalloproteinases. IL-1 alpha treatment of normal human cartilage explants or isolated chondrocytes induced increased levels of gelatinase B and increased mRNA for tissue collagenase and stromelysin-1. Under identical conditions, mRNA levels for gelatinase A were not increased indicating that regulation of this enzyme in human articular chondrocytes is distinct from that of other metalloproteinases. Our data showing expression of gelatinase B in fibrillated cartilage suggest that it is a marker of progressive articular cartilage degradation in Osteoarthritis.
