Results 11 to 20 of about 380 (133)
The role of serum ADAMTS-1 levels in Hyperemesis Gravidarum
BMC Pregnancy and Childbirth, 2022 Background We aimed to investigate the levels of ADAMTS-1, which is secreted from the extracellular matrix during trophoblastic invasion in hyperemesis gravidarum (HEG).
Burcu Timur, Gurhan Guney
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ADAMTS-1 Is Found in the Nuclei of Normal and Tumoral Breast Cells. [PDF]
PLoS ONE, 2016 Proteins secreted in the extracellular matrix microenvironment (ECM) by tumor cells are involved in cell adhesion, motility, intercellular communication and invasion.
Suély V Silva +4 more
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ADAMTS-1 Expression in Cumulus Cells: A Biomarker for Oocyte Maturity [PDF]
پزشکی بالینی ابن سینا, 2018 Background and Objective: Cumulus cells regulate oocyte maturation through bilateral communication during follicular growth. Expression of disintegrin-like and metalloproteinase with thrombospondin type I motifs-1 (ADAMTS-1) is essential for structural ...
Sepide Gohari Taban +6 more
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Role of adamts-1 in pleomorphic xanthoastrocytoma tumor cells progression [PDF]
Turkish Neurosurgery, 2021 To analyze the expression of ADAMTS-1, NF-?B, and STAT3 in human pleomorphic xanthoastrocytoma specimens, and their correlation with glioma advancement.Pleomorphic xanthoastrocytoma tumor cell lines were treated with low and high doses of cytokines at 24 and 48 hours (h) to replicate the inflammatory environment.
Gokce, Aysun +2 more
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ADAMTS‐1 cleaves a cartilage proteoglycan, aggrecan [PDF]
FEBS Letters, 2000 A disintegrin‐like and metalloproteinase with thrombospondin type I motifs‐1 (ADAMTS‐1) is an extracellular matrix‐anchored metalloproteinase. In this study we have demonstrated that ADAMTS‐1 is able to cleave a major cartilage proteoglycan, aggrecan.
Kuno, Kouji +6 more
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Identification of Prodomain Determinants Involved in ADAMTS-1 Biosynthesis [PDF]
Journal of Biological Chemistry, 2004 The metalloprotease ADAMTS-1 (a disintegrin and metalloprotease with thrombospondin type I motif), similarly to other members of the ADAMTS family, is initially synthesized as a zymogen, proADAMTS-1, that undergoes proteolytic processing at the prodomain/catalytic domain junction by serine proteinases of the furin-like family of proprotein convertases.
Jean-Michel, Longpré, Richard, Leduc
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ADAMTS-1 Is an Active Metalloproteinase Associated with the Extracellular Matrix [PDF]
Journal of Biological Chemistry, 1999 Cellular disintegrin and metalloproteinases (ADAMs) are a family of genes with a sequence similar to the snake venom metalloproteinases and disintegrins. ADAMTS-1 is a unique ADAM family protein with respect to the presence of thrombospondin type I motifs and the capacity to bind to the extracellular matrix.
K, Kuno, Y, Terashima, K, Matsushima
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The Mechanism and Role of ADAMTS Protein Family in Osteoarthritis
Biomolecules, 2022 Osteoarthritis (OA) is a principal cause of aches and disability worldwide. It is characterized by the inflammation of the bone leading to degeneration and loss of cartilage function.
Ting Li +5 more
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ADAMTS-1 and syndecan-4 intersect in the regulation of cell migration and angiogenesis [PDF]
Journal of Cell Science, 2020 ABSTRACT ADAMTS-1 is an extracellular protease with critical roles in organogenesis and angiogenesis. Here we demonstrate a functional convergence of ADAMTS-1 and the transmembrane heparan sulfate proteoglycan syndecan-4 in influencing adhesion, migration and angiogenesis.
Jordi Lambert +6 more
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Differential Effects of ADAMTS-1, -4, and -5 in the Trabecular Meshwork [PDF]
Investigative Opthalmology & Visual Science, 2009 Matrix metalloproteinases (MMPs) degrade extracellular matrix (ECM) and increase outflow facility in anterior segment perfusion culture. One group is the ADAMTSs (a disintegrin and metalloproteinase with thrombospondin type 1 motifs). In this study, the authors examined the effects of ADAMTS-1, -4, and -5 on outflow facility and investigated their mRNA
Kate E, Keller +2 more
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