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MATN3 encodes a member of von Willebrand factor A domain containing protein family. Zusätzlich bieten wir Ihnen Matrilin 3 Antikörper (62) und Matrilin 3 Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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miR (zeige MLXIP Proteine)-448 contributed to the progression of osteoarthritis by directly targeting matrilin-3.
Study confirmed that MATN3 protein was highly expressed in GAC (zeige GLS Proteine) patients, and MATN3 overexpression could be used as an independent predictor of poor prognosis in GAC (zeige GLS Proteine) patients.
our results revealed miR (zeige MLXIP Proteine)-483-5p directly targeted to the cartilage matrix protein (zeige MATN1 Proteine) matrilin 3 (Matn3) and tissue inhibitor of metalloproteinase 2 (Timp2 (zeige TIMP2 Proteine)) to stimulate chondrocyte hypertrophy, extracellular matrix degradation, and cartilage angiogenesis, and it consequently initiated and accelerated the development of OA.
The results of the study indicate a potential role for the MATN3 rs28598872 polymorphism in the pathogenesis of Temporomandibular Joint Internal Derangement.
This report is the first to show the involvement of MATN3 in C-type natriuretic peptide/natriuretic peptide receptor-B signaling pathway during the process of transforming growth factor-beta induced chondrogenic differentiation of mesenchymal stem cells.
MATN3 plays a regulatory role in cartilage homeostasis due to its capacity to induce IL-1Ra (zeige IL1RN Proteine), upregulate gene expression of major cartilage matrix components, and downregulate the expression of OA-associated matrix-degrading proteinases in chondrocytes.
MATN3 may have the inherent ability to inhibit premature chondrocyte hypertrophy by suppressing BMP-2 (zeige BMP2 Proteine)/Smad1 (zeige GARS Proteine) activity
The VWA1 (zeige VWA1 Proteine) domain of matrilin-3 is primarily responsible for the induction of IL-6 (zeige IL6 Proteine) release from primary human chondrocytes.
Polymorphism in the MATN3 gene might play a role in osteoarthritis in the Chinese Han population.
Haplotype-4 of MATN3 is associated with vertebral fracture risk independent of bone mineral density in Chinese postmenopausal women.
Data show that hand osteoarthritis (HOA)-related matrilin-3 mutation (T298M) leads to a high expression level of growth arrest DNA damage-inducible gene 153 (GADD153 (zeige DDIT3 Proteine))
MATN3 may have the inherent ability to inhibit premature chondrocyte hypertrophy by suppressing BMP-2 (zeige BMP2 Proteine)/Smad1 (zeige SMAD1 Proteine) activity
study will facilitate better awareness of the differential diagnoses that might be associated with the PSACH (zeige COMP Proteine)/MED spectrum and subsequent care of PSACH (zeige COMP Proteine)/MED patients
Lack of COMP (zeige COMP Proteine) and matrilin 3 leads to increased deposition of TIMP-3 (zeige TIMP3 Proteine), which causes partial inactivation of matrix metalloproteinases in bone, including MMP-13 (zeige MMP13 Proteine).
Secretion of matrilin 3 V194D mutant protein is not dependent on hetero-oligomerization with matrilin 1 (zeige MATN1 Proteine).
matrilin-3 mutation associated with osteoarthritis does not affect collagen affinity but promotes the formation of wider cartilage collagen (zeige COL2A1 Proteine) fibrils
potential of matrilin-3 to modulate gene expression profile of primary chondrocytes; tested matrilin3-dependent induction of pro-inflammatory cytokines, inducible nitric oxide synthetase & cyclooxygenase-2 (zeige PTGS2 Proteine), MMP1 (zeige MMP1 Proteine), -3 & -13, & matrilin-3 itself
Expression of matrilin-3 during maturation of mouse skeletal tissues
To assess the function of matrilin-3 during skeletal development, we have generated Matn-3 null mice; phenotypes of multiple epiphyseal dysplasia disorders are not caused by the absence of matrilin-3 in cartilage ECM (zeige MMRN1 Proteine).
This gene encodes a member of von Willebrand factor A domain containing protein family. This family of proteins is thought to be involved in the formation of filamentous networks in the extracellular matrices of various tissues. This protein contains two von Willebrand factor A domains\; it is present in the cartilage extracellular matrix and has a role in the development and homeostasis of cartilage and bone. Mutations in this gene result in multiple epiphyseal dysplasia.