Редактирование: ADAMTS1

A disintegrin and metalloproteinase with thrombospondin motifs 1 precursor (EC 3.4.24.-) (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (METH-1) [KIAA1346] [METH1]

==Publications==

{{medline-entry
|title=Increased [[ADAMTS1]] mediates [[SPARC]]-dependent collagen deposition in the aging myocardium.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/27143554
|abstract=Secreted protein acidic and rich in cysteine ([[SPARC]]) is a collagen-binding matricellular protein highly expressed during fibrosis. Fibrosis is a prominent component of cardiac aging that reduces myocardial elasticity. Previously, we reported that [[SPARC]] deletion attenuated myocardial stiffness and collagen deposition in aged mice. To investigate the mechanisms by which [[SPARC]] promotes age-related cardiac fibrosis, we evaluated six groups of mice (n = 5-6/group): young (3-5 mo old), middle-aged (10-12 mo old), and old (18-29 mo old) C57BL/6 wild type (WT) and [[SPARC]]-null (Null) mice. Collagen content, determined by picrosirius red staining, increased in an age-dependent manner in WT but not in Null mice. A disintegrin and metalloproteinase with thrombospondin-like motifs 1 ([[ADAMTS1]]) increased in middle-aged and old WT compared with young, whereas in Null mice only old animals showed increased [[ADAMTS1]] expression. Versican, a substrate of [[ADAMTS1]], decreased with age only in WT. To assess the mechanisms of [[SPARC]]-induced collagen deposition, we stimulated cardiac fibroblasts with [[SPARC]]. [[SPARC]] treatment increased secretion of collagen I and [[ADAMTS1]] (both the 110-kDa latent and 87-kDa active forms) into the conditioned media as well as the cellular expression of transforming growth factor-β1-induced protein (Tgfbi) and phosphorylated Smad2. An [[ADAMTS1]] blocking antibody suppressed the [[SPARC]]-induced collagen I secretion, indicating that [[SPARC]] promoted collagen production directly through [[ADAMTS1]] interaction. In conclusion, [[ADAMTS1]] is an important mediator of [[SPARC]]-regulated cardiac aging.
|mesh-terms=* ADAMTS1 Protein
* Aging
* Animals
* Cells, Cultured
* Collagen
* Extracellular Matrix
* Extracellular Matrix Proteins
* Female
* Fibroblasts
* Male
* Mice
* Mice, Inbred C57BL
* Mice, Knockout
* Myocardium
* Osteonectin
* Signal Transduction
* Up-Regulation
|keywords=* a disintegrin and metalloproteinase with thrombospondin-like motifs 1
* fibroblast
* heart
* matrix metalloproteinase
* secreted protein acidic and rich in cysteine
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4935141
}}
{{medline-entry
|title=[[ADAMTS9]] is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cells.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/20093484
|abstract=The metalloprotease [[ADAMTS9]] participates in melanoblast development and is a tumor suppressor in esophageal and nasopharyngeal cancer. [[ADAMTS9]] null mice die before gastrulation, but, [[ADAMTS9]] /- mice were initially thought to be normal. However, when congenic with the C57Bl/6 strain, 80% of [[ADAMTS9]] /- mice developed spontaneous corneal neovascularization. beta-Galactosidase staining enabled by a lacZ cassette targeted to the [[ADAMTS9]] locus showed that capillary endothelial cells (ECs) in embryonic and adult tissues and in capillaries growing into heterotopic tumors expressed [[ADAMTS9]]. Heterotopic B.16-[[F10]] melanomas elicited greater vascular induction in [[ADAMTS9]] /- mice than in wild-type littermates, suggesting a potential inhibitory role in tumor angiogenesis. Treatment of cultured human microvascular ECs with [[ADAMTS9]] small-interfering RNA resulted in enhanced filopodial extension, decreased cell adhesion, increased cell migration, and enhanced formation of tube-like structures on Matrigel. Conversely, overexpression of catalytically active, but not inactive, [[ADAMTS9]] in ECs led to fewer tube-like structures, demonstrating that the proteolytic activity of [[ADAMTS9]] was essential. However, unlike the related metalloprotease [[ADAMTS1]], which exerts anti-angiogenic effects by cleavage of thrombospondins and sequestration of vascular endothelial growth factor165, [[ADAMTS9]] neither cleaved thrombospondins 1 and 2, nor bound vascular endothelial growth factor165. Taken together, these data identify [[ADAMTS9]] as a novel, constitutive, endogenous angiogenesis inhibitor that operates cell-autonomously in ECs via molecular mechanisms that are distinct from those used by [[ADAMTS1]].
|mesh-terms=* ADAM Proteins
* ADAMTS9 Protein
* Aging
* Animals
* Biocatalysis
* Cell Movement
* Corneal Neovascularization
* Embryo, Mammalian
* Endothelial Cells
* Enzyme Activation
* Gene Knockdown Techniques
* Humans
* Mice
* Mice, Inbred C57BL
* Microvessels
* Neoplasm Transplantation
* Neoplasms
* Neovascularization, Pathologic
* Organ Specificity
* Phosphorylation
* RNA, Messenger
* RNA, Small Interfering
* Receptors, Vascular Endothelial Growth Factor
* Thrombospondin 1
* Thrombospondins
* Vascular Endothelial Growth Factor A

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2832168
}}