RESUMO
Mutations in the triggering receptor expressed in myeloid 2 (TREM2) gene have recently been found to be closely related to the development of Alzheimer's disease (AD) and other neurodegenerative diseases. However, the detailed mechanism underlying TREM2's participation in the pathogenesis of AD and other diseases has yet to be fully elucidated. In this review, we discuss current understanding on the structure and function of TREM2, the relevance between TREM2 and AD, and the possible causes of AD by TREM2 mutations.
RESUMO
ObjectiveTo understand the pathological and physiological roles of Presenilin 1 (PS1) in Alzheimer's disease (AD) recurrence, and the interaction between PSI and carhoxyl terminus of Hsc70 interacting protein (CHIP). MethodsThe yeast two-hybrid system was applied to identify a novel PS1 interacting protein as CHIP. After pGBKT7-PS1-C203 bait plasmid and full fragement CHIP of pACT2-CHIP expression vector were constructed, the interaction between PSI and CHIP was tested by β-galactosidase assay, pGBKT7-PS1-C203 was co-transfected with pACT2-CHIP into 293T cells and the interaction between PS1 and CHIP was tested by co-immunoprecipitation and Western blot. ResultsSpecificity of the interaction between PS1 and CHIP was identified by β-galactosidase assay and co- immunoprecipitation. ConclusionsCHIP is able to modulate chaperone functions and the pathway of protein ubiquitination/degradation. CHIP may regulate a proper assembly of the γ-secretase complex through its interaction with PSI, which is helpful to elucidate the mechanism of AD pathology.
