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MATN3 encodes a member of von Willebrand factor A domain containing protein family. Additionally we are shipping Matrilin 3 Antibodies (54) and Matrilin 3 Proteins (4) and many more products for this protein.
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our results revealed miR (show MLXIP ELISA Kits)-483-5p directly targeted to the cartilage matrix protein (show MATN1 ELISA Kits) matrilin 3 (Matn3) and tissue inhibitor of metalloproteinase 2 (Timp2 (show TIMP2 ELISA Kits)) 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 (show NPPC ELISA Kits)/natriuretic peptide receptor-B signaling pathway during the process of transforming growth factor-beta induced (show TGFBI ELISA Kits) chondrogenic differentiation of mesenchymal stem cells.
MATN3 plays a regulatory role in cartilage homeostasis due to its capacity to induce IL-1Ra (show IL1RN ELISA Kits), 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 (show BMP2 ELISA Kits)/Smad1 (show GARS ELISA Kits) activity
The VWA1 (show VWA1 ELISA Kits) domain of matrilin-3 is primarily responsible for the induction of IL-6 (show IL6 ELISA Kits) 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.
MATN3 mutations were identified in 13 multiple epiphyseal dysplasia patients and comprised predominantly of missense mutations.
Radiographic findings in patients with COMP (show COMP ELISA Kits) and MATN3 mutations showed marked abnormalities in hip and knee joints.
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 (show DDIT3 ELISA Kits))
MATN3 may have the inherent ability to inhibit premature chondrocyte hypertrophy by suppressing BMP-2 (show BMP2 ELISA Kits)/Smad1 (show SMAD1 ELISA Kits) activity
study will facilitate better awareness of the differential diagnoses that might be associated with the PSACH (show COMP ELISA Kits)/MED spectrum and subsequent care of PSACH (show COMP ELISA Kits)/MED patients
Lack of COMP (show COMP ELISA Kits) and matrilin 3 leads to increased deposition of TIMP-3 (show TIMP3 ELISA Kits), which causes partial inactivation of matrix metalloproteinases in bone, including MMP-13 (show MMP13 ELISA Kits).
Secretion of matrilin 3 V194D mutant protein is not dependent on hetero-oligomerization with matrilin 1 (show MATN1 ELISA Kits).
matrilin-3 mutation associated with osteoarthritis does not affect collagen affinity but promotes the formation of wider cartilage collagen (show COL2A1 ELISA Kits) 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 (show PTGS2 ELISA Kits), MMP1 (show MMP1 ELISA Kits), -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 (show MMRN1 ELISA Kits).
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.