Přejít k hlavnímu obsahu

Přihlášení pro studenty

Přihlášení pro zaměstnance

Publikace detail

Phosphorylation of tau protein by soluble and immobilized kinases
Autoři: Strouhalová Eliška | Hromádková Lenka | Kupčík Rudolf | Slováková Marcela | Bílková Zuzana
Rok: 2019
Druh publikace: ostatní - přednáška nebo poster
Strana od-do: nestránkováno
Tituly:
Jazyk Název Abstrakt Klíčová slova
eng Phosphorylation of tau protein by soluble and immobilized kinases Phosphorylation is a significant post-translational modification of proteins. Phosphorylation is catalyzed by kinases and is based on the transfer of the phosphate group from adenosine triphosphate to the hydroxyl group of serine, threonine or tyrosine [1]. Phosphorylation is involved in the regulation of protein functions, intercellular communication, cell proliferation, differentiation and apoptosis [2]. Tau protein is a diagnostically significant phosphoprotein with 85 potential phosphorylation sites [3]. Tau protein is phosphorylated at about 18 phosphorylation sites under physiological conditions. In the case of Alzheimer's disease, tau protein is hyperphosphorylated [4]. The aim of our study is to prepare phosphorylated protein standards for detection and quantification of hyperphosphorylated tau in cerebrospinal fluid of patients with Alzheimer’s disease. Recombinant tau protein was phosphorylated by soluble and immobilized kinases on magnetic particles and final products of catalyzed reaction were evaluated by mass spectrometry. The advantages of immobilized kinases include product purity, separation of the enzyme from the reaction, reuse of carrier with enzyme and enzyme change. 1. Lodish H., Berk A., Matsudaira P., Kaiser CA., Krieger M., Scott MP., Zipursky SL., Darnell J., Molecular cell biology (5th Edition), W. H. Freeman and Company, New York, 2004. 2. Manning G., Whyte DB., Martinez R., Hunter T., Sudarsanam S., Science 2002, 298(5600), 1912-1934. 3. Martin L., Latypova X., Terro F., Neurochemistry International 2011, 58(4), 458-471. 4. Prokopovich DV., Whittaker JW., Muthee MM., Ahmed A., Larini L., The Journal of Physical Chemistry B 2017, 121(9), 2095-2103. Phosphorylation; tau; immobilized; kinases