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Development of an Assay for Quantitation of Tau Aggregation and Tau Phosphorylation on the Basis of Non-Antibody Protein-Protein Interaction

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Development of an Assay for Quantitation of Tau Aggregation and Tau Phosphorylation on the Basis of Non-Antibody Protein-Protein Interaction

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Samenvatting

The Alzheimer’s disease (AD) is a neurodegenerative disease associated with accumulation of plaques composed of aggregated tau protein. Tau protein belongs to the family of microtubule-associated proteins; it assists in polymerization of tubulin monomers into microtubule, which are important for neuronal shape and metabolism.
Hook1, Hook2 and Hook3 are linker proteins connecting tau-microtubule to plasma membrane and various organelles. Hook3 protein was found to localize with aggregated tau. Pin1 is a protein that isomerases the bond serine (Ser) or threonine (Thr) residues in a close proximity of proline (Pro) residues. Pin1 protein only binds phosphorylated tau. Further, the tau is known to bind iron cations, which induce au phosphorylation and aggregation in AD. We researched the potential of using those protein-protein interactions to develop an indirect ELISA assay for tau detection in early AD. We found that insoluble iron (ii,iii) oxide has a prominent tau binding, thus a potential for assay development. More research is needed to drive conclusions about specificity and potential use of tau-Pin1 and tau-Hook3

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OrganisatieHZ University of Applied Sciences
OpleidingChemie
AfdelingAcademie voor Technologie & Innovatie
Domein Technology, Water & Environment
PartnerHZ University of Applied Sciences, Vlissingen
Datum2015-08-28
TypeBachelor
TaalEngels

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