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ADAMTS9 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family.
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Human Polyclonal ADAMTS9 Primary Antibody für IHC, IHC (p) - ABIN4278312
Peluffo, Murphy, Baughman, Stouffer, Hennebold: Systematic analysis of protease gene expression in the rhesus macaque ovulatory follicle: metalloproteinase involvement in follicle rupture. in Endocrinology 2011
Extracellular matrix dynamics is a major influence on umbilical vascular SMC (zeige DYM Antikörper) fate, with ADAMTS9 acting as its principal mediator.
The present study reveals ADAMT-9 expression by mast cells(MCs (zeige SMCP Antikörper)) and that MC activation regulates the expression of the protease, thus implicating the ADAMT-9 of protease in MC function.
Western blot analyses indicated that aggrecanase (zeige ADAMTS4 Antikörper)-generated proteoglycan (zeige Vcan Antikörper) fragments are produced after SCI.
These findings support a model in which cooperative versican proteolysis by ADAMTS9 in vascular endothelium and by ADAMTS20 in palate mesenchyme drives palatal shelf sculpting and extension.
These data identify ADAMTS9 as a novel, constitutive, endogenous angiogenesis inhibitor that operates cell-autonomously in endothelial cells.
ancillary domains of ADAMTS-9 are required both for specific extracellular localization and for its versicanase and aggrecanase (zeige ADAMTS4 Antikörper) activities
Adamts9 is widely expressed during mouse embryo development
show that combinatorial mouse alleles for the secreted metalloproteases Adamts5, Adamts20 (bt), and Adamts9 result in fully penetrant soft-tissue syndactyly.
expression by synovial cells induced by hemoglobin at low doses, suggesting a possible role for hemoglobin in cartilage damage after intra-articular hemorrhage
By inhibiting ADAMTS-9, miR (zeige MLXIP Antikörper)-338-5p suppressed the proliferation and metastasis of rheumatoid arthritis synovial fibroblasts.
Exogenous expression of ADAMTS9 in colorectal cancer cell lines inhibited cell proliferation and migration through the regulation of cell cycle and apoptosis.
Our data showed that four SNPs (rs73832338, rs9985304, rs4317088, and rs9831846) in the ADAMTS9 gene were significantly associated with cognitive aging among the subjects. Additionally, we found that interactions between the ADAMTS9 rs9985304 and ADAMTS9 rs76346246 SNPs influenced cognitive aging.
we identified the top 10 highly differentiated SNPs in Brazilian Amerindian ancestry compared to Asian, European, and African Genomes.SNPs within or proximal to CIITA (zeige CIITA Antikörper) (rs6498115), SMC6 (zeige SMC6 Antikörper) (rs1834619), and KLHL29 (rs2288697) were most differentiated in the Amerindian-specific branch. SNPs in ADAMTS9 (rs7631391), DOCK2 (zeige DOCK2 Antikörper) (rs77594147), SLC28A1 (zeige SLC28A1 Antikörper) (rs28649017), ARHGAP5 (zeige ARHGAP5 Antikörper) (rs7151991), and CIITA (zeige CIITA Antikörper) (rs45601437) in the Asian comparison.
study identified a suggestive genome-wide significant association of ADAMTS9 with asthma in Spanish subjects
NF-kappaBp65 bound to elements located at -1177 and -1335 in the ADAMTS9 promoter region, in contrast to the untreated samples. The results of the present study suggested that NF-kappaB (zeige NFKB1 Antikörper) may be involved in IL-1beta (zeige IL1B Antikörper)-induced activation of ADAMTS9 in human chondrocytes
A deletion at ADAMTS9-MAGI1 (zeige MAGI1 Antikörper) locus is associated with psoriatic arthritis risk.
LncRNA ADAMTS9-AS2 (zeige ARSA Antikörper) is regulated by DNMT1 (zeige DNMT1 Antikörper) and inhibits migration of glioma cells.
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. Members of the ADAMTS family have been implicated in the cleavage of proteoglycans, the control of organ shape during development, and the inhibition of angiogenesis. This gene is localized to chromosome 3p14.3-p14.2, an area known to be lost in hereditary renal tumors.
a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 9
, A disintegrin and metalloproteinase with thrombospondin motifs 9
, ADAM-TS 9