Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
about
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) familyA disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanismsInsidious changes in stromal matrix fuel cancer progressionThe metalloproteinase ADAMTS1: a comprehensive review of its role in tumorigenic and metastatic pathways.Extracellular Matrix, a Hard Player in AngiogenesisBreast cancer cells induce stromal fibroblasts to secrete ADAMTS1 for cancer invasion through an epigenetic changeThe cleavage of semaphorin 3C induced by ADAMTS1 promotes cell migrationPGF2α-F-prostanoid receptor signalling via ADAMTS1 modulates epithelial cell invasion and endothelial cell function in endometrial cancer.Relevance of IGFBP2 proteolysis in glioma and contribution of the extracellular protease ADAMTS1Podocytes require the engagement of cell surface heparan sulfate proteoglycans for adhesion to extracellular matrices.The ADAMTS1 protease gene is required for mammary tumor growth and metastasis.ADAMTS-10 and -6 differentially regulate cell-cell junctions and focal adhesions.Syndecans in cartilage breakdown and synovial inflammation.Proteolytic remodeling of the synaptic cell adhesion molecules (CAMs) by metzincins in synaptic plasticity.Syndecans as modulators and potential pharmacological targets in cancer progression.Shed proteoglycans in tumor stroma.Contribution of ADAMTS1 as a tumor suppressor gene in human breast carcinoma. Linking its tumor inhibitory properties to its proteolytic activity on nidogen-1 and nidogen-2.Stroma-derived but not tumor ADAMTS1 is a main driver of tumor growth and metastasis.New and paradoxical roles of matrix metalloproteinases in the tumor microenvironment.The miR-181d-regulated metalloproteinase Adamts1 enzymatically impairs adipogenesis via ECM remodeling.Increased hypertrophic response with increased mechanical load in skeletal muscles receiving identical activity patterns.Syndecan-4: a novel regulator of collagen synthesis and deposition in the pressure-overloaded myocardium.Assessing the Influence of a Protease in Cell Migration Using the Barrier-Migration Assay.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-15Processed eggshell membrane powder regulates cellular functions and increase MMP-activity important in early wound healing processes
P2860
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P2860
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
@en
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
@nl
type
label
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
@en
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
@nl
prefLabel
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
@en
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion.
@nl
P2093
P2860
P50
P1476
Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion
@en
P2093
Darren Carpizo
M Luisa Iruela-Arispe
María del Carmen Plaza-Calonge
Shelley N-M Thai
P2860
P304
P356
10.1016/J.BIOCEL.2008.08.014
P577
2008-08-15T00:00:00Z