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dc.contributor.authorFontanil T.
dc.contributor.authorMohamedi Y.
dc.contributor.authorMoncada-Pazos A.
dc.contributor.authorCobo T.
dc.contributor.authorVega J.A.
dc.contributor.authorCobo J.L.
dc.contributor.authorGarcía-Suárez O.
dc.contributor.authorCobo J.
dc.contributor.authorObaya Á.J.
dc.contributor.authorCal S.
dc.date.accessioned2020-09-02T22:17:56Z
dc.date.available2020-09-02T22:17:56Z
dc.date.issued2019
dc.identifier10.33594/000000069
dc.identifier.citation52, 5, 1003-1016
dc.identifier.issn10158987
dc.identifier.urihttps://hdl.handle.net/20.500.12728/4508
dc.descriptionBackground/Aims: The composition of the extracellular matrix (ECM) in the central nervous system (CNS) has several features that make it unique. For instance, it is remarkable for the presence of proteoglycans such as versican, brevican, and neurocan, some of which have been identified as substrates of different members of the ADAMTS family of secreted metalloproteases. Previous studies have associated ADAMTSs with the repair of the CNS, including recovery following degradation of glial scar tissue and the stimulation of axonal growth after brain injury. However, the involvement of ADAMTSs in diseases of the CNS is complex and not understood fully, and a current challenge is unraveling the precise roles of these metalloproteases in the brain. Methods: ADAMTS12 and neurocan gene expression was examined by quantitative PCR. Western blot analysis was employed to detect ADAMTS12 and neurocan protein expression in cell lines, and immunostaining techniques were used to detect neurocan in mouse brain tissues. Neurocan cleavage using recombinant ADAMTS1, ADAMTS4, ADAMTS5, and ADAMTS12 metalloproteases was evaluated by western blotting. Cell adhesion and migration were assessed using uncoated culture dishes or dishes coated with Matrigel or ECM components. Results: We identified neurocan as a novel component of brain ECM that can be cleaved by ADAMTS12. In addition, we showed that neurocan cleavage by ADAMTS12 altered the adhesive properties of the human neuroglioma H4 cell line. Moreover, immunohistochemical analysis of Adamts12-deficient mice revealed the significant accumulation of neurocan in the brain of neonatal mice. Conclusion: Overall, our results suggest that ADAMTS12 could be involved in the repair of the CNS through its ability to degrade neurocan. Moreover, it can be inferred that alterations in neurocan degradation processes could be associated with the pathogenesis of neurological disorders. © 2019 The Author(s). Published by Cell Physiol Biochem Press GmbH&Co. KG.
dc.language.isoen
dc.publisherCell Physiol Biochem Press GmbH & Co KG
dc.subjectADAMTS
dc.subjectExtracellular matrix
dc.subjectMetalloprotease
dc.subjectNeurocan
dc.subjectNeurocanase
dc.subjectADAMTS protein
dc.subjectADAMTS12 protein
dc.subjectneurocan
dc.subjectunclassified drug
dc.subjectADAMTS protein
dc.subjectADAMTS12 protein, human
dc.subjectAdamts12 protein, mouse
dc.subjectlectin
dc.subjectNCAN protein, human
dc.subjectNcan protein, mouse
dc.subjectnerve protein
dc.subjectproteochondroitin sulfate
dc.subjectproteoglycan
dc.subjectadult
dc.subjectanimal cell
dc.subjectanimal tissue
dc.subjectArticle
dc.subjectbioaccumulation
dc.subjectbrain
dc.subjectcell adhesion
dc.subjectcontrolled study
dc.subjectembryo
dc.subjectextracellular matrix
dc.subjectH4 cell line
dc.subjecthuman
dc.subjecthuman cell
dc.subjectimmunohistochemistry
dc.subjectmouse
dc.subjectneuropathy
dc.subjectnewborn
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein cleavage
dc.subjectanimal
dc.subjectbiosynthesis
dc.subjectcell motion
dc.subjectcranial neuropathy
dc.subjectgene expression regulation
dc.subjectgenetics
dc.subjectmetabolism
dc.subjectpathology
dc.subjectprotein degradation
dc.subjecttumor cell line
dc.subjectADAMTS Proteins
dc.subjectAnimals
dc.subjectCell Adhesion
dc.subjectCell Line, Tumor
dc.subjectCell Movement
dc.subjectChondroitin Sulfate Proteoglycans
dc.subjectCranial Nerve Diseases
dc.subjectGene Expression Regulation
dc.subjectHumans
dc.subjectLectins, C-Type
dc.subjectMice
dc.subjectNerve Tissue Proteins
dc.subjectProteoglycans
dc.subjectProteolysis
dc.titleNeurocan is a new substrate for the ADAMTS12 metalloprotease: Potential implications in neuropathies
dc.typeArticle


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