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Review
. 2016 Jan 11;7(4):479-90.
doi: 10.14336/AD.2016.0111. eCollection 2016 Aug.

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

Murat Serdar Gurses  1 , Mustafa Numan Ural  1 , Mehmet Akif Gulec  2 , Omer Akyol  3 , Sumeyya Akyol  4
Affiliations
Review

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

Murat Serdar Gurses et al. Aging Dis. .

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.

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

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Figures

Figure 1.
Figure 1.
Domain structure of ADAMTS proteins (It was adapted from Apte SS [7] and Stanton et al. [11])
Figure 2.
Figure 2.
The representation of the effects of ADAMTS on Tau production. Reelin binds to its receptors and activates phosphatidylinositol-3-kinase (PI3K) and protein kinase B (PKB/Akt). It leads a remarkable inhibition in glycogen synthase kinase 3β (GSK3β), which is an enzyme that regulates phosphorylation of the microtubule-stabilizing protein tau. After ADAMTS digest Reelin, depressed reelin level may in turn increase tau phosphorylation at the end of the signaling pathway. (It was adapted from the resources Krstic D [57], Hisanaga A [82], and Yu NN [83]).
See this image and copyright information in PMC

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References

    1. Hardy J, Selkoe DJ (2002). The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science, 297: 353-356. - PubMed
    1. Kuno K, Kanada N, Nakashima E, Fujiki F, Ichimura F, Matsushima K (1997). Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J Biol Chem, 272: 556-562. - PubMed
    1. Nardi JB, Martos R, Walden KK, Lampe DJ, Robertson HM (1999). Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta. Insect Biochem Mol Biol, 29: 883-897. - PubMed
    1. Bork P, Beckmann G (1993). The CUB domain. A widespread module in developmentally regulated proteins. J Mol Biol, 231: 539-545. - PubMed
    1. Baenziger NL, Brodie GN, Majerus PW (1971). A thrombin-sensitive protein of human platelet membrane. Proc Natl Acad Sci USA, 68: 240-243. - PMC - PubMed

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