Literature DB >> 27493839

Pathophysiological Function of ADAMTS Enzymes on Molecular Mechanism of Alzheimer's Disease.

Murat Serdar Gurses1, Mustafa Numan Ural1, Mehmet Akif Gulec2, Omer Akyol3, Sumeyya Akyol4.   

Abstract

The 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.

Entities:  

Keywords:  ADAM; ADAMTS; Alzheimer’s disease; matrix metalloproteinases; neurodegeneration

Year:  2016        PMID: 27493839      PMCID: PMC4963191          DOI: 10.14336/AD.2016.0111

Source DB:  PubMed          Journal:  Aging Dis        ISSN: 2152-5250            Impact factor:   6.745


  83 in total

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Review 2.  A review of the ADAMTS family, pharmaceutical targets of the future.

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5.  Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura.

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Journal:  Nature       Date:  2001-10-04       Impact factor: 49.962

Review 6.  The non-amyloidogenic pathway: structure and function of alpha-secretases.

Authors:  Elzbieta Kojro; Falk Fahrenholz
Journal:  Subcell Biochem       Date:  2005

Review 7.  Regulation of APP cleavage by alpha-, beta- and gamma-secretases.

Authors:  J Nunan; D H Small
Journal:  FEBS Lett       Date:  2000-10-13       Impact factor: 4.124

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Authors:  Rolf Postina; Anja Schroeder; Ilse Dewachter; Juergen Bohl; Ulrich Schmitt; Elzbieta Kojro; Claudia Prinzen; Kristina Endres; Christoph Hiemke; Manfred Blessing; Pascaline Flamez; Antoine Dequenne; Emile Godaux; Fred van Leuven; Falk Fahrenholz
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Review 9.  The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics.

Authors:  John Hardy; Dennis J Selkoe
Journal:  Science       Date:  2002-07-19       Impact factor: 47.728

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Authors:  Joanne Mayer; Michelle G Hamel; Paul E Gottschall
Journal:  BMC Neurosci       Date:  2005-08-25       Impact factor: 3.288

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2.  Genome-wide meta-analysis identifies new loci and functional pathways influencing Alzheimer's disease risk.

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Journal:  Nat Genet       Date:  2019-01-07       Impact factor: 38.330

Review 3.  Basal Forebrain Cholinergic Neurons: Linking Down Syndrome and Alzheimer's Disease.

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4.  Serum Glycoproteomics and Identification of Potential Mechanisms Underlying Alzheimer's Disease.

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Review 6.  New Insights into ADAMTS Metalloproteases in the Central Nervous System.

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  6 in total

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