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Journal articles on the topic 'ADAMTS 1 e 4'

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Published: 4 June 2021

Last updated: 2 February 2022

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1

TURNER, SHARON L., DAVID MANGNALL, NIGEL C. BIRD, ROWENA A. D. BUNNING, and MARIA E. BLAIR-ZAJDEL. "Expression of ADAMTS-1, ADAMTS-4, ADAMTS-5 and TIMP3 by hepatocellular carcinoma cell lines." International Journal of Oncology 41, no. 3 (2012): 1043–49. http://dx.doi.org/10.3892/ijo.2012.1525.

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2

Lim, Ngee H., Masahide Kashiwagi, Robert Visse, et al. "Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications." Biochemical Journal 431, no. 1 (2010): 113–22. http://dx.doi.org/10.1042/bj20100725.

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We have reported previously that reactive-site mutants of N-TIMP-3 [N-terminal inhibitory domain of TIMP-3 (tissue inhibitor of metalloproteinases 3)] modified at the N-terminus, selectively inhibited ADAM17 (a disintegrin and metalloproteinase 17) over the MMPs (matrix metalloproteinases). The primary aggrecanases ADAMTS (ADAM with thrombospondin motifs) -4 and -5 are ADAM17-related metalloproteinases which are similarly inhibited by TIMP-3, but are poorly inhibited by other TIMPs. Using a newly developed recombinant protein substrate based on the IGD (interglobular domain) of aggrecan, gst-I

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3

Haddock, G., A. K. Cross, J. Plumb, et al. "Expression of ADAMTS-1, -4, -5 and TIMP-3 in normal and multiple sclerosis CNS white matter." Multiple Sclerosis Journal 12, no. 4 (2006): 386–96. http://dx.doi.org/10.1191/135248506ms1300oa.

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ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) -1, -4 and -5 proteases have been identified in the CNS at the mRNA level. These glutamyl endopeptidases, inhibited by tissue inhibitor of metalloproteinases (TIMP)-3, are key enzymes in the degradation of the aggregating chondroitin sulphate proteoglycans (CSPGs), and may therefore play a role in CNS extracellular matrix (ECM) changes in multiple sclerosis (MS). We have investigated ADAMTS and TIMP-3 expression in normal and MS CNS white matter by real-time RT-PCR, western blotting and immunohistochemistry. We report for

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4

Tajima, Takuya, Nami Yamaguchi, Takuji Yokoe, Etsuo Chosa, and Yudai Morita. "A possible issue of articular cartilage degeneration in acute phase after anterior cruciate ligament reconstruction." Orthopaedic Journal of Sports Medicine 9, no. 7_suppl4 (2021): 2325967121S0021. http://dx.doi.org/10.1177/2325967121s00218.

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Objectives: Intra-articular hematoma are caused by articular injury such as ligament rupture or intra-articular fracture and following knee surgery. It has been reported that intra-articular hematoma leads to cartilage degeneration. Exposure of articular cartilage to low concentrations of blood for a period as short as 2 days has been confirmed to induce the irreversible cartilage damage. Anterior cruciate ligament (ACL) injury is increased risk for developing posttraumatic osteoarthritis (OA). Despite improvement in ACL reconstruction (ACLR), the incidence of posttraumatic OA has remained rel

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5

Yoshida, Koji, Yasuyuki Suzuki, Akio Saito, Kanji Fukuda, Chiaki Hamanishi та Hiroshi Munakata. "Aggrecanase-1 (ADAMTS-4) interacts with α1-antitrypsin". Biochimica et Biophysica Acta (BBA) - General Subjects 1725, № 2 (2005): 152–59. http://dx.doi.org/10.1016/j.bbagen.2005.06.009.

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6

Tortorella, Micky D., Elizabeth C. Arner, Robert Hills, et al. "ADAMTS-4 (aggrecanase-1): N-Terminal activation mechanisms." Archives of Biochemistry and Biophysics 444, no. 1 (2005): 34–44. http://dx.doi.org/10.1016/j.abb.2005.09.018.

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7

Mao, Guping, Peihui Wu, Ziji Zhang та ін. "MicroRNA-92a-3p Regulates Aggrecanase-1 and Aggrecanase-2 Expression in Chondrogenesis and IL-1β-Induced Catabolism in Human Articular Chondrocytes". Cellular Physiology and Biochemistry 44, № 1 (2017): 38–52. http://dx.doi.org/10.1159/000484579.

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Background/Aims: Aggrecanase-1 (ADAMTS-4) and aggrecanase-2 (ADAMTS-5) are secreted enzymes belonging to the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family that play significant roles in the progression of osteoarthritis (OA). Here, we aimed to determine whether the expression of ADAMTS-4/5 in chondrogenesis and inflammation is regulated by microRNA-92a-3p (miR-92a-3p). Methods: MiR-92a-3p and ADAMTS-4/5 expressions were determined by quantitative polymerase chain reaction (qPCR). To investigate the repressive effect of miR-92a-3p on ADAMTS-4/5 expression, chond

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8

Lee, So-Young, Hyang-Sin Lee, Minchan Gil, et al. "Differential Expression Patterns of a Disintegrin and Metalloproteinase With Thrombospondin Motifs (ADAMTS) -1, -4, -5, and -14 in Human Placenta and Gestational Trophoblastic Diseases." Archives of Pathology & Laboratory Medicine 138, no. 5 (2014): 643–50. http://dx.doi.org/10.5858/arpa.2012-0227-oa.

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Context.—The ability of intermediate trophoblasts to invade maternal tissue during placentation depends on how well they can degrade the extracellular matrix. Invasion into the extracellular matrix requires many complex proteases. A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) is a novel family of secreted metalloproteinases. The ADAMTS-1, -4, -5, and -14 subtypes are known to be expressed in human placenta, but little is understood about their expression patterns. Objective.—To examine the expression patterns of ADAMTS-1, -4, -5, and -14 in specific human placenta cel

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9

Ren, Pingping, Lin Zhang, Gaiping Xu, et al. "ADAMTS-1 and ADAMTS-4 Levels Are Elevated in Thoracic Aortic Aneurysms and Dissections." Annals of Thoracic Surgery 95, no. 2 (2013): 570–77. http://dx.doi.org/10.1016/j.athoracsur.2012.10.084.

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10

Santamaria, Salvatore, and Rens de Groot. "ADAMTS proteases in cardiovascular physiology and disease." Open Biology 10, no. 12 (2020): 200333. http://dx.doi.org/10.1098/rsob.200333.

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The a disintegrin-like and metalloproteinase with thrombospondin motif (ADAMTS) family comprises 19 proteases that regulate the structure and function of extracellular proteins in the extracellular matrix and blood. The best characterized cardiovascular role is that of ADAMTS-13 in blood. Moderately low ADAMTS-13 levels increase the risk of ischeamic stroke and very low levels (less than 10%) can cause thrombotic thrombocytopenic purpura (TTP). Recombinant ADAMTS-13 is currently in clinical trials for treatment of TTP. Recently, new cardiovascular roles for ADAMTS proteases have been discovere

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11

Dancevic, Carolyn M., Daniel R. McCulloch, and Alister C. Ward. "The ADAMTS hyalectanase family: biological insights from diverse species." Biochemical Journal 473, no. 14 (2016): 2011–22. http://dx.doi.org/10.1042/bcj20160148.

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The a disintegrin-like and metalloproteinase with thrombospondin type-1 motifs (ADAMTS) family of metzincins are complex secreted proteins that have diverse functions during development. The hyalectanases (ADAMTS1, 4, 5, 8, 9, 15 and 20) are a subset of this family that have enzymatic activity against hyalectan proteoglycans, the processing of which has important implications during development. This review explores the evolution, expression and developmental functions of the ADAMTS family, focusing on the ADAMTS hyalectanases and their substrates in diverse species. This review gives an overv

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12

Shozu, M., N. Minami, H. Yokoyama, et al. "ADAMTS-1 is involved in normal follicular development, ovulatory process and organization of the medullary vascular network in the ovary." Journal of Molecular Endocrinology 35, no. 2 (2005): 343–55. http://dx.doi.org/10.1677/jme.1.01735.

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To clarify the role of disintegrin-like and metalloproteinase with thrombospondin type I motifs-1 (ADAMTS-1) in ovarian function, we examined abnormalities in ovulatory processes, folliculogenesis and the vascular system of ADAMTS-1 null ovaries. First, when immature female mice were treated with pregnant mare serum gonadotropin (PMSG)/human chorionic gonadotropin (hCG), the number of ovulated oocytes was markedly decreased in ADAMTS-1 null mice in comparision to ADAMTS-1 (+/−) controls. The proportion of anovulated follicles to total mature follicles was significantly higher in ADAMTS-1 null

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13

WESTLING, Jennifer, Paul E. GOTTSCHALL, Vivian P. THOMPSON, et al. "ADAMTS4 (aggrecanase-1) cleaves human brain versican V2 at Glu405-Gln406 to generate glial hyaluronate binding protein." Biochemical Journal 377, no. 3 (2004): 787–95. http://dx.doi.org/10.1042/bj20030896.

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Human brain tissue from cerebellum and hippocampus was obtained between 2 h and 24 h post mortem and, after extraction in the presence of proteinase inhibitors, proteoglycans were purified by anion-exchange chromatography. The versican component was characterized by Western analysis with antibodies to the N-terminal peptide (LF99), the N-terminal globular domain (12C5) and the two GAG (glycosaminoglycan) attachment regions (anti-GAG-α and anti-GAG-β). The results indicated that versican V2 is the major variant in all brain samples, and that it exists as the full-length form and also as at leas

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14

Namli Kalem, Müberra, Ziya Kalem, Batuhan Bakirarar, and Kadir Demircan. "Adamts 1, 4, 5, 8, and 9 in Early Pregnancies." Fetal and Pediatric Pathology 36, no. 5 (2017): 387–99. http://dx.doi.org/10.1080/15513815.2017.1354410.

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15

Chen, Jianjun, Yang Luo, Yong Zhou, et al. "Promotion of Tumor Growth by ADAMTS4 in Colorectal Cancer: Focused on Macrophages." Cellular Physiology and Biochemistry 46, no. 4 (2018): 1693–703. http://dx.doi.org/10.1159/000489245.

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Background/Aims: ADAMTSs (A disintegrin and metalloprotease domains with thrombospondins motifs) are a family of extracellular proteases that have been related to both oncogenic and tumor-suppressive functions. The aim of the present study was to investigate: 1) the mutation, copy-number alterations, and expression profile of ADAMTSs in colorectal cancer and 2) whether ADAMTSs participate in colorectal cancer (CRC) progression and invasion. Methods: The mutation, copy-number alterations, and expression profile of ADAMTSs in CRC were analyzed in the TCGA cohort using cBioportal. ADAMTS4 express

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16

Mladenovic, Zvezdana, Anne-Sophie Saurel, Francis Berenbaum, and Claire Jacques. "Potential Role of Hyaluronic Acid on Bone in Osteoarthritis: Matrix Metalloproteinases, Aggrecanases, and RANKL Expression are Partially Prevented by Hyaluronic Acid in Interleukin 1-stimulated Osteoblasts." Journal of Rheumatology 41, no. 5 (2014): 945–54. http://dx.doi.org/10.3899/jrheum.130378.

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Objective.To determine the effect of hyaluronic acid (HA) on proteolytic enzymes and bone remodeling mediators induced by interleukin 1β (IL-1β) and related to cartilage catabolism in murine osteoblasts.Methods.Osteoblasts were obtained from Swiss mice and cultured for 3 weeks. HA-treated osteoblasts were incubated with 100 μg/ml HA during the last week of culture, then stimulated with IL-1β (10 ng/ml) for 24 h. The expression of matrix metalloproteinases 3 and 13 (MMP-3 and MMP-13), ADAMTS-4 and ADAMTS-5, tissue inhibitor of metalloproteinases (TIMP), osteoprotegerin, and receptor activator o

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17

Shimada, Masayuki, Masahide Nishibori, Yasuhisa Yamashita, Junya Ito, Takahide Mori, and JoAnne S. Richards. "Down-Regulated Expression of A Disintegrin and Metalloproteinase with Thrombospondin-Like Repeats-1 by Progesterone Receptor Antagonist Is Associated with Impaired Expansion of Porcine Cumulus-Oocyte Complexes." Endocrinology 145, no. 10 (2004): 4603–14. http://dx.doi.org/10.1210/en.2004-0542.

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Abstract ADAMTS-1, a member of the A disintegrin and metalloproteinase family of proteases, is expressed in rodent follicles via progesterone receptor (PR)-dependent pathways. However, the functional relationship between ADAMTS-1 expression and PR has not been studied extensively in other species. In the present study, we investigated the time-dependent changes in ADAMTS-1 expression in cumulus cells of porcine cumulus-oocyte complexes (COCs), and the roles of ADAMTS-1 in cumulus expansion during in vitro maturation of oocytes. ADAMTS-1 message was not detected in cumulus cells at the time of

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18

Tortorella, Micky D., Michael Pratta, Rui-Qin Liu, et al. "Sites of Aggrecan Cleavage by Recombinant Human Aggrecanase-1 (ADAMTS-4)." Journal of Biological Chemistry 275, no. 24 (2000): 18566–73. http://dx.doi.org/10.1074/jbc.m909383199.

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19

Wayne, Gareth J., Su-Jun Deng, Augustin Amour, et al. "TIMP-3 Inhibition of ADAMTS-4 (Aggrecanase-1) Is Modulated by Interactions between Aggrecan and the C-terminal Domain of ADAMTS-4." Journal of Biological Chemistry 282, no. 29 (2007): 20991–98. http://dx.doi.org/10.1074/jbc.m610721200.

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20

Chen, Wei-Ping, Zhong-Nan Hu, Li-Bin Jin та Li-Dong Wu. "Licochalcone A Inhibits MMPs and ADAMTSs via the NF-κB and Wnt/β-Catenin Signaling Pathways in Rat Chondrocytes". Cellular Physiology and Biochemistry 43, № 3 (2017): 937–44. http://dx.doi.org/10.1159/000481645.

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Background: Osteoarthritis (OA) is a joint disease in which cartilage degradation is the central pathological change. In this study, we investigated the anti-osteoarthritic effects of licochalcone A (Lico A) in rat chondrocytes. Methods: Polymerase chain reaction and Western blotting were performed to evaluate the expression of a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-5, ADAMTS-4, collagen II, matrix metalloproteinase (MMP)-13 and MMP-1 at both the gene and protein levels, respectively. In addition, the wnt/β-catenin and nuclear factor kappa B (NF-κB) signaling p

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21

Scully, Marie, Richard Starke, Ian Mackie, and Samuel J. Machin. "Acute Idiopathic Thrombotic Thrombocytopenic Purpura: Predicting Relapse and Response to Treatment." Blood 108, no. 11 (2006): 1059. http://dx.doi.org/10.1182/blood.v108.11.1059.1059.

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Abstract Thrombotic thrombocytopenic purpura (TTP) is an acute, life threatening disorder. Idiopathic, antibody mediated disease accounts for 70% of cases of acute TTP, primarily IgG. We reviewed all cases of acute idiopathic TTP with serial samples available from diagnosis, relapse and in clinical remission to determine if there were factors predicting relapse and the benefit of Rituximab in preventing further episodes. All 25 cases presented with ADAMTS 13 activity <5%(NR 66–126%), during an acute TTP episode. Group A received Rituximab: 3 males and 10 females, the median age of presentat

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22

Vazquez Mellado, Alberto, Olga Graciela Cantu-Rodriguez, Myrna Pequeño-Luévano, et al. "Low Dose Rituximab and Plasma Exchange As Frontline Therapy for Patients with Thrombotic Thrombocytopenic Purpura." Blood 126, no. 23 (2015): 2257. http://dx.doi.org/10.1182/blood.v126.23.2257.2257.

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Abstract Thrombotic thombocytopenic purpura (TTP) is characterized by a reduction in the von Willebrand cleavage protein ADAMTS-13, caused mainly by autoimmunity. Plasmapheresis is the standard of care achieving complete remission (CR) in 77-83% of cases but figures are variable depending on clinical context and ADAMTS-13 activity. Relapse is frequent in patients with <10% ADAMTS-13, and has been reported in 34-41% of cases. In most of these patients, an inhibitor against ADAMS-13 is detected thus, an effective frontline immunosuppressive treatment is needed to prevent relapses. Originally

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23

Vankemmelbeke, Mireille N., Gavin C. Jones, Cyprianne Fowles, et al. "Selective inhibition of ADAMTS-1, -4 and -5 by catechin gallate esters." European Journal of Biochemistry 270, no. 11 (2003): 2394–403. http://dx.doi.org/10.1046/j.1432-1033.2003.03607.x.

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24

Keller, Kate E., John M. Bradley, and Ted S. Acott. "Differential Effects of ADAMTS-1, -4, and -5 in the Trabecular Meshwork." Investigative Opthalmology & Visual Science 50, no. 12 (2009): 5769. http://dx.doi.org/10.1167/iovs.09-3673.

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25

Flannery, Carl R., Weilan Zeng, Chris Corcoran, et al. "Autocatalytic Cleavage of ADAMTS-4 (Aggrecanase-1) Reveals Multiple Glycosaminoglycan-binding Sites." Journal of Biological Chemistry 277, no. 45 (2002): 42775–80. http://dx.doi.org/10.1074/jbc.m205309200.

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26

Dunning, K. R., C. X. Yeo, and D. L. Russell. "230. Altered matrix composition of cumulus oocyte complexes following in vitro maturation." Reproduction, Fertility and Development 17, no. 9 (2005): 90. http://dx.doi.org/10.1071/srb05abs230.

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The luteinizing hormone (LH) surge initiates cumulus expansion, through synthesis of hyaluronan and cross-linking proteins including versican, which stabilise the cumulus oocyte complex (COC) matrix. Versican is a substrate for the protease ADAMTS-1 and mRNA for each are localised to granulosa cells (GCs) and greatly induced following the LH surge. In humans, the use of in vitro maturation (IVM) of oocytes is an appealing option, reducing costs and risk of side effects associated with in vitro fertilisation. IVM oocytes are of poorer quality, likely resulting from altered gene expression and e

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27

Xia, Tianwei, Runzi Gao, Guowei Zhou, Jinzhu Liu, Jinsheng Li та Jirong Shen. "Trans-Cinnamaldehyde Inhibits IL-1β-Stimulated Inflammation in Chondrocytes by Suppressing NF-κB and p38-JNK Pathways and Exerts Chondrocyte Protective Effects in a Rat Model of Osteoarthritis". BioMed Research International 2019 (8 травня 2019): 1–12. http://dx.doi.org/10.1155/2019/4039472.

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Objective. Trans-cinnamaldehyde (TCA), a compound from Cinnamomum cassia Presl, has been reported to have anti-inflammatory effect. However, its effect on cartilage degradation in osteoarthritis is unclear. This study is designed to examine the effects of TCA on cartilage in vitro and in vivo. Material and Methods. SW1353 cells and human primary chondrocytes were treated with varying concentrations of TCA (2-20 μg/ml) for 2 h followed by IL-1β stimulation. Cell viability was examined by the MTT assay. Expression of MMP-1, MMP-3, MMP-13, ADAMTS-4, and ADAMTS-5 was examined by Western blot and R

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28

Shu, Cindy, Carl Flannery, Christopher Little, and James Melrose. "Catabolism of Fibromodulin in Developmental Rudiment and Pathologic Articular Cartilage Demonstrates Novel Roles for MMP-13 and ADAMTS-4 in C-terminal Processing of SLRPs." International Journal of Molecular Sciences 20, no. 3 (2019): 579. http://dx.doi.org/10.3390/ijms20030579.

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Background: Cartilage regeneration requires a balance of anabolic and catabolic processes. Aim: To examine the susceptibility of fibromodulin (FMOD) and lumican (LUM) to degradation by MMP-13, ADAMTS-4 and ADAMTS-5, the three major degradative proteinases in articular cartilage, in cartilage development and in osteoarthritis (OA). Methods: Immunolocalization of FMOD and LUM in fetal foot and adult knee cartilages using an FMOD matrix metalloprotease (MMP)-13 neoepitope antibody (TsYG11) and C-terminal anti-FMOD (PR184) and anti-LUM (PR353) antibodies. The in vitro digestion of knee cartilage w

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29

Wei, Yaheng, Zuoming Yang, Pengfei Guan, and Lifeng Zhang. "Expression of Galectins-1 in Rat Traumatic Osteoarthritis and Its Regulation Mechanism." Journal of Biomaterials and Tissue Engineering 9, no. 12 (2019): 1724–30. http://dx.doi.org/10.1166/jbt.2019.2190.

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Traumatic arthritis is a common orthopedic surgery disease that seriously affects the health of patients. The expression and role of Galectins in traumatic osteoarthritis remains unclear. SD rats were divided into control group and osteoarthritis model group. Real-time PCR and ELISA were used to analyze Galectins-1 expression. Chondrocytes were isolated and cultured and divided into control group, Galectins-1 siRNA group and Galectins-1 group followed by analysis of proliferation of chondrocytes by MTT assay, cell migration by Transewell chamber, expression of RUNX2 and ADAMTS-4/5 by Real-time

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Li, Zongdong, Michael Nardi, Ruimin Pan, Herman Yee, and Simon Karpatkin. "A New Mechanism of Platelet Activation and Oxidative Death Induced by ADAMTS-18 and Regulating Bleeding Time." Blood 110, no. 11 (2007): 133. http://dx.doi.org/10.1182/blood.v110.11.133.133.

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Abstract Anti-platelet integrin GPIIIa49-66 Ab obtained from HIV-ITP patients (or raised in rabbits) induces complement-independent platelet oxidative fragmentation and death by activating platelet 12-lipoxygenase (generation of 12(S)-HETE) and NADPH oxidase (JCI, 113:973, 2004). Platelet oxidative fragmentation is measured by flow cytometry of generated microparticles as well as intracellular DCFH oxidation. We now report that oxidative fragmentation in human platelets is preceded by Ca++ flux and P-selectin activation, n=6. However, the activation mechanism is different from classic platelet

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Scully, Marie, Richard Starke, Richard Lee, Ian Mackie, Samuel J. Machin, and Hannah Cohen. "Successful Pregnancy Outcome in 5 Patients with Thrombotic Thrombocytopenic Purpura." Blood 106, no. 11 (2005): 3016. http://dx.doi.org/10.1182/blood.v106.11.3016.3016.

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Abstract Pregnancy is an initiating event for acute thrombotic thrombocytopenic purpura (TTP). Patients with a history of TTP have a high risk of relapse during pregnancy with associated maternal and fetal morbidity/mortality. We report 5 TTP patients who underwent serial clinical and laboratory monitoring (haemoglobin, platelets, blood film, reticulocytes, lactate dehydrogenase (LDH), ADAMTS-13 activity and IgG antibodies) and treatment within a specialist obstetric/haematology clinic, resulting in successful pregnancy outcomes. Patients: Cases 1 and 2 presented with TTP in their first pregna

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Ding, Shi, Xuerong Zhao, Ruiting Wang, et al. "Expression of Adamts-4, Vcam-1 and Tak1 In Cartilage Tissue of Osteoarthritis." Journal of Biomaterials and Tissue Engineering 9, no. 1 (2019): 124–27. http://dx.doi.org/10.1166/jbt.2019.1944.

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Deshmukh, V., S. Grogan, T. Seo, et al. "AB0070 LORECIVIVINT (SM04690), A POTENTIAL DISEASE-MODIFYING TREATMENT FOR KNEE OSTEOARTHRITIS, DEMONSTRATED CARTILAGE-PROTECTIVE EFFECTS ON HUMAN OSTEOARTHRITIC EXPLANTS." Annals of the Rheumatic Diseases 79, Suppl 1 (2020): 1335.1–1336. http://dx.doi.org/10.1136/annrheumdis-2020-eular.6346.

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Background:Wnt pathway upregulation contributes to knee osteoarthritis (OA) through osteocyte differentiation, cartilage thinning, and inflammation. Lorecivivint (LOR; SM04690), a novel, small-molecule CLK/DYRK1A inhibitor that modulates the Wnt pathway, demonstrated disease-modifying potential for knee OA in preclinical studies.1However, the specific mechanisms by which LOR protects cartilage in knee OA are unclear.Objectives:To evaluate the cartilage-protective effects of LOR on human OA explants from total knee replacement (TKR) donors.Methods:Knee joint tissue from 22 TKR donors was obtain

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Dupuis, Loren E., E. Lockett Nelson, Brittany Hozik, et al. "Adamts5 −/− Mice Exhibit Altered Aggrecan Proteolytic Profiles That Correlate With Ascending Aortic Anomalies." Arteriosclerosis, Thrombosis, and Vascular Biology 39, no. 10 (2019): 2067–81. http://dx.doi.org/10.1161/atvbaha.119.313077.

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Objective: Investigate the requirement of Aggrecan (Acan) cleavage during aortic wall development in a murine model with ADAMTS (a disintegrin-like and metalloprotease domain with thrombospondin-type motifs) 5 deficiency and bicuspid aortic valves. Approach: Mice with altered extracellular matrix remodeling of proteoglycans will be examined for anomalies in ascending aortic wall development. Neo-epitope antibodies that recognize ADAMTS cleaved Acan fragments will be used to investigate the mechanistic requirement of Acan turnover, in aortic wall development. Results: Adamts5 −/− ;Smad2 +/− mic

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Nakamura, Megumi, Shinya Sone, Ichiro Takahashi, Itaru Mizoguchi, Seishi Echigo, and Yasuyuki Sasano. "Expression of Versican and ADAMTS1, 4, and 5 During Bone Development in the Rat Mandible and Hind Limb." Journal of Histochemistry & Cytochemistry 53, no. 12 (2005): 1553–62. http://dx.doi.org/10.1369/jhc.5a6669.2005.

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Extracellular matrix (ECM) remodeling is achieved by both production and degradation of ECM molecules during bone development. ADAMTS (a disintegrin and metalloprotease with thrombospondin type 1 motifs) constitutes a family of extracellular proteases which are implicated in cleaving the protein versican. The present study was designed to investigate the expression of versican and ADAMTS1, 4, and 5 mRNA during bone development in rat mandibles and hind limbs by RT-PCR and in situ hybridization. Versican was localized by immunohistochemistry. The process of bone development from day 14 postcoit

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Wang, Wei-Man, Gaoxiang Ge, N. H. Lim, Hideaki Nagase, and Daniel S. Greenspan. "TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2." Biochemical Journal 398, no. 3 (2006): 515–19. http://dx.doi.org/10.1042/bj20060630.

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ADAMTS-2 is an extracellular metalloproteinase responsible for cleaving the N-propeptides of procollagens I–III; an activity necessary for the formation of collagenous ECM (extracellular matrix). The four TIMPs (tissue inhibitors of metalloproteinases) regulate the activities of matrix metalloproteinases, which are involved in degrading ECM components. Here we delineate the abilities of the TIMPs to affect biosynthetic processing of procollagens. TIMP-1, -2 and -4 show no inhibitory activity towards ADAMTS-2, in addition none of the TIMPs showed inhibitory activity towards bone morphogenetic p

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Hoppensteadt, Debra, Josephine Cunanan, Jeanine M. Walenga, et al. "Von Willebrand Factor Cleaving Protease (ADAMTS-13) Antigen Levels Are Decreased in Patients with Heparin-Induced Thrombocytopenia." Blood 106, no. 11 (2005): 3970. http://dx.doi.org/10.1182/blood.v106.11.3970.3970.

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Abstract Heparin-induced thrombocytopenia (HIT) represents a complex pathologic syndrome including all components of the hemostatic system and inflammatory response. ADAMTS-13 is a metalloprotease which mediates the cleavage of von Willebrand factor (vWF) multimers. A deficiency or decreased activity of this protease may result in a TTP-related syndrome manifested by the development of intravascular platelet aggregates, thrombocytopenia, endothelial dysfunction and the deposition of vWF at thrombotic sites. Several recent reports have described decreased functionality of ADAMTS-13 in patients

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Lambert, Jordi, Kate Makin, Sophia Akbareian, et al. "ADAMTS-1 and syndecan-4 intersect in the regulation of cell migration and angiogenesis." Journal of Cell Science 133, no. 7 (2020): jcs235762. http://dx.doi.org/10.1242/jcs.235762.

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Matsukawa, Tetsuya, Tadahiro Sakai, Tomo Yonezawa, et al. "MicroRNA-125b regulates the expression of aggrecanase-1 (ADAMTS-4) in human osteoarthritic chondrocytes." Arthritis Research & Therapy 15, no. 1 (2013): R28. http://dx.doi.org/10.1186/ar4164.

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Schieppati, Francesca, Laura Russo, Marina Marchetti, et al. "Combined Elevated Anti-Adamts-13 Antibody Level and Low Adamts-13 Activity during Remission Highly Predicts Disease Relapse in a Prospective Cohort of Patients with Autoimmune Thrombotic Thrombocytopenic Purpura (TTP)." Blood 132, Supplement 1 (2018): 2443. http://dx.doi.org/10.1182/blood-2018-99-119317.

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Abstract Introduction Autoimmune TTP (aTTP) is a rare life-threatening microangiopathy characterized by hemolytic anemia, thrombocytopenia, and severe ADAMTS-13 deficiency. Daily therapeutic plasma exchange (TPE) and preemptive use of rituximab have considerably improved patient outcome. However, a high proportion of patients still experience relapse and several studies are evaluating the role of ADAMTS-13 activity and its inhibitors to predict disease recurrence. In this study, in a large prospective cohort of aTTP patients, we aimed to characterize the therapeutic approach, the clinical outc

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Sandy, John D., Jennifer Westling, Richard D. Kenagy, et al. "Versican V1 Proteolysis in Human Aortain VivoOccurs at the Glu441-Ala442Bond, a Site That Is Cleaved by Recombinant ADAMTS-1 and ADAMTS-4." Journal of Biological Chemistry 276, no. 16 (2001): 13372–78. http://dx.doi.org/10.1074/jbc.m009737200.

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Binder, Nikolaus B., Margaret Griffiths, and Helga Vetr. "A Rapid and Simple Assay for the Determination of Adamts-13 Activity." Blood 128, no. 22 (2016): 1399. http://dx.doi.org/10.1182/blood.v128.22.1399.1399.

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Abstract In recent years the determination of ADAMTS-13 activity in plasma has become an important diagnostics test in the differentiation of Thromobocytopenic Purpura (TTP) patients from those with other forms of Thrombotic micoangiopathies (TMA). Moreover, it is also useful for monitoring the effectiveness of treatment in such patients. The standard laboratory test for ADAMTS-13 Activity is an ELISA assay, which has an assay which requires 4 hours to process. This assay tends to be performed by specialized laboratories, so samples are usually batch tested. Therefore for a physician to receiv

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Fidalgo, Teresa, Patricia Martinho, Ramon Salvado, et al. "Screening for ADAMTS13 Gene Mutations in Thrombotic Thrombocytopenic Purpura Reveals a New Deletional Mutation." Blood 112, no. 11 (2008): 2300. http://dx.doi.org/10.1182/blood.v112.11.2300.2300.

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Abstract Thrombotic Thrombocytopenic Purpura (TTP) is a rare severe thrombotic microangiopathy due to the presence of ultra large von Willebrand factor (UL-vWF) multimers in circulation. The aetiology has been linked to a congenital deficiency or inhibition of the vWF-cleaving protease (ADAMTS-13) activity by autoantibodies, which neutralise the enzymatic activity or bind the protease, increasing the plasmatic clearance (non-neutralising). The presence of autoantibodies can be associated with mutations and polymorphisms (SNPs) in the ADAMTS-13 gene. The goal of this study was to characterize t

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Carmona, Jorge U., Diana L. Ríos, Catalina López, María E. Álvarez, and Jorge E. Pérez. "Proinflammatory and Anabolic Gene Expression Effects of Platelet-Rich Gel Supernatants on Equine Synovial Membrane Explants Challenged with Lipopolysaccharide." Veterinary Medicine International 2017 (2017): 1–9. http://dx.doi.org/10.1155/2017/6059485.

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Platelet-rich plasma (PRP) preparations are used in horses with osteoarthritis (OA). However, some controversies remain regarding the ideal concentration of platelets and leukocytes to produce an adequate anti-inflammatory and anabolic response in the synovial membrane. The aims of this study were to study the influence of leukoconcentrated platelet-rich gel (Lc-PRG) and leukoreduced platelet-rich gel (Lr-PRG) supernatants on the quantitative expression of some proinflammatory and anabolic genes in equine synovial membrane explants (SMEs) challenged with lipopolysaccharide (LPS). SMEs from six

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Häußler, Katja Susanne, Michael Keese, Christian Friedrich Weber, Christof Geisen, and Wolfgang Miesbach. "Prospective Evaluation of the Pre-, Intra-, and Postoperative Kinetics of ADAMTS-13, von Willebrand Factor, and Interleukin-6 in Vascular Surgery." Clinical and Applied Thrombosis/Hemostasis 26 (January 1, 2020): 107602962093027. http://dx.doi.org/10.1177/1076029620930273.

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Postoperative thrombotic thrombocytopenic purpura (TTP) shows clinical presentation similar to classical TTP, whereas exact pathophysiological contexts remain unexplained. In this study, we investigated intraoperative and postoperative changes in ADAMTS-13 (a disintegrin and metalloprotease with thrombospondin type 1 motifs, member 13), von Willebrand factor (VWF), large VWF multimers, and interleukin-6 (IL-6) in vascular surgery patients. The objective was to compare the impact of endovascular, peripheral, and aortic surgery on target parameters which are supposed to play a role in surgery-as

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Ahmad, Rasheed, Judith Sylvester, Mushtaq Ahmad, and Muhammad Zafarullah. "Adaptor Proteins and Ras Synergistically Regulate IL-1-Induced ADAMTS-4 Expression in Human Chondrocytes." Journal of Immunology 182, no. 8 (2009): 5081–87. http://dx.doi.org/10.4049/jimmunol.0803544.

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Wittwer, Arthur J., Robert L. Hills, Robert H. Keith, et al. "Substrate-Dependent Inhibition Kinetics of an Active Site-Directed Inhibitor of ADAMTS-4 (Aggrecanase 1)." Biochemistry 46, no. 21 (2007): 6393–401. http://dx.doi.org/10.1021/bi7000642.

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Chijiiwa, Miyuki, Satsuki Mochizuki, Tokuhiro Kimura, et al. "CCN1 (Cyr61) Is Overexpressed in Human Osteoarthritic Cartilage and Inhibits ADAMTS-4 (Aggrecanase 1) Activity." Arthritis & Rheumatology 67, no. 6 (2015): 1557–67. http://dx.doi.org/10.1002/art.39078.

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Liacini, Abdelhamid, and Muhammad Zafarullah. "Induction of ADAMTS-4 by interleukin-1: Comment on the article by Pratta et al." Arthritis & Rheumatism 50, no. 6 (2004): 2038–39. http://dx.doi.org/10.1002/art.20456.

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Hatano, Eiju, Takuya Fujita, Yoshimichi Ueda, et al. "Expression of ADAMTS-4 (aggrecanase-1) and Possible Involvement in Regression of Lumbar Disc Herniation." Spine 31, no. 13 (2006): 1426–32. http://dx.doi.org/10.1097/01.brs.0000219954.67368.be.

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