| ADAMTS4 is a crucial proteolytic enzyme for versican cleavage in the amnion at parturition. | ADAMTS4 is a crucial proteolytic enzyme for versican cleavage in the amnion at parturition.
Li MD, Lu JW, Zhang F, Lei WJ, Pan F, Lin YK, Ling LJ, Myatt L, Wang WS, Sun K., Free PMC Article | 03/28/2024 |
| Decreased miR-329-3p upregulates Adamts4 and Dnajb1 in mouse hepatic I/R injury in an age-independent manner. | Decreased miR-329-3p upregulates Adamts4 and Dnajb1 in mouse hepatic I/R injury in an age-independent manner.
Zhu L, Duan W, Yang B, Wang L., Free PMC Article | 10/30/2023 |
| ADAMTS4 Enhances Oligodendrocyte Differentiation and Remyelination by Cleaving NG2 Proteoglycan and Attenuating PDGFRalpha Signaling. | ADAMTS4 Enhances Oligodendrocyte Differentiation and Remyelination by Cleaving NG2 Proteoglycan and Attenuating PDGFRα Signaling.
Jiang C, Qiu W, Yang Y, Huang H, Dai ZM, Yang A, Tang T, Zhao X, Qiu M., Free PMC Article | 07/6/2023 |
| ADAMTS4 is involved in the production of the Alzheimer disease amyloid biomarker APP669-711. | ADAMTS4 is involved in the production of the Alzheimer disease amyloid biomarker APP669-711.
Matsuzaki M, Yokoyama M, Yoshizawa Y, Kaneko N, Naito H, Kobayashi H, Korenaga A, Sekiya S, Ikemura K, Opoku G, Hirohata S, Iwamoto S, Tanaka K, Tomita T., Free PMC Article | 05/30/2023 |
| Inhibition of ADAMTS-4 Expression in Olfactory Ensheathing Cells Enhances Recovery after Transplantation within Spinal Cord Injury. | Inhibition of ADAMTS-4 Expression in Olfactory Ensheathing Cells Enhances Recovery after Transplantation within Spinal Cord Injury.
Delarue Q, Mayeur A, Chalfouh C, Honoré A, Duclos C, Di Giovanni M, Li X, Salaun M, Dampierre J, Vaudry D, Marie JP, Guérout N. | 06/12/2021 |
| MiR-126a-5p limits the formation of abdominal aortic aneurysm in mice and decreases ADAMTS-4 expression. | MiR-126a-5p limits the formation of abdominal aortic aneurysm in mice and decreases ADAMTS-4 expression.
Li L, Ma W, Pan S, Li Y, Wang H, Wang B, Khalil RA., Free PMC Article | 05/15/2021 |
| Exuberant fibroblast activity compromises lung function via ADAMTS4. | Exuberant fibroblast activity compromises lung function via ADAMTS4.
Boyd DF, Allen EK, Randolph AG, Guo XJ, Weng Y, Sanders CJ, Bajracharya R, Lee NK, Guy CS, Vogel P, Guan W, Li Y, Liu X, Novak T, Newhams MM, Fabrizio TP, Wohlgemuth N, Mourani PM, PALISI Pediatric Intensive Care Influenza (PICFLU) Investigators, Wight TN, Schultz-Cherry S, Cormier SA, Shaw-Saliba K, Pekosz A, Rothman RE, Chen KF, Yang Z, Webby RJ, Zhong N, Crawford JC, Thomas PG., Free PMC Article | 02/20/2021 |
| ADAMTS4 was exclusively expressed in oligodendrocytes | The metalloprotease ADAMTS4 generates N-truncated Aβ4-x species and marks oligodendrocytes as a source of amyloidogenic peptides in Alzheimer's disease.
Walter S, Jumpertz T, Hüttenrauch M, Ogorek I, Gerber H, Storck SE, Zampar S, Dimitrov M, Lehmann S, Lepka K, Berndt C, Wiltfang J, Becker-Pauly C, Beher D, Pietrzik CU, Fraering PC, Wirths O, Weggen S. | 03/28/2020 |
| Aortas in Adamts-4-/- mice showed reduced elastic fiber destruction, versican degradation, macrophage infiltration, and apoptosis. Interestingly, Adamts-4 was directly involved in smooth muscle cell (SMC) apoptosis. Study findings indicate that Adamts-4 induces SMC apoptosis, degrades versican, promotes inflammatory cell infiltration, and thus contributes to sporadic aortic aneurysm and dissection development. | Critical Role of ADAMTS-4 in the Development of Sporadic Aortic Aneurysm and Dissection in Mice.
Ren P, Hughes M, Krishnamoorthy S, Zou S, Zhang L, Wu D, Zhang C, Curci JA, Coselli JS, Milewicz DM, LeMaire SA, Shen YH., Free PMC Article | 07/6/2019 |
| host-derived ADAMTS4 was expressed at the tumor vessels and was associated with early-stage tumor growth. | Host-produced ADAMTS4 Inhibits Early-Stage Tumor Growth.
Asano K, Edamatsu M, Hatipoglu OF, Inagaki J, Ono M, Ohtsuki T, Oohashi T, Hirohata S. | 11/10/2018 |
| This study demonstrated that ADAMTS-4 is a new marker of mature oligodendrocytes contributing to the myelination processes and thus to the control of motor capacities. | ADAMTS-4 in oligodendrocytes contributes to myelination with an impact on motor function.
Pruvost M, Lépine M, Leonetti C, Etard O, Naveau M, Agin V, Docagne F, Maubert E, Ali C, Emery E, Vivien D. | 06/9/2018 |
| results demonstrate for the first time that ADAMTS4 contributes to diet induced atherosclerosis in ApoE(-/-) mice | Loss of ADAMTS4 reduces high fat diet-induced atherosclerosis and enhances plaque stability in ApoE(-/-) mice.
Kumar S, Chen M, Li Y, Wong FH, Thiam CW, Hossain MZ, Poh KK, Hirohata S, Ogawa H, Angeli V, Ge R., Free PMC Article | 05/5/2018 |
| the reduction of ADAMTS-4 activity during the progression of ALS pathology may be an adaptive change to mitigate its neurodegenerative impact in CNS tissues | ADAMTS-4 promotes neurodegeneration in a mouse model of amyotrophic lateral sclerosis.
Lemarchant S, Pomeshchik Y, Kidin I, Kärkkäinen V, Valonen P, Lehtonen S, Goldsteins G, Malm T, Kanninen K, Koistinaho J., Free PMC Article | 11/12/2016 |
| Results show that ADAMTS15 and ADAMTS4 not only exhibit unique cellular expression patterns in the brain but their developmental upregulation by these cell types coincides with critical aspects of neural development | Cell-specific and developmental expression of lectican-cleaving proteases in mouse hippocampus and neocortex.
Levy C, Brooks JM, Chen J, Su J, Fox MA., Free PMC Article | 10/10/2015 |
| aggrecan and brevican proteolysis is compensated in Adamts4-/- or Adamts5-/- mice by ADAMTS proteoglycanase family members but a threshold of versican proteolysis is sensitive to the loss of a single ADAMTS proteoglycanase during spinal cord injury | ADAMTS4 and ADAMTS5 knockout mice are protected from versican but not aggrecan or brevican proteolysis during spinal cord injury.
Demircan K, Topcu V, Takigawa T, Akyol S, Yonezawa T, Ozturk G, Ugurcu V, Hasgul R, Yigitoglu MR, Akyol O, McCulloch DR, Hirohata S., Free PMC Article | 04/18/2015 |
| ADAMTS4 has roles in melanoma growth and angiogenesis in mice | ADAMTS4 and its proteolytic fragments differentially affect melanoma growth and angiogenesis in mice.
Rao N, Ke Z, Liu H, Ho CJ, Kumar S, Xiang W, Zhu Y, Ge R. | 07/13/2013 |
| The serine protease tissue plasminogen activator (tPA) and two matrix metalloproteinases, ADAMTS-4 and ADAMTS-5, were identified as Reelin cleaving enzymes. | Regulated proteolytic processing of Reelin through interplay of tissue plasminogen activator (tPA), ADAMTS-4, ADAMTS-5, and their modulators.
Krstic D, Rodriguez M, Knuesel I., Free PMC Article | 04/13/2013 |
| ADAMTS-4 cleaves Reelin in an isoform-specific manner. Among ADAMTS-4 isoforms, p50 cleaves the N-t site only, while p75 cleaves both sites. | A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAMTS-4) cleaves Reelin in an isoform-dependent manner.
Hisanaga A, Morishita S, Suzuki K, Sasaki K, Koie M, Kohno T, Hattori M. | 12/8/2012 |
| Data demonstrate that Adamts1 and Adamts4 play redundant and essential roles in perinatal kidney development. | Partially redundant functions of Adamts1 and Adamts4 in the perinatal development of the renal medulla.
Boerboom D, Lafond JF, Zheng X, Lapointe E, Mittaz L, Boyer A, Pritchard MA, DeMayo FJ, Mort JS, Drolet R, Richards JS., Free PMC Article | 12/17/2011 |
| Drastic down-regulation of Adamts4 observed at both E16 and E18; RT-PCR revealed post-natal reduction in expression (Adamts4, 1/3). Results suggest down-regulation of gene is important factor in normal odontogenesis in dental papillae. | Down-regulated genes in mouse dental papillae and pulp.
Sasaki H, Muramatsu T, Kwon HJ, Yamamoto H, Hashimoto S, Jung HS, Shimono M. | 07/26/2010 |
| proteolysis of hevin by ADAMTS4 in the mouse cerebellum is important for the normal development of this tissue | Processing of the matricellular protein hevin in mouse brain is dependent on ADAMTS4.
Weaver MS, Workman G, Cardo-Vila M, Arap W, Pasqualini R, Sage EH., Free PMC Article | 03/15/2010 |
| after stimulation, the protease activity of PC5A is enhanced, as evidenced by the cleavage of the PC5A substrates Lefty, ADAMTS-4, endothelial lipase, and PCSK9. | The regulated cell surface zymogen activation of the proprotein convertase PC5A directs the processing of its secretory substrates.
Mayer G, Hamelin J, Asselin MC, Pasquato A, Marcinkiewicz E, Tang M, Tabibzadeh S, Seidah NG. | 01/21/2010 |
| comparison of aggrecan loss with aggrecan processing in mice with single and double deletions of ADAMTS-4 and -5 activity (Deltacat) | Distinguishing aggrecan loss from aggrecan proteolysis in ADAMTS-4 and ADAMTS-5 single and double deficient mice.
Ilic MZ, East CJ, Rogerson FM, Fosang AJ, Handley CJ. | 01/21/2010 |
| Deletion of ADAMTS-4/5 provided significant protection against proteoglycan degradation ex vivo and decreased the severity of murine osteoarthritis | Double-knockout of ADAMTS-4 and ADAMTS-5 in mice results in physiologically normal animals and prevents the progression of osteoarthritis.
Majumdar MK, Askew R, Schelling S, Stedman N, Blanchet T, Hopkins B, Morris EA, Glasson SS. | 01/21/2010 |
| ADAMTS-5 is entirely responsible for cleavage in the interglobular domain, but cleavage in the chondroitin sulfate-rich region may be driven by ADAMTS-4 | ADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulfate-rich region of aggrecan.
East CJ, Stanton H, Golub SB, Rogerson FM, Fosang AJ. | 01/21/2010 |