Phosphoprotein involved in microtubule assembly and stability as well as brain development. Contains an arginine residue labelled with stable 13C and 15N isotopes
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Gendreau and Hall (2013) Tangles, Toxicity, and Tau Secretion in AD – New Approaches to a Vexing Problem. Front. Neurol. 4 PMID: 24151487
Pottiez et al (2017) Mass-Spectrometry-Based Method To Quantify in Parallel Tau and Amyloid β 1–42 in CSF for the Diagnosis of Alzheimer’s Disease. J. Proteome Res. 16(3) 1228 PMID: 28112948
Šimić et al (2016) Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies. Biomolecules 6(1) 6 PMID: 26751493
Amino acids 195-209 of tubulin-associated unit (tau). This region represents a tau tryptic peptide and is part of the core of the tau protein. Tau is a phosphoprotein involved in microtubule (MT) assembly and stability as well as brain development. Tau is phosphorylated at multiple sites by several protein kinases, including cyclic-AMP-dependent protein kinases and casein kinase type-1. Tau phosphorylation causes tau to change shape, negatively regulating its ability to stimulate MT assembly. Tau is also glycosylated, and O-glycosylation may have a role in its subcellular localisation and degradation.
Malfunctioning tau protein contributes to the structural core of the paired helical filaments (PHFs), which make up neurofibrillary tangles (NFTs). NFTs are often observed in neurodegenerative disorders, such as Alzheimer’s disease and other tauopathies. Tau is expressed from a single gene and is alternatively spliced to yield six different isoforms in the adult central nervous system (CNS).
The arginine residue at position 15 of this peptide is isotopically labelled with carbon-13 (6) and nitrogen-15 (4), giving this peptide a mass increase of 10 compared to the unlabelled peptide
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