Atlas of Genetics and Cytogenetics in Oncology and Haematology


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ADAMTS1 (ADAM metallopeptidase with thrombospondin type 1 motif, 1)

Identity

Other namesADAM-TS1
C3-C5
EC 3.4.24.-
KIAA1346
METH-1
METH1
HGNC (Hugo) ADAMTS1
LocusID (NCBI) 9510
Location 21q21.3
Location_base_pair Starts at 28208606 and ends at 28217728 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Note Mouse: 16 region C3-C5.

DNA/RNA

Description Gene : 1 --> 4670
Exon : 1 --> 1185
CDS : 456 --> 3359
Signal peptide : 456 --> 602
Proprotein: 603 --> 3356
Mature peptide : 1212 --> 3356
Human ADAMTS1 DNA spans 4,649 bps. Its sequence is composed of 9 exons.
Transcription The ADAMTS1 gene is composed of nine exons, all of which are present within the 9.2-kb genomic region. Sequence analysis shows that the open reading frame of ADAMTS1 codes for a protein of 950 amino acids (Vazquez et al., 1999). Among these exons, exons 2 to 8 range from 133 to 347 bp in size. The first and the last exons are longer than the others. There are 4 polyadenylation signals in the untranslated region of exon 9. Exons 1, 5, and 6 encode a proprotein domain, a disintegrin-like domain and a TSP type I motif, respectively, of the ADAMTS1 protein. The metalloproteinase domain is encoded by the 3 exons: 2, 3 and 4. Exons 7 and 8 encode the spacer region (Kuno et al., 1997a).
ADAMTS1 is an IL-1 inducible gene since ADAMTS1 mRNA levels are enhanced 2 h after IL-1 stimulation (Kuno et al., 1997a). Moreover, ADAMTS1 mRNA expression is significantly enhanced in heart and kidney after lipopolysaccharide (LPS) treatment. These data indicate that the ADAMTS1 gene is an inflammation-associated gene.
Pseudogene No pseudogenes reported.

Protein

Note ADAMTS1 precursor: 967 amino acids; 105358 Da.
 
  Structure of ADAMTS1 proteinase. ADAMTS1 is composed of a propeptide (Pro), a metalloproteinase domain (Metallo), a disintegrin domain (Dis), a thrombospondin type 1-like motif (TSP1), a cystein-rich domain (Cysrich), a spacer domain (SP) followed by two additional thrombospondin type 1-like motifs (TSP1). ADAMTS1 proteinase contains in addition a sequence recognized by furin-like enzymes (FU) (Rocks et al., 2008a).
Description There are many cysteine residues, especially from residues 346 to 950, and four putative N-glycosylation sites in the ADAMTS1 protein. Comparison of the deduced amino acid sequence of ADAMTS1 protein with the data base (Human Genome Center, Institute of Medical Science, University of Tokyo) reveales that the middle part (519-615 amino acids) of the ADAMTS1 gene product shows about 40% homology with thrombospondin-1 and thrombospondin-2 (Kuno et al., 1997b). The TSP type I motifs present in the C-terminal half of ADAMTS1 are functional for binding to heparin. Moreover, analyses of deletion mutants have revealed that the carboxyl-terminal spacing region as well as three TSP type I motifs are responsible for the anchoring to the extracellular matrix (Kuno and Matsushima, 1998).
The proteinase domain of ADAMTS1 is capable of forming a covalent complex with alpha2-macroglobulin, a plasma proteolytic enzyme inhibitor that binds various types of proteinases, revealing that ADAMTS1 is an active metalloproteinase. The finding that a mutation of the zinc-binding motif of ADAMTS1 abrogates its capacity to bind to alpha2-macroglobulin confirmes the notion of an active proteinase (Kuno et al., 1999). However, in the potential zinc-binding motif of ADAMTS1, the Gly residue of the consensus sequence (HEXXHXXGXXH) is not conserved. Since ADAMTS1 is an active metalloproteinase, it is likely that the conserved Gly residue of the zinc-binding motif is functionally interchangeable with Asn (Kuno et al., 1999).
Studies have demonstrated that ADAMTS1 and fibulin-1 are colocalized in vivo. Interestingly, fibulin-1 has been found to enhance the capacity of ADAMTS1 to cleave aggrecan. Fibulin-1 seems therefore to be a new regulator of ADAMTS1-mediated proteoglycan proteolysis and may play an important role in proteoglycan turnover in tissues where there is overlapping expression (Lee et al., 2005).
Expression To date, studies analyzing the expression of ADAMTS1 in normal tissues have leaded to controversial data. Tissue distribution of ADAMTS1 mRNA has been examined by Northern blot analysis by several research groups. While some research groups describe a very weak signal for ADAMTS1 mRNA in the heart and kidney and no ADAMTS1 mRNA expression in other organs including lung, liver, brain, and muscle, other groups describe an ADAMTS1 expression in every tissues analyzed, with abundant ADAMTS1 mRNA expression in adrenal, heart, and placenta, skeletal muscle, thyroid, and stomach. Of the embryonic tissues analyzed, kidney has showed the highest expression of ADAMTS1 mRNA. ADAMTS1 mRNA has been detected in dermal fibroblasts and at lower levels in vascular smooth muscle cells, endometrial stromal cells and in some endothelial cells (Vazquez et al., 1999).
Since the ADAMTS1 gene is activated by IL-1 stimulation in vitro, LPS has been administered intravenously into mice for induction of systemic inflammation. ADAMTS1 mRNA levels are significantly enhanced in heart and kidney after LPS treatment, but not in other organs (evaluated by Northern blot analysis). This result indicates that the ADAMTS1 gene is an inflammation-associated gene (Kuno et al., 1997b).
ADAMTS1 mRNA has been detected in the ischemic myocardium. Endothelial cells, which weakly express ADAMTS1 mRNA in the normal heart, have shown increased expression of ADAMTS1 mRNA immediately after myocardial infarction concomitant with VEGF expression (Nakamura et al., 2004).
Increased ADAMTS1 mRNA expression has been observed in the kidney by in situ hybridization after induction of unilateral ureteral obstruction (Nakamura et al., 2007).
In granulosa cells, progesterone receptor appears to play the role of an inducible coregulator of the ADAMTS1 gene (Doyle et al., 2004).
Localisation Extracellular localization, anchored to the extracellular matrix through C-terminal spacing region and thrombospondin type I motifs.
Function ADAMTS1 is a catalytic active protein and identified substrates of ADAMTS1 are principally proteoglycans such as aggrecan and versican (Kuno et al., 2000; Rodriguez-Manzaneque et al., 2002).
ADAMTS1 is able to cleave ligands of the EGF (Epidermal Growth Factor) receptor such as pro-HBEGF (Heparin-binding EGF-like Growth Factor) or pro-amphiregulin (Liu et al., 2006).
Two new substrates of ADAMTS1 have been identified recently: thrombospondin-1 and thrombospondin-2 (Lee et al., 2006).
Like many members of the ADAM and ADAMTS subfamilies, ADAMTS1 shares many physiological and pathological functions. Studies using ADAMTS1-knock-out mice showed that this proteinase is important for normal growth, organogenesis and fertility (Mittaz et al., 2004).
ADAMTS1 is implicated in inflammatory processes since a treatment of mice with LPS enhances ADAMTS1 expression in tissues (Kuno et al., 1997b).
Homology Comparison of the human and mouse sequences of ADAMTS1 reveals highly conservation (83.4% amino acid identity). The overall amino acid sequence identity between ADAMTS1 and ADAMTS-8 is 51.7% (Vazquez et al., 1999).

Mutations

Note A down-regulation of ADAMTS1 has been observed in some non small cell lung cancer (NSCLC) cell lines and is concordant with an aberrant methylation of the gene. In NSCLC tumours, aberrant methylation of the gene has been observed in 31.6% of samples, while it was found in only 7.1% of nonmalignant tissues (Choi et al., 2008).
In colorectal tumors, ADAMTS1 gene is associated to a cancer-specific hypermethylation. Among 20 colon cancer cell lines, hypermethylation of the ADAMTS1 gene was identified in 85% of cell lines. The methylation status of ADAMTS1 has also been investigated in colorectal adenomas and carcinomas. 37% of adenomas as well as 71% of carcinomas showed hypermethylation for the ADAMTS1 gene. However, ADAMTS1 is unmethylated in tumors from three other organs, prostate, testis, and kidney (Lind et al., 2006).

Implicated in

Entity Lung cancer
Note ADAMTS1 stable transfection in human epithelial lung cancer cells (BZR) accelerates the in vivo tumor growth after subcutaneous injection of cell transfectants into severe combined immunodeficient (SCID) mice (Rocks et al., 2008a).
The proteolytic status of ADAMTS1 is determinant for its effects on tumor metastasis since the catalytically inactive ADAMTS1 and the ADAMTS1 fragments generated by auto-proteolytic cleavage inhibit tumor metastasis of cells subcutaneously injected into mice by negatively regulating the availability and activity of soluble heparin-binding EGF (HB-EGF) and amphiregulin (Liu et al., 2006).
Prognosis Not determined
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
Oncogenesis Tumours derived from ADAMTS1 overexpressing cells display an enhanced stromal reaction characterized by a myofibroblast infiltration and excessive matrix deposition (Rocks et al., 2008b). These features are, however, not observed in tumors derived from cells overexpressing a catalytically inactive mutant of ADAMTS1. A Boyden Chamber assay has shown that conditioned media from ADAMTS1-overexpressing cells display a potent chemotactic activity towards fibroblasts. Moreover, ADAMTS1 overexpression in tumors is associated with increased production of matrix metalloproteinase-13, fibronectin, transforming growth factor (TGF) beta, and interleukin (IL)-1 beta. Neutralizing antibodies against TGF-beta and IL-1 beta block the chemotactic effect of medium conditioned by ADAMTS1-overexpressing cells on fibroblasts, showing the contribution of these factors in ADAMTS1-induced stromal reaction (Rocks et al., 2008b).
Moreover, overexpression of ADAMTS1 in Lewis lung carcinoma cells promotes pulmonary metastasis of these cells. Interestingly, the proteinase-dead mutant of ADAMTS1 inhibits their metastasis, indicating again that the prometastatic activity of ADAMTS1 requires its metalloproteinase activity. Overexpression of ADAMTS1 in these cells promotes tumor angiogenesis and invasion, shedding of the transmembrane precursors of HB-EGF and amphiregulin. This study shows that ADAMTS1 undergoes auto-proteolytic cleavage to generate the NH2- and COOH-terminal cleavage fragments containing at least one thrombospondin-type-I-like motif. Overexpression of the NH2-terminal ADAMTS1 fragment and the COOH-terminal ADAMTS1 fragment inhibits pulmonary tumor metastasis (Liu et al., 2006).
  
Entity Breast cancer
Note Real-Time PCR analysis of human breast tissues shows that ADAMTS1 is downregulated in breast carcinomas in respect to non neoplastic mammary tissue, irrespective of the heterogeneity of the samples and the tumor type or grade. ADAMTS1 is expressed predominantly in stromal fibroblasts (Porter et al., 2004).
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  
Entity Pancreatic cancer
Note ADAMTS1 expression has been identified in pancreatic cancer cell lines and quantified by TaqMan reverse transcription-PCR in 18 paired samples of pancreatic cancer and surrounding noncancerous pancreas. ADAMTS1 expression in pancreatic cancer tissue is significantly lower than that in noncancerous pancreas (Masui et al., 2001).
Prognosis Pancreatic cancer displaying higher ADAMTS1 expression show significantly severe lymph node metastasis or retroperitoneal invasion and worse prognosis. ADAMTS1 seems to be involved in progression of pancreatic cancer through local invasion and lymph node metastasis (Masui et al., 2001).
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  
Entity Myocardial infarction
Note Normal endothelium expresses little ADAMTS1 mRNA, and normal myocardium expresses no detectable ADAMTS1 mRNA. In situ hybridization has revealed strong ADAMTS1 mRNA signals in the endothelium and myocardium in the infarcted heart, mainly in the infarct zone. The rapid and transient up-regulation of the ADAMTS1 gene in the ischemic heart is distinct from the regulatory patterns of other MMPs (Nakamura et al., 2004).
Prognosis Not determined
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  
Entity Normal growth, organogenesis, fertility
Note ADAMTS1 is produced by the granulosa cells of ovarian follicles. Mice with ADAMTS1 gene disruption are subfertile due to a significant reduction in the number of healthy growing follicles. Follicle dysmorphogenesis starting at the stage of antrum formation was identified in ADAMTS1 -/- ovaries. ADAMTS1 is therefore necessary for structural remodelling during ovarian follicle growth (Brown et al., 2006). In addition, ovulation in ADAMTS1 null females was impaired because of mature oocytes remaining trapped in ovarian follicles. Moreover, forty-five percent of newborn ADAMTS1 null mice die, with death most likely caused by a kidney malformation that becomes apparent at birth (Mittaz et al., 2004). These mice present enlarged renal calices with fibrotic changes from the ureteropelvic junction through the ureter, and abnormal adrenal medullary architecture without capillary formation (Shindo et al., 2000).
Prognosis Not determined
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  
Entity Angiogenesis inhibitor
Note ADAMTS1 suppresses fibroblast growth factor-2 (FGF2)-induced vascularization in the cornea pocket assay and inhibits VEGF-induced angiogenesis in the chorioallantoic membrane assay. ADAMTS1 binds to VEGF and therewith abrogates the phosphorylation of its receptor, VEGFR2 (Vazquez et al., 1999).
Prognosis Not determined
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  
Entity Renal ischemia or obstruction
Note Rats subjected to bilateral renal ischemia display an enhanced expression of ADAMTS1 in renal tissues. Immunofluorescence localized the ADAMTS1 expression to proximal tubules following ischemia-reperfusion injury. An inhibition of the VEGF pathway by ADAMTS1 during the early injury and repair phase of renal ischemia may therefore contribute to an overall reduction in renal microvascular density (Basile et al., 2008).
Increased ADAMTS1 mRNA expression (in situ hybridization) has also been observed in the kidney of rats after induction of unilateral ureteral obstruction. The mRNA is then localized in the renal tubular epithelial cells in the outer stripe of the outer medulla (Nakamura et al., 2007).
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
Oncogenesis Not determined
  
Entity Asthma
Note Expression profile of several ADAM and ADAMTS proteinases has been measured in sputum cells from patients with asthma. The relationship between the expression of these proteinases and asthma-associated inflammation and airway obstruction has been assessed. Levels of ADAMTS1 mRNA are significantly decreased in patients with asthma compared to control patients (Paulissen et al., 2006).
Prognosis ADAMTS1 expression is positively correlated to Forced Expiratory Volume at the first second (FEV(1)) (r = 0.45, P < 0.05) (Paulissen et al., 2006).
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  
Entity New bone formation
Note ADAMTS1 mRNA expression has been identified by RT-PCR in cultures of rat osteoblasts treated with molecules known to drive osteoblast differentiation (ascorbic acid, beta-glycerophosphate and dexamethasone). ADAMTS1 expression follows the expression of osteogenic marker osteocalcin during in vitro mineralization. ADAMTS1 production has been investigated by immunostaining during in vitro osteogenesis and in sections from 2- and 10-day-old rat femur. These results show a strong expression of ADAMTS1 around mineralized nodules and intense focal staining of putative new areas of nodule formation in vitro. In 2- and 10-days-old rat femurs, ADAMTS1 protein is localized in regions associated with osteogenesis. These data show that ADAMTS1 protein accumulates in osteoblast extracellular matrix during differentiation (Lind et al., 2005).
Prognosis Not determined
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  
Entity Neurodegenerative disorders
Note Levels of ADAMTS1 have been assessed in extracted proteins from Down syndrome (DS) brain and brains of patients with Alzheimer's (AD) and Pick's disease (PD) used as controls. ADAMTS1 immunoreactivity is increased in brains with DS and neurodegeneration. Overexpression of this metalloproteinase might thus be involved in proteoglycan degradation and handling in brain of patients with neurodegenerative disease which in turn may lead to or reflect pathological lesions in DS, AD and PD brain (Miguel et al., 2005).
Prognosis This overexpression of ADAMTS1 may be used as marker protein for neurodegeneration.
Cytogenetics Not determined
Hybrid/Mutated Gene Not determined
Abnormal Protein Not determined
  

External links

Nomenclature
HGNC (Hugo)ADAMTS1   217
Cards
AtlasADAMTS1ID574ch21q21
Entrez_Gene (NCBI)ADAMTS1  9510  ADAM metallopeptidase with thrombospondin type 1 motif, 1
GeneCards (Weizmann)ADAMTS1
Ensembl (Hinxton)ENSG00000154734 [Gene_View]  chr21:28208606-28217728 [Contig_View]  ADAMTS1 [Vega]
ICGC DataPortalENSG00000154734
AceView (NCBI)ADAMTS1
Genatlas (Paris)ADAMTS1
WikiGenes9510
SOURCE (Princeton)NM_006988
Genomic and cartography
GoldenPath (UCSC)ADAMTS1  -  21q21.3   chr21:28208606-28217728 -  21q21.3   [Description]    (hg19-Feb_2009)
EnsemblADAMTS1 - 21q21.3 [CytoView]
Mapping of homologs : NCBIADAMTS1 [Mapview]
OMIM605174   
Gene and transcription
Genbank (Entrez)AB037767 AF060152 AF170084 AF207664 AK023795
RefSeq transcript (Entrez)NM_006988
RefSeq genomic (Entrez)AC_000153 NC_000021 NC_018932 NT_011512 NW_001838706 NW_004929426
Consensus coding sequences : CCDS (NCBI)ADAMTS1
Cluster EST : UnigeneHs.643357 [ NCBI ]
CGAP (NCI)Hs.643357
Alternative Splicing : Fast-db (Paris)GSHG0019605
Alternative Splicing GalleryENSG00000154734
Gene ExpressionADAMTS1 [ NCBI-GEO ]     ADAMTS1 [ SEEK ]   ADAMTS1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UHI8 (Uniprot)
NextProtQ9UHI8  [Medical]
With graphics : InterProQ9UHI8
Splice isoforms : SwissVarQ9UHI8 (Swissvar)
Catalytic activity : Enzyme3.4.24.- [ Enzyme-Expasy ]   3.4.24.-3.4.24.- [ IntEnz-EBI ]   3.4.24.- [ BRENDA ]   3.4.24.- [ KEGG ]   
Domaine pattern : Prosite (Expaxy)ADAM_MEPRO (PS50215)    TSP1 (PS50092)    ZINC_PROTEASE (PS00142)   
Domains : Interpro (EBI)ADAM_Cys-rich    ADAM_spacer1    MetalloPept_cat_dom    Pept_M12B_ADAM-TS1    Peptidase_M12B    Peptidase_M12B_ADAM-TS    Peptidase_M12B_N    Thrombospondin_1_rpt   
Related proteins : CluSTrQ9UHI8
Domain families : Pfam (Sanger)ADAM_spacer1 (PF05986)    Pep_M12B_propep (PF01562)    Reprolysin (PF01421)    TSP_1 (PF00090)   
Domain families : Pfam (NCBI)pfam05986    pfam01562    pfam01421    pfam00090   
Domain families : Smart (EMBL)ACR (SM00608)  TSP1 (SM00209)  
DMDM Disease mutations9510
Blocks (Seattle)Q9UHI8
PDB (SRS)2JIH    2V4B    3Q2G    3Q2H   
PDB (PDBSum)2JIH    2V4B    3Q2G    3Q2H   
PDB (IMB)2JIH    2V4B    3Q2G    3Q2H   
PDB (RSDB)2JIH    2V4B    3Q2G    3Q2H   
Human Protein AtlasENSG00000154734
Peptide AtlasQ9UHI8
HPRD05530
IPIIPI00005908   IPI00442897   IPI00980063   IPI00979702   IPI01022996   
Protein Interaction databases
DIP (DOE-UCLA)Q9UHI8
IntAct (EBI)Q9UHI8
FunCoupENSG00000154734
BioGRIDADAMTS1
IntegromeDBADAMTS1
STRING (EMBL)ADAMTS1
Ontologies - Pathways
QuickGOQ9UHI8
Ontology : AmiGOovulation from ovarian follicle  kidney development  metalloendopeptidase activity  basement membrane  cytoplasm  proteolysis  integrin-mediated signaling pathway  heparin binding  metallopeptidase activity  zinc ion binding  negative regulation of cell proliferation  cytoplasmic vesicle  heart trabecula formation  
Ontology : EGO-EBIovulation from ovarian follicle  kidney development  metalloendopeptidase activity  basement membrane  cytoplasm  proteolysis  integrin-mediated signaling pathway  heparin binding  metallopeptidase activity  zinc ion binding  negative regulation of cell proliferation  cytoplasmic vesicle  heart trabecula formation  
REACTOMEQ9UHI8 [protein]
REACTOME PathwaysREACT_118779 Extracellular matrix organization [pathway]
Protein Interaction DatabaseADAMTS1
Wikipedia pathwaysADAMTS1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)ADAMTS1
SNP (GeneSNP Utah)ADAMTS1
SNP : HGBaseADAMTS1
Genetic variants : HAPMAPADAMTS1
1000_GenomesADAMTS1 
ICGC programENSG00000154734 
CONAN: Copy Number AnalysisADAMTS1 
Somatic Mutations in Cancer : COSMICADAMTS1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
DECIPHER (Syndromes)21:28208606-28217728
Mutations and Diseases : HGMDADAMTS1
OMIM605174   
MedgenADAMTS1
GENETestsADAMTS1
Disease Genetic AssociationADAMTS1
Huge Navigator ADAMTS1 [HugePedia]  ADAMTS1 [HugeCancerGEM]
Genomic VariantsADAMTS1  ADAMTS1 [DGVbeta]
Exome VariantADAMTS1
dbVarADAMTS1
ClinVarADAMTS1
snp3D : Map Gene to Disease9510
General knowledge
Homologs : HomoloGeneADAMTS1
Homology/Alignments : Family Browser (UCSC)ADAMTS1
Phylogenetic Trees/Animal Genes : TreeFamADAMTS1
Chemical/Protein Interactions : CTD9510
Chemical/Pharm GKB GenePA24536
Clinical trialADAMTS1
Cancer Resource (Charite)ENSG00000154734
Other databases
Probes
Litterature
PubMed67 Pubmed reference(s) in Entrez
CoreMineADAMTS1
GoPubMedADAMTS1
iHOPADAMTS1

Bibliography

The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1 gene encoding an ADAM family protein with TSP motifs.
Kuno K, Iizasa H, Ohno S, Matsushima K.
Genomics. 1997a Dec 15;46(3):466-71.
PMID 9441751
 
Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene.
Kuno K, Kanada N, Nakashima E, Fujiki F, Ichimura F, Matsushima K.
J Biol Chem. 1997b Jan 3;272(1):556-62.
PMID 8995297
 
ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region.
Kuno K, Matsushima K.
J Biol Chem. 1998 May 29;273(22):13912-7.
PMID 9593739
 
ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix.
Kuno K, Terashima Y, Matsushima K.
J Biol Chem. 1999 Jun 25;274(26):18821-6.
PMID 10373500
 
METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity.
Vazquez F, Hastings G, Ortega MA, Lane TF, Oikemus S, Lombardo M, Iruela-Arispe ML.
J Biol Chem. 1999 Aug 13;274(33):23349-57.
PMID 10438512
 
ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan.
Kuno K, Okada Y, Kawashima H, Nakamura H, Miyasaka M, Ohno H, Matsushima K.
FEBS Lett. 2000 Aug 4;478(3):241-5.
PMID 10930576
 
ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function.
Shindo T, Kurihara H, Kuno K, Yokoyama H, Wada T, Kurihara Y, Imai T, Wang Y, Ogata M, Nishimatsu H, Moriyama N, Oh-hashi Y, Morita H, Ishikawa T, Nagai R, Yazaki Y, Matsushima K.
J Clin Invest. 2000 May;105(10):1345-52.
PMID 10811842
 
Expression of METH-1 and METH-2 in pancreatic cancer.
Masui T, Hosotani R, Tsuji S, Miyamoto Y, Yasuda S, Ida J, Nakajima S, Kawaguchi M, Kobayashi H, Koizumi M, Toyoda E, Tulachan S, Arii S, Doi R, Imamura M.
Clin Cancer Res. 2001 Nov;7(11):3437-43.
PMID 11705860
 
ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors.
Rodriguez-Manzaneque JC, Westling J, Thai SN, Luque A, Knauper V, Murphy G, Sandy JD, Iruela-Arispe ML.
Biochem Biophys Res Commun. 2002 Apr 26;293(1):501-8.
PMID 12054629
 
Coordinate transcription of the ADAMTS-1 gene by luteinizing hormone and progesterone receptor.
Doyle KM, Russell DL, Sriraman V, Richards JS.
Mol Endocrinol. 2004 Oct;18(10):2463-78. Epub 2004 Jul 15.
PMID 15256533
 
ADAMTS1 is essential for the development and function of the urogenital system.
Mittaz L, Russell DL, Wilson T, Brasted M, Tkalcevic J, Salamonsen LA, Hertzog PJ, Pritchard MA.
Biol Reprod. 2004 Apr;70(4):1096-105. Epub 2003 Dec 10.
PMID 14668204
 
Dynamic induction of ADAMTS1 gene in the early phase of acute myocardial infarction.
Nakamura K, Hirohata S, Murakami T, Miyoshi T, Demircan K, Oohashi T, Ogawa H, Koten K, Toeda K, Kusachi S, Ninomiya Y, Shiratori Y.
J Biochem. 2004 Oct;136(4):439-46.
PMID 15625312
 
Dysregulated expression of adamalysin-thrombospondin genes in human breast carcinoma.
Porter S, Scott SD, Sassoon EM, Williams MR, Jones JL, Girling AC, Ball RY, Edwards DR.
Clin Cancer Res. 2004 Apr 1;10(7):2429-40.
PMID 15073121
 
Fibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1.
Lee NV, Rodriguez-Manzaneque JC, Thai SN, Twal WO, Luque A, Lyons KM, Argraves WS, Iruela-Arispe ML.
J Biol Chem. 2005 Oct 14;280(41):34796-804. Epub 2005 Aug 1.
PMID 16061471
 
The hyalectan degrading ADAMTS-1 enzyme is expressed by osteoblasts and up-regulated at regions of new bone formation.
Lind T, McKie N, Wendel M, Racey SN, Birch MA.
Bone. 2005 Mar;36(3):408-17.
PMID 15777654
 
Metalloproteinase ADAMTS-1 but not ADAMTS-5 is manifold overexpressed in neurodegenerative disorders as Down syndrome, Alzheimer's and Pick's disease.
Miguel RF, Pollak A, Lubec G.
Brain Res Mol Brain Res. 2005 Jan 5;133(1):1-5.
PMID 15661359
 
Requirement for ADAMTS-1 in extracellular matrix remodeling during ovarian folliculogenesis and lymphangiogenesis.
Brown HM, Dunning KR, Robker RL, Pritchard M, Russell DL.
Dev Biol. 2006 Dec 15;300(2):699-709. Epub 2006 Oct 14.
PMID 17097630
 
ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2.
Lee NV, Sato M, Annis DS, Loo JA, Wu L, Mosher DF, Iruela-Arispe ML.
EMBO J. 2006 Nov 15;25(22):5270-83. Epub 2006 Nov 2.
PMID 17082774
 
ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis.
Lind GE, Kleivi K, Meling GI, Teixeira MR, Thiis-Evensen E, Rognum TO, Lothe RA.
Cell Oncol. 2006;28(5-6):259-72.
PMID 17167179
 
Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro- and antimetastatic activity, respectively.
Liu YJ, Xu Y, Yu Q.
Oncogene. 2006 Apr 20;25(17):2452-67.
PMID 16314835
 
Expression of ADAMs and their inhibitors in sputum from patients with asthma.
Paulissen G, Rocks N, Quesada-Calvo F, Gosset P, Foidart JM, Noel A, Louis R, Cataldo DD.
Mol Med. 2006 Jul-Aug;12(7-8):171-9.
PMID 17088949
 
Expression and significance of a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-1 in an animal model of renal interstitial fibrosis induced by unilateral ureteral obstruction.
Nakamura A, Sakai Y, Ohata C, Komurasaki T.
Exp Toxicol Pathol. 2007 Sep;59(1):1-7. Epub 2007 Jun 20.
PMID 17583485
 
Renal ischemia reperfusion inhibits VEGF expression and induces ADAMTS-1, a novel VEGF inhibitor
Basile DP, Fredrich K, Chelladurai B, Leonard EC, Parrish AR.
Am J Physiol Renal Physiol. 2008 Apr;294(4):F928-36. Epub 2008 Feb 13.
PMID 18272597
 
Aberrant methylation of ADAMTS1 in non-small cell lung cancer.
Choi JE, Kim DS, Kim EJ, Chae MH, Cha SI, Kim CH, Jheon S, Jung TH, Park JY.
Cancer Genet Cytogenet. 2008 Dec;187(2):80-4.
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Contributor(s)

Written01-2009Natacha Rocks, Didier Cataldo
Laboratory of Tumor and Developmental Biology, GIGA-research, CHU Sart-Tilman, B-4000 Liege, Belgique

Citation

This paper should be referenced as such :
Rocks, N ; Cataldo, D
ADAMTS1 (ADAM metallopeptidase with thrombospondin type 1 motif, 1)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(12):901-906.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/ADAMTS1ID574ch21q21.html

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