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

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Gürses, Murat Serdar
Ural, Mustafa Numan

Yazarlar

Güleç, Mehmet Akif
Akyol, Ömer
Akyol, Sümeyya

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Int Soc Aging & Disease

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Özet

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.

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Geriatrics & gerontology, Matrix metalloproteinases, ADAM, ADAMTS, Alzheimer's disease, Neurodegeneration, Amyloid precursor protein, Central-nervous-system, Spinal-cord-injury, Chondroitin sulfate proteoglycans, Alpha-secretase adam10, Thrombospondin motifs, Extracellular-matrix, Tau-protein, Proteolytic cleavage, Reelin expression

Alıntı

Gürses, M. S. vd. (2016). "Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer's disease". Aging and Disease", 7(4), 479-490.

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