PMID- 10090668
OWN - NLM
STAT- MEDLINE
DCOM- 19990630
LR  - 20190812
IS  - 0001-6322 (Print)
IS  - 0001-6322 (Linking)
VI  - 97
IP  - 3
DP  - 1999 Mar
TI  - Phosphorylated serine422 on tau proteins is a pathological epitope found in
      several diseases with neurofibrillary degeneration.
PG  - 221-30
AB  - Neuronal inclusions with bundles of abnormal filaments made of tau polymers are
      found in numerous diseases with neurofibrillary degeneration. Tau proteins are
      the basic components of paired helical filaments (PHF) in Alzheimer's disease
      (AD), and are abnormally phosphorylated. A disease-specific phosphorylation site 
      at serine422 was demonstrated on PHF, but not on tau proteins from biopsy-derived
      brain samples. In the present study, we report the characterization of a
      polyclonal antibody (988) against the serine422 phosphorylation site. By using
      biochemical and immunohistochemical methods, we confirmed that it is not found on
      tau proteins from biopsy- or autopsy-derived control samples, and we investigated
      the presence of this epitope on tau proteins in several neurodegenerative
      disorders, including AD, Down syndrome (DS), Guamanian amyotrophic lateral
      sclerosis/Parkinsonism-dementia complex (ALS/PDC), corticobasal degeneration
      (CBD), progressive supranuclear palsy (PSP), postencephalitic parkinsonism (PEP) 
      and Pick's disease (PiD). By Western blotting, antibody 988 labeled the
      characteristic tau triplet (tau 55, 64, 69) in AD, DS, Guamanian ALS/PDC and PEP.
      PSP and CBD exhibited their typical tau doublet (tau 64, 69), whereas the doublet
      tau 55 and 64 was detected in PiD. In all of these neurodegenerative disorders,
      antibody 988 clearly labeled NFT and dystrophic neurites, as well as Pick bodies 
      in PiD cases, whereas no staining was observed in control cases. These data
      indicate that phosphorylation of serine422 on tau proteins is a common feature
      among neurodegenerative disorders and is therefore not specific of AD. Moreover, 
      phosphorylation of this epitope permits the distinction between normal tau
      proteins and pathological tau proteins.
FAU - Bussiere, T
AU  - Bussiere T
AD  - INSERM U 422, Place de Verdun, F-59045 Lille, France.
FAU - Hof, P R
AU  - Hof PR
FAU - Mailliot, C
AU  - Mailliot C
FAU - Brown, C D
AU  - Brown CD
FAU - Caillet-Boudin, M L
AU  - Caillet-Boudin ML
FAU - Perl, D P
AU  - Perl DP
FAU - Buee, L
AU  - Buee L
FAU - Delacourte, A
AU  - Delacourte A
LA  - eng
GR  - AG05138/AG/NIA NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Germany
TA  - Acta Neuropathol
JT  - Acta neuropathologica
JID - 0412041
RN  - 0 (tau Proteins)
RN  - 452VLY9402 (Serine)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibody Specificity
MH  - Brain/metabolism
MH  - Humans
MH  - Immunoblotting
MH  - Immunohistochemistry
MH  - Middle Aged
MH  - Neurodegenerative Diseases/*metabolism
MH  - Neurofibrillary Tangles/*metabolism
MH  - Phosphorylation
MH  - Serine/*metabolism
MH  - tau Proteins/immunology/*metabolism
EDAT- 1999/03/25 00:00
MHDA- 1999/03/25 00:01
CRDT- 1999/03/25 00:00
PHST- 1999/03/25 00:00 [pubmed]
PHST- 1999/03/25 00:01 [medline]
PHST- 1999/03/25 00:00 [entrez]
AID - 10.1007/s004010050978 [doi]
PST - ppublish
SO  - Acta Neuropathol. 1999 Mar;97(3):221-30. doi: 10.1007/s004010050978.