Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer's disease

dc.contributor.authorGüleç, Mehmet Akif
dc.contributor.authorAkyol, Ömer
dc.contributor.authorAkyol, Sümeyya
dc.contributor.buuauthorGürses, Murat Serdar
dc.contributor.buuauthorUral, Mustafa Numan
dc.contributor.departmentUludağ Üniversitesi/Tıp Fakültesi/Adli Tıp Anabilim Dalı.tr_TR
dc.contributor.orcid0000-0002-9982-0476tr_TR
dc.contributor.researcheridAAC-8913-2020tr_TR
dc.contributor.scopusid55979536300tr_TR
dc.contributor.scopusid57163358100tr_TR
dc.date.accessioned2022-12-07T12:21:38Z
dc.date.available2022-12-07T12:21:38Z
dc.date.issued2016-01-11
dc.description.abstractThe extracellular matrix (ECM) is an environment that has various enzymes attended in regeneration and restoration processes which is very important to sustain physiological and biological functions of central nervous system (CNS). One of the participating enzyme systems in ECM turnover is matrix metalloproteinases. A disintegrin-like and metalloproteinase with thrombospondin type 1 motifs (ADAMTS) is a unique family of ECM proteases found in mammals. Components of this family may be distinguished from the ADAM (A Disintegrin and Metalloproteinase) family based on the multiple copies of thrombospondin 1-like repeats. The considerable role of the ADAMTS in the CNS continues to develop. Evidences indicate that ADAMTS play an important role in neuroplasticity as well as nervous system pathologies such as Alzheimer's disease (AD). It is hopeful and possible that ADAMTS family members may be utilized to develop therapies for CNS pathologies, ischemic injuries, neurodegenerative and neurological diseases. To understand and provide definitive data on ADAMTS to improve structural and functional recovery in CNS injury and diseases, this review aimed to enlighten the subject extensively to reach certain information on metalloproteinases and related molecules/enzymes. It will be interesting to examine how ADAMTS expression and action would affect the initiation/progression of above-mentioned clinical situations, especially AD.en_US
dc.identifier.citationGürses, M. S. vd. (2016). "Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer's disease". Aging and Disease", 7(4), 479-490.en_US
dc.identifier.endpage490tr_TR
dc.identifier.issn2152-5250
dc.identifier.issue4tr_TR
dc.identifier.pubmed27493839tr_TR
dc.identifier.scopus2-s2.0-85043323988tr_TR
dc.identifier.startpage479tr_TR
dc.identifier.urihttps://doi.org/10.14336/AD.2016.0111
dc.identifier.urihttp://www.aginganddisease.org/EN/10.14336/AD.2016.0111
dc.identifier.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4963191/
dc.identifier.urihttp://hdl.handle.net/11452/29733
dc.identifier.volume7tr_TR
dc.identifier.wos000384840600006
dc.indexed.pubmedPubMeden_US
dc.indexed.scopusScopusen_US
dc.indexed.wosSCIEen_US
dc.language.isoenen_US
dc.publisherInt Soc Aging & Diseaseen_US
dc.relation.collaborationYurt içitr_TR
dc.relation.journalAging and Diseaseen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergitr_TR
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectGeriatrics & gerontologyen_US
dc.subjectMatrix metalloproteinasesen_US
dc.subjectADAMen_US
dc.subjectADAMTSen_US
dc.subjectAlzheimer's diseaseen_US
dc.subjectNeurodegenerationen_US
dc.subjectAmyloid precursor proteinen_US
dc.subjectCentral-nervous-systemen_US
dc.subjectSpinal-cord-injuryen_US
dc.subjectChondroitin sulfate proteoglycansen_US
dc.subjectAlpha-secretase adam10en_US
dc.subjectThrombospondin motifsen_US
dc.subjectExtracellular-matrixen_US
dc.subjectTau-proteinen_US
dc.subjectProteolytic cleavageen_US
dc.subjectReelin expressionen_US
dc.subject.emtreeADAMTS proteinen_US
dc.subject.emtreeAmyloid beta proteinen_US
dc.subject.emtreeAmyloid precursor proteinen_US
dc.subject.emtreeCalcium calmodulin dependent protein kinaseen_US
dc.subject.emtreeDisintegrinen_US
dc.subject.emtreeMetalloproteinaseen_US
dc.subject.emtreeMicrotubule associated proteinen_US
dc.subject.emtreeTau proteinen_US
dc.subject.emtreeThrombospondin 1en_US
dc.subject.emtreeAlzheimer diseaseen_US
dc.subject.emtreeBlood brain barrieren_US
dc.subject.emtreeBrain developmenten_US
dc.subject.emtreeChromosome 17en_US
dc.subject.emtreeCognitive defecten_US
dc.subject.emtreeDegenerative diseaseen_US
dc.subject.emtreeEhlers danlos syndromeen_US
dc.subject.emtreeExtracellular matrixen_US
dc.subject.emtreeGene expression profilingen_US
dc.subject.emtreeGene knockouten_US
dc.subject.emtreeGene mutationen_US
dc.subject.emtreeHumanen_US
dc.subject.emtreeImmunocytochemistryen_US
dc.subject.emtreeMental diseaseen_US
dc.subject.emtreeMultiple sclerosisen_US
dc.subject.emtreeNerve cell plasticityen_US
dc.subject.emtreeNerve degenerationen_US
dc.subject.emtreeNervous system injuryen_US
dc.subject.emtreeNeurite outgrowthen_US
dc.subject.emtreeNeurofibrillary tangleen_US
dc.subject.emtreeNeurologic diseaseen_US
dc.subject.emtreeNeurotoxicityen_US
dc.subject.emtreeNonhumanen_US
dc.subject.emtreeProtein aggregationen_US
dc.subject.emtreeProtein degradationen_US
dc.subject.emtreeProtein expressionen_US
dc.subject.emtreeProtein functionen_US
dc.subject.emtreeProtein structureen_US
dc.subject.emtreeReviewen_US
dc.subject.emtreeUpregulationen_US
dc.subject.emtreeWestern blottingen_US
dc.subject.scopusProtein; Disintegrins; Aggrecanaseen_US
dc.subject.wosGeriatrics & gerontologyen_US
dc.titlePathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer's diseaseen_US
dc.typeReview
dc.wos.quartileQ1en_US

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