ArticleMolecular and cellular biology2005
Matrix metalloproteinases are not essential for aggrecan turnover during normal skeletal growth and development.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Aggrecanase-selective tissue inhibitor of metalloproteinase-3 (TIMP3) protects articular cartilage in a surgical mouse model of osteoarthritis.Scientific reports · 2020Article
- Metalloprotease inhibitor TIMP proteins control FGF-2 bioavailability and regulate skeletal growth.The Journal of cell biology · 2019Article
- Article
- Article
- Hyaluronan as a therapeutic target in human diseases.Advanced drug delivery reviews · 2016Review
- Post-traumatic osteoarthritis: from mouse models to clinical trials.Nature reviews. Rheumatology · 2013Review
- Mast cell-restricted, tetramer-forming tryptases induce aggrecanolysis in articular cartilage by activating matrix metalloproteinase-3 and -13 zymogens.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Genetically Engineered Mouse Models Reveal the Importance of Proteases as Osteoarthritis Drug Targets.Current rheumatology reports · 2013Review
- Evidence for lysosomal exocytosis and release of aggrecan-degrading hydrolases from hypertrophic chondrocytes, in vitro and in vivo.Biology open · 2012Article
- Investigating ADAMTS-mediated aggrecanolysis in mouse cartilage.Nature protocols · 2011Article
- Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases.Pathology international · 2010Review
- Cartilage degradation is fully reversible in the presence of aggrecanase but not matrix metalloproteinase activity.Arthritis research & therapy · 2008Article
- Blocking aggrecanase cleavage in the aggrecan interglobular domain abrogates cartilage erosion and promotes cartilage repair.The Journal of clinical investigation · 2007Article
- Matrix metalloproteinases and the regulation of tissue remodelling.Nature reviews. Molecular cell biology · 2007Review
- The accumulation of intracellular ITEGE and DIPEN neoepitopes in bovine articular chondrocytes is mediated by CD44 internalization of hyaluronan.Arthritis and rheumatism · 2006Article
- Role of matrix metalloproteinases in bone regeneration: Narrative review.Journal of oral biology and craniofacial researchReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The growth plate is a transitional region of cartilage and highly diversified chondrocytes that controls long bone formation. The composition of growth plate cartilage changes markedly from the epiphysis to the metaphysis, notably with the loss of type II collagen, concomitant with an increase in MMP-13; type X collagen; and the C-propeptide of type II collagen. In contrast, the fate of aggrecan in the growth plate is not clear: there is biosynthesis and loss of aggrecan from hypertrophic cartilage, but the mechanism of loss is unknown. All matrix metalloproteinases (MMPs) cleave aggrecan between amino acids N341 and F342 in the proteinase-sensitive interglobular domain (IGD), and MMPs in the growth plate are thought to have a role in aggrecanolysis. We have generated mice with aggrecan resistant to proteolysis by MMPs in the IGD and found that the mice develop normally with no skeletal deformities. The mutant mice do not accumulate aggrecan, and there is no significant compensatory proteolysis occurring at alternate sites in the IGD. Our studies reveal that MMP cleavage in this key region is not a predominant mechanism for removing aggrecan from growth plate cartilage.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.