TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors.
about
The ADAMTS metalloproteinasesReactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implicationsUse of cartilage derived from murine induced pluripotent stem cells for osteoarthritis drug screening.Lack of tissue inhibitor of metalloproteinases-3 results in an enhanced inflammatory response in antigen-induced arthritis.Regulation of chondrocyte gene expression by osteogenic protein-1.Effects of the mycotoxin nivalenol on bovine articular chondrocyte metabolism in vitro.Proteases involved in cartilage matrix degradation in osteoarthritis.Pentosan polysulfate increases affinity between ADAMTS-5 and TIMP-3 through formation of an electrostatically driven trimolecular complex.Tenascin-C fragments are endogenous inducers of cartilage matrix degradation.Differential regulation of extracellular tissue inhibitor of metalloproteinases-3 levels by cell membrane-bound and shed low density lipoprotein receptor-related protein 1.Bovine lactoferricin induces TIMP-3 via the ERK1/2-Sp1 axis in human articular chondrocytes.Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanases.Engineered Tissue Inhibitor of Metalloproteinases-3 Variants Resistant to Endocytosis Have Prolonged Chondroprotective Activity.Overexpression of TIMP-3 in Chondrocytes Produces Transient Reduction in Growth Plate Length but Permanently Reduces Adult Bone Quality and Quantity.Fibronectin III 13-14 domains induce joint damage via Toll-like receptor 4 activation and synergize with interleukin-1 and tumour necrosis factor.IGF-1 does not moderate the time-dependent transcriptional patterns of key homeostatic genes induced by sustained compression of bovine cartilageTumor necrosis factor alpha-dependent aggrecan cleavage and release of glycosaminoglycans in the meniscus is mediated by nitrous oxide-independent aggrecanase activity in vitroHuman nasal cartilage responds to oncostatin M in combination with interleukin 1 or tumour necrosis factor alpha by the release of collagen fragments via collagenases.Metalloproteinase and inhibitor expression profiling of resorbing cartilage reveals pro-collagenase activation as a critical step for collagenolysis.Oncostatin M in combination with tumour necrosis factor {alpha} induces a chondrocyte membrane associated aggrecanase that is distinct from ADAMTS aggrecanase-1 or -2.Hypoxia promotes the production and inhibits the destruction of human articular cartilage.Suppression of matrix metalloproteinase production from synovial fibroblasts by meloxicam in-vitro.Suramin increases cartilage proteoglycan accumulation in vitro and protects against joint damage triggered by papain injection in mouse knees in vivo.Do model polymer therapeutics sufficiently diffuse through articular cartilage to be a viable therapeutic route?Investigating ADAMTS-mediated aggrecanolysis in mouse cartilage.
P2860
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P2860
TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
TIMP-3 inhibits aggrecanase-me ...... imulated by catabolic factors.
@en
type
label
TIMP-3 inhibits aggrecanase-me ...... imulated by catabolic factors.
@en
prefLabel
TIMP-3 inhibits aggrecanase-me ...... imulated by catabolic factors.
@en
P2093
P2860
P1433
P1476
TIMP-3 inhibits aggrecanase-me ...... imulated by catabolic factors.
@en
P2093
Christi Gendron
Hideaki Nagase
Masahide Kashiwagi
P2860
P304
P356
10.1016/S0014-5793(03)01295-X
P407
P577
2003-12-01T00:00:00Z