ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells. - Wikidata - wikimedia - TriplyDB

ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells.

ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells.

http://www.wikidata.org/entity/Q38327734

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The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms Neutrophil-Derived Proteases in the Microenvironment of Pancreatic Cancer -Active Players in Tumor Progression The metalloproteinase ADAMTS1: a comprehensive review of its role in tumorigenic and metastatic pathways.Grainyhead-like 2 regulates neural tube closure and adhesion molecule expression during neural fold fusion Mig6 is a negative regulator of EGF receptor-mediated skin morphogenesis and tumor formation PGF2α-F-prostanoid receptor signalling via ADAMTS1 modulates epithelial cell invasion and endothelial cell function in endometrial cancer.ADAMTS9 is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cells.Plasminogen Tochigi mice exhibit phenotypes similar to wild-type mice under experimental thrombotic conditions.ADAM and ADAMTS gene expression in native and wound healing human lens epithelial cells Age-related differences in human skin proteoglycans.Impaired biomechanical properties of diabetic skin implications in pathogenesis of diabetic wound complications.Human Hematopoietic Signal peptide-containing Secreted 1 (hHSS1) modulates genes and pathways in glioma: implications for the regulation of tumorigenicity and angiogenesis.Expression of ADAMs and their inhibitors in sputum from patients with asthma.ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2 Proteolytic cleavage of versican and involvement of ADAMTS-1 in VEGF-A/VPF-induced pathological angiogenesis.The ADAMTS1 protease gene is required for mammary tumor growth and metastasis.Adamts1 mediates ethanol-induced alterations in collagen and elastin via a FoxO1-sestrin3-AMPK signaling cascade in myocytes.ADAMTS-18 in the host tissues exerts little effect on breast tumor progress in a murine 4T1 breast cancer model ADAMTS-1 and ADAMTS-4 levels are elevated in thoracic aortic aneurysms and dissections.Decreased expression of ADAMTS-1 in human breast tumors stimulates migration and invasion.Emerging Roles of ADAMTSs in Angiogenesis and Cancer.ADAMTS1 is a unique hypoxic early response gene expressed by endothelial cells.Adamts5, the gene encoding a proteoglycan-degrading metalloprotease, is expressed by specific cell lineages during mouse embryonic development and in adult tissues.Adrenomedullin22-52 suppresses high-glucose-induced migration, proliferation, and tube formation of human retinal endothelial cells.Genetics of breast cancer bone metastasis: a sequential multistep pattern.Lower levels of interleukin-1β gene expression are associated with impaired Langerhans' cell migration in aged human skin.Aberrant ERG expression cooperates with loss of PTEN to promote cancer progression in the prostate.Characterization and regulation of ADAMTS-16.Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.Critical Role of ADAMTS-4 in the Development of Sporadic Aortic Aneurysm and Dissection in Mice.Kaempferol targets estrogen-related receptor α and suppresses the angiogenesis of human retinal endothelial cells under high glucose conditions.Molecular Regulation of Sprouting Angiogenesis.AHR, a novel acute hypoxia-response sequence, drives reporter gene expression under hypoxia in vitro and in vivo.Effects of blocking αvβ3 integrin by a recombinant RGD disintegrin on remodeling of wound healing after induction of incisional hernia in rats.Effects of Blocking αvβ₃ integrin by a recombinant RGD disintegrin on remodeling of wound healing after induction of incisional hernia in rats.Metalloproteinase-dependent and -independent processes contribute to inhibition of breast cancer cell migration, angiogenesis and liver metastasis by a disintegrin and metalloproteinase with thrombospondin motifs-15 Protease profiling of liver fibrosis reveals the ADAM metallopeptidase with thrombospondin type 1 motif, 1 as a central activator of transforming growth factor beta

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ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells.

http://www.wikidata.org/entity/Q38327734

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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2005年學術文章

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ADAMTS1 proteinase is up-regul ...... oblasts and endothelial cells.

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type

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ADAMTS1 proteinase is up-regul ...... oblasts and endothelial cells.

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ADAMTS1 proteinase is up-regul ...... oblasts and endothelial cells.

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ADAMTS1 proteinase is up-regul ...... oblasts and endothelial cells.

@en

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M Luisa Iruela-Arispe

http://www.w3.org/2001/XMLSchema#string

Monika Krampert

http://www.w3.org/2001/XMLSchema#string

Nathan Lee

http://www.w3.org/2001/XMLSchema#string

Sandra Kuenzle

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Shelley N-M Thai

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P2860

METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity

The function of KGF in morphogenesis of epithelium and reepithelialization of wounds

Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene

ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function

Syndecan-regulated receptor signaling

Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

High-efficiency transformation of mammalian cells by plasmid DNA

ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation

ADAMTS: a novel family of extracellular matrix proteases

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25

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