TY - JOUR
T1 - The state of phosphorylation of normal adult brain τ, fetal τ, and τ from Alzheimer paired helical filaments at amino acid residue ser262
AU - Liu, Wan Kyng
AU - Yen, Shu Hui
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1996/3
Y1 - 1996/3
N2 - Antibody Ab262 was raised against a synthetic τ peptide (SKIGSTENLK, amino acids 258-267 of τ, termed Ser262 peptide). The antibody was more reactive with Ser262 peptide and unphosphorylated τ than a related phosphopeptide [SKIGS(P)TENLK, termed P-Ser262 peptide] and τ phosphorylated by a partially purified kinase, glycogen synthase kinase (GSK) 3β. Ab262 reacted poorly with a peptide having the sequence DRV-QSKIGSLD (amino acids 348-358). Treatment of P-Ser262 peptide or GSK 3β phosphorylated τ with alkaline phosphatase increased Ab262 immunoreactivity, indicating that Ab262 is a reagent useful for studying τ phosphorylation at the Ser262 residue. The Ab262 immunoreactivity was detected in τ from normal brains and Alzheimer paired helical filament (PHF-τ) and in PHFs. Alkaline phosphatase treatment had no effect on the Ab262 immunoreactivity of normal τ and PHF-τ but altered the Tau-1 and PHF-1 immunoreactivities. τ proteins from rat brains at 3 and 8 h postmortem exhibited 5 and 19%, respectively, more Ab262 immunoreactivity than τ from fresh tissues. In comparison, rat τ at 8 h postmortem was 40% more immunoreactive with Tau-1. The results suggest that Ser262 is not a major phosphorylation site in vivo. Moreover, there is little or no difference between PHF-τ and normal τ in the extent of phosphorylation at Ser262.
AB - Antibody Ab262 was raised against a synthetic τ peptide (SKIGSTENLK, amino acids 258-267 of τ, termed Ser262 peptide). The antibody was more reactive with Ser262 peptide and unphosphorylated τ than a related phosphopeptide [SKIGS(P)TENLK, termed P-Ser262 peptide] and τ phosphorylated by a partially purified kinase, glycogen synthase kinase (GSK) 3β. Ab262 reacted poorly with a peptide having the sequence DRV-QSKIGSLD (amino acids 348-358). Treatment of P-Ser262 peptide or GSK 3β phosphorylated τ with alkaline phosphatase increased Ab262 immunoreactivity, indicating that Ab262 is a reagent useful for studying τ phosphorylation at the Ser262 residue. The Ab262 immunoreactivity was detected in τ from normal brains and Alzheimer paired helical filament (PHF-τ) and in PHFs. Alkaline phosphatase treatment had no effect on the Ab262 immunoreactivity of normal τ and PHF-τ but altered the Tau-1 and PHF-1 immunoreactivities. τ proteins from rat brains at 3 and 8 h postmortem exhibited 5 and 19%, respectively, more Ab262 immunoreactivity than τ from fresh tissues. In comparison, rat τ at 8 h postmortem was 40% more immunoreactive with Tau-1. The results suggest that Ser262 is not a major phosphorylation site in vivo. Moreover, there is little or no difference between PHF-τ and normal τ in the extent of phosphorylation at Ser262.
KW - Alzheimer paired helical filament-τ
KW - Alzheimer's disease
KW - Peptide phosphorylation
KW - Serine phosphorylation
KW - τ protein
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U2 - 10.1046/j.1471-4159.1996.66031131.x
DO - 10.1046/j.1471-4159.1996.66031131.x
M3 - Article
C2 - 8769876
AN - SCOPUS:0030040597
VL - 66
SP - 1131
EP - 1139
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
SN - 0022-3042
IS - 3
ER -