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G-protein coupled receptors regulates Tauopathy in neurodegeneration.
Chinnathambi, Subashchandrabose; Chidambaram, Hariharakrishnan.
Affiliation
  • Chinnathambi S; Department of Neurochemistry, National Institute of Mental Health and Neuro Sciences (NIMHANS), Institute of National Importance, Bangalore, Karnataka, India. Electronic address: subashneuro@nimhans.ac.in.
  • Chidambaram H; Department of Neurochemistry, National Institute of Mental Health and Neuro Sciences (NIMHANS), Institute of National Importance, Bangalore, Karnataka, India.
Adv Protein Chem Struct Biol ; 141: 467-493, 2024.
Article de En | MEDLINE | ID: mdl-38960483
ABSTRACT
In Alzheimer's disease, the microtubule-associated protein, Tau misfolds to form aggregates and filaments in the intra- and extracellular region of neuronal cells. Microglial cells are the resident brain macrophage cells involved in constant surveillance and activated by the extracellular deposits. Purinergic receptors are involved in the chemotactic migration of microglial cells towards the site of inflammation. From our recent study, we have observed that the microglial P2Y12 receptor is involved in phagocytosis of full-length Tau species such as monomers, oligomers and aggregates by actin-driven chemotaxis. This study shows the interaction of repeat-domain of Tau (TauRD) with the microglial P2Y12 receptor and the corresponding residues for interaction have been analyzed by various in-silico approaches. In the cellular studies, TauRD was found to interact with microglial P2Y12R and induces its cellular expression confirmed by co-immunoprecipitation and western blot analysis. Furthermore, the P2Y12R-mediated TauRD internalization has demonstrated activation of microglia with an increase in the Iba1 level, and TauRD becomes accumulated at the peri-nuclear region for the degradation.
Sujet(s)

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Tauopathies Limites: Animals / Humans Langue: En Journal: Adv Protein Chem Struct Biol Sujet du journal: BIOLOGIA / BIOQUIMICA Année: 2024 Type de document: Article Pays de publication: Pays-Bas

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Tauopathies Limites: Animals / Humans Langue: En Journal: Adv Protein Chem Struct Biol Sujet du journal: BIOLOGIA / BIOQUIMICA Année: 2024 Type de document: Article Pays de publication: Pays-Bas