The Molecular Chaperone Artemin Efficiently Blocks Fibrillization of TAU Protein In Vitro

Journal Title: Cell Journal(Yakhteh) - Year 2018, Vol 19, Issue 4

Abstract

Objective: Aggregation of the TAU proteins in the form of neurofibrillary tangles (NFTs) in the brain is a common risk factor in tauopathies including Alzheimer’s disease (AD). Several strategies have been implemented to target NFTs, among which chaperones, which facilitate the proper folding of proteins, appear to hold great promise in effectively inhibiting TAU polymerization. The aim of this study was to analyze the impact of the chaperone Artemin on TAU aggregation in vitro. Materials and Methods: In this experimental study, recombinant TAU- or Artemin proteins were expressed in E.coli bacteria, and purified using ion-exchange and affinity chromatography. Sodium dodecyl sulfate-poly acrylamide gel electrophoresis (SDS-PAGE) was used to run the extracted proteins and check their purity. Heparin was used as an aggregation inducer. The interaction kinetics of TAU aggregation and disassembly was performed using thioflavin T (ThT) fluorescence analysis and circular dichroism (CD) spectroscopy. Results: Ion-exchange and affinity chromatography yielded highly pure TAU and Artemin proteins for subsequent analyses. In addition, we found that heparin efficiently induced TAU fibrillization 48 hours post-incubation, as evidenced by ThT assay. Importantly, Artemin was observed to effectively block the aggregation of both physiologic- and supraphysiologic TAU concentrations in a dose-dependent manner, as judged by ThT and CD spectroscopy analyses. Conclusion: Our collective results show, for the first time, that the chaperone Artemin could significantly inhibit aggregation of the TAU proteins in a dose-dependent manner, and support Artemin as a potential potent blocker of TAU aggregation in people with AD.

Authors and Affiliations

Zahra Khosravi Anbaran, Mohammad Ali Nasiri Khalili et al. , Sharif Moradi, Reza Hassan Sajedi, Mehdi Zeinoddini

Keywords

Related Articles

The Angiogenic Chemokines Expression Profile of Myeloid Cell Lines Co-Cultured with Bone Marrow-Derived Mesenchymal Stem Cells

Objective: Angiogenesis, the process of formation of new blood vessels, is essential for development of solid tumors. At first, it was first assumed that angiogenesis is not implicated in the development of acute myeloid...

Rapid Scientific Promotion of Scientific Productions in Stem Cells According to The Indexed Papers in The ISI (web of knowledge)

Objective: In recent years emphasis has been placed on evaluation studies and the publication of scientific papers in national and international journals. In this regard the publication of scientific papers in journals i...

Generation and Characterization of Induced Pluripotent Stem Cells from Mononuclear Cells in Schizophrenic Patients

Objective: Schizophrenia (SZ) is a mental disorder in which psychotic symptoms are the main problem. The pathogenesis of SZ is not fully understood, partly because of limitations in current disease models and technology....

CD133 Is Not Suitable Marker for Isolating Melanoma Stem Cells from D10 Cell Line

Objective Cutaneous melanoma is the most hazardous malignancy of skin cancer with a high mortality rate. It has been reported that cancer stem cells (CSCs) are responsible for malignancy in most of cancers including mela...

A Pathogenic Homozygous Mutation in The Pleckstrin Homology Domain of RASA1 Is Responsible for Familial Tricuspid Atresia in An Iranian Consanguineous Family

Objective: Tricuspid atresia (TA) is a rare life-threatening form of congenital heart defect (CHD). The genetic mechanisms underlying TA are not clearly understood. According to previous studies, the endocardial cushioni...

Download PDF file
  • EP ID EP532385
  • DOI 10.22074/cellj.2018.4510
  • Views 197
  • Downloads 0

How To Cite

Zahra Khosravi Anbaran, Mohammad Ali Nasiri Khalili et al. , Sharif Moradi, Reza Hassan Sajedi, Mehdi Zeinoddini (2018). The Molecular Chaperone Artemin Efficiently Blocks Fibrillization of TAU Protein In Vitro. Cell Journal(Yakhteh), 19(4), 569-577. https://europub.co.uk/articles/-A-532385