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ADAM metallopeptidase with thrombospondin type 1 motif, 12

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-1) motif. Individual members of this family differ in the number of C-terminal TS-1 motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains eight TS-1 motifs. It may play roles in pulmonary cells during fetal development or in tumor processes through its proteolytic activity or as a molecule potentially involved in regulation of cell adhesion. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ADAMTS, thrombospondin-1, ADAMTS-7, Comp, metalloprotease
Papers on ADAMTS-12
ADAMTS genes and the risk of cerebral aneurysm.
Holling et al., Kiel, Germany. In J Neurosurg, Feb 2016
Three SNPs under investigation are associated with a protective effect in CA pathogenesis (ADAMTS12 variant rs1364044: OR 0.65, p = 0.0001; and ADAMTS13 variants rs739469 and rs4962153: OR 0.77 and 0.63, p = 0.02 and 0.0006, respectively), while 2 other ADAMTS13 variants may confer a significant risk (rs2301612: OR 1.26, p = 0.011; rs2285489: OR 1.24, p = 0.02).
Evaluation of ADAMTS12, ADAMTS16, ADAMTS18 and IL-33 serum levels in pre-eclampsia.
Demircan et al., Ankara, Turkey. In J Matern Fetal Neonatal Med, Oct 2015
The aim of this study was to compare serum molecules including IL-33, ADAMTS12, ADAMTS16 and ADAMTS18 levels between pre-eclampsia and control groups and to investigate the role of these molecules in pre-eclampsia.
Placental ADAMTS-12 Levels in the Pathogenesis of Preeclampsia and Intrahepatic Cholestasis of Pregnancy.
Danisman et al., Ankara, Turkey. In Reprod Sci, Oct 2015
UNASSIGNED: Our aim was to determine whether placental A Disintegrin-like Metalloproteinase with ThromboSpondin motif 12 (ADAMTS-12), arylesterase (ARES) levels, total oxidant status (TOS), and total antioxidant status (TAS) differ in preeclampsia, intrahepatic cholestasis of pregnancy (ICP), and uncomplicated pregnancies or not.
Co-segregation of Freiberg's infraction with a familial translocation t(5;7)(p13.3;p22.2) ascertained by a child with cri du chat syndrome and brachydactyly type A1B.
Midro et al., In Am J Med Genet A, Feb 2015
Mapping of the chromosome breakpoints using fluorescent in situ hybridization (FISH) narrowed them to the coding sequence of ADAMTS12 on chromosome 5p13.3
Influence of vascular endothelial growth factor stimulation and serum deprivation on gene activation patterns of human adipose tissue-derived stromal cells.
Ekblond et al., Copenhagen, Denmark. In Stem Cell Res Ther, 2014
Genes most prominently and significantly upregulated by both conditions were growth factors (IGF1, BMP6, PDGFD, FGF9), adhesion molecule CLSTN2, extracellular matrix-related proteins such as matricellular proteins SMOC2, SPON1 and ADAMTS12, and inhibitors of proliferation (JAG1).
Interaction between the ADAMTS-12 metalloprotease and fibulin-2 induces tumor-suppressive effects in breast cancer cells.
Cal et al., Oviedo, Spain. In Oncotarget, 2014
On this basis we searched for molecular partners of ADAMTS-12, a secreted metalloprotease that shows both oncogenic and tumor-suppressive effects.
ADAMTS-12: a multifaced metalloproteinase in arthritis and inflammation.
Liu et al., New York City, United States. In Mediators Inflamm, 2013
ADAMTS-12 is a member of a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family of proteases, which were known to play important roles in various biological and pathological processes, such as development, angiogenesis, inflammation, cancer, arthritis, and atherosclerosis.
c-Maf Transcription Factor Regulates ADAMTS-12 Expression in Human Chondrogenic Cells.
Haudenschild et al., Sacramento, United States. In Cartilage, 2013
ADAMTS-12 is up-regulated during in vitro chondrogenesis and embryonic limb development; however, the regulation of ADAMTS-12 expression in cartilage remains unknown.
A genome-wide association study identifies a gene network of ADAMTS genes in the predisposition to pediatric stroke.
Nowak-Göttl et al., Münster, Germany. In Blood, 2013
We observed clustering of association signals in 4 genes belonging to one family of metalloproteinases at high (ADAMTS12, P = 2.9 × 10(-6); ADAMTS2, P = 8.0 × 10(-6)) and moderate (ADAMTS13, P = 9.3 × 10(-4); ADAMTS17, P = 8.5 × 10(-4)) significance levels.
Genetic diversity, linkage disequilibrium and selection signatures in chinese and Western pigs revealed by genome-wide SNP markers.
Ren et al., Nanchang, China. In Plos One, 2012
Interestingly, we highlighted several genes including ADAMTS12, SIM1 and NOS1 that show signatures of natural selection in Tibetan pigs and are likely important for genetic adaptation to high altitude.
ADAMTS-12 metalloprotease is necessary for normal inflammatory response.
López-Otín et al., Oviedo, Spain. In J Biol Chem, 2012
In this work, we have investigated the putative role of ADAMTS-12 in inflammation by using a mouse model deficient in this metalloprotease.
Control of allergen-induced inflammation and hyperresponsiveness by the metalloproteinase ADAMTS-12.
Cataldo et al., Liège, Belgium. In J Immunol, 2012
Among them, ADAMTS12 was identified as an asthma-associated gene in a human genome screening program.
Negative effects of ADAMTS-7 and ADAMTS-12 on endplate cartilage differentiation.
Wang et al., Beijing, China. In J Orthop Res, 2012
statistically significant increase in mRNA expression of ADAMTS-7 and ADAMTS-12 was observed in the endplate cells in degenerative discs compared with nondegenerative discs
Association of ADAMTS12 polymorphisms with rheumatoid arthritis.
Kim et al., Ch'ŏnan, South Korea. In Mol Med Report, 2012
Our results suggest that ADAMTS12 may be a susceptibility gene for RA development.
Genetic variations in the ADAMTS12 gene are associated with schizophrenia in Puerto Rican patients of Spanish descent.
Silverman et al., New York City, United States. In Neuromolecular Med, 2012
The data supported the hypothesis that genetic variations in ADAMTS12 influence the risk of schizophrenia.
Expression of ADAMTS12 in colorectal cancer-associated stroma prevents cancer development and is a good prognostic indicator of colorectal cancer.
He et al., Hangzhou, China. In Dig Dis Sci, 2011
expression of ADAMTS12 in colorectal cancer stroma plays an important role in inhibiting tumor development
Regulated expression of ADAMTS-12 in human trophoblastic cells: a role for ADAMTS-12 in epithelial cell invasion?
Leung et al., Toronto, Canada. In Plos One, 2010
This study identifies a novel biological role for ADAMTS-12, and highlights the importance and complexity of its non-proteolytic domain(s) pertaining to its function.
The role of ADAMTSs in arthritis.
Liu et al., New York City, United States. In Protein Cell, 2010
This review briefly summarizes the structural organization and functional roles of ADAMTSs in normal and pathological conditions, focusing on members that are known to be involved in the degradation of extracellular matrix and loss of cartilage in arthritis, including the aggrecanases (ADAMTS-4 and ADAMTS-5), ADAMTS-7 and ADAMTS-12, the latter two are associated with cartilage oligomeric matrix protein (COMP), a component of the cartilage extracellular matrix (ECM).
The role of ADAMTS-7 and ADAMTS-12 in the pathogenesis of arthritis.
Liu, New York City, United States. In Nat Clin Pract Rheumatol, 2009
ADAMTS-7 and ADAMTS-12 are newly identified enzymes responsible for cartilage oligomeric matrix protein degradation in arthritis.
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