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Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404
Abstract
The microtubule‐associated protein τ is hyperphosphorylated in the paired helical filaments (PHFs) of Alzheimer's disease. Immunological and direct chemical studies have identified Ser 396 and Ser 404 as two of the phosphorylated sites. Previously, we have demonstrated, using synthetic τ peptides containing phosphorylated Ser 396 , that this site is recognized by the monoclonal antibody PHF‐1. The present sudy extends this observation by showing that PHF‐1 recognizes τ peptides containing either individually phosphorylated Ser 396 or Ser 404 , but that there is a >10‐fold increase in the sensitivity of detection of τ peptides by PHF‐1 when both serines are phosphorylated. The recognition of singly or doubly phosphorylated Ser 396 and Ser 404 in τ by PHF‐1 can also be demonstrated in Chinese hamster ovary cells transfected with full‐length wild‐type τ constructs or mutant constructs with Ala substituted for Ser 396 or Ser 404 . We conclude that the PHF‐1 epitope contains both phosphorylated Ser 396 and Ser 404 . © 1994 Wiley‐Liss, Inc.
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“…la Recherche Médicale U422, Lille, France) and PHF1 (a kind gift from Dr. P. Davies) recognize human and murine tau phosphorylated at S396 and S404 (Otvos et al., 1994; Buée-Scherrer et al., 1996); PG5 (a kind gift from Dr. P. Davies) recognizes human and murine tau phosphorylated at S409…”
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“…antibodies (specificity given in parentheses) were a generous gift from Dr. Peter Davies (Albert Einstein University, New York, NY): TG-3, phospho-Ser231 and conformation specific (Jicha et al., 1997); MC-6, phospho-Ser235 (Jicha et al., 1997); and PHF-1, phospho-Ser396/404 (Otvos et al., 1994).”
BackgroundSpittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M. H., Sciot, R., Lommel, A. V., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 390
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“The following monoclonal antibodies were used to stain free-floating brain sections: CP13 [1:5000; Ps202 (Duff et al., 2000; Lewis et al., 2000)] and PHF1 [1:5000; Ps396/404 (Greenberg et al., 1992; Otvos et al., 1994)].”
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Self-citationPERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia
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“A number of different antibodies have been described that recognise different tau phosphorylation sites and pathology, including AT8 [10, 22], which detects phosphorylation at Ser/Thr and is a marker for pretangles and tangles, and PHF1 [28], which detects late-stage tangles including tau phosphorylated at Ser.”
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Self-citationAcetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies
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“…(1) mouse monoclonal tau antibodies that stain pathological tau PHF1 [1:1000, recognizes phosphorylated serines 396 and 404 of tau protein (Otvos et al., 1994), and shows only minimal axonal staining in normal human brain, generously provided by Peter Davies (Albert Einstein College of…”
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“The same samples were analyzed by immunoblotting using anti-tau antibodies that recognize a phosphorylation-independent anti-tau polyclonal antibody raised to recombinant tau (17025, 1:2,000; produced in the Penn Center for Neurodegenerative Disease Research (CNDR); [52]) and PHF tau phosphorylated at Ser 396/404 (mon…”
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“AD2 and PHF1 among others, are located in this region [25–29].”
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“The labeling by 4G10 was weaker than PHF-1, and it was found to be necessary to enrich for PHF-tau to observe clear labeling by 4G10, suggesting that the phosphotyrosine content is lower than the level of phosphorylation at the PHF-1 epitope (serines 396 and 404) (Otvos et al., 1994).”
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Self-citationSpecificity and Regulation of Casein Kinase-Mediated Phosphorylation of ??-Synuclein
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cAMP-Dependent Protein Kinase Phosphorylations on Tau in Alzheimer’s Disease
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Tau Phosphorylation at Serine 396 Residue Is Required for Hippocampal LTD
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“…(Zhu et al., 2002; Peineau et al., 2007; Kimura et al., 2014), using the antibodies PHF-1 (an antibody that recognizes phosphorylation at residues S396 and S404 of tau; Otvos et al., 1994) and AT8 (an antibody that recognizes phosphorylation at S202 and T205 residues of tau; Goedert et al., 1995).”
MethodGlycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells
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Waxman, E. A., & Giasson, B. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0297-11.2011 · Cited by 201
“Intracellular localization of these pathological aggregates can be identified in these disorders, primarily composed of tau-forming neurofibrilliary tangles (NFTs) in AD or of -synuclein ( -syn)-forming Lewy pathology in PD.”
BackgroundInfluentialLong-Term In Vivo Imaging of Fibrillar Tau in the Retina of P301S Transgenic Mice
Schön, C., Hoffmann, N. A., Ochs, S. M., Burgold, S., Filser, S., Steinbach, S., Seeliger, M. W., Arzberger, T., Goedert, M., Kretzschmar, H. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0053547 · Cited by 193
“After blocking 30 min with Casein-I, probes were stained with antibodies against hyperphosphorylated tau (AT8, 1:200; AT100, 1:200; AT180, 1:50, Thermo Scientific, product #MN1040; AT270, 1:200, Thermo Scientific, product # MN1050 or PHF-1, 1:1000 [25]) and Ab (4G8, 1:1000; Table 1.”
MethodSelf-citationQuantification of Axonal Damage in Traumatic Brain Injury
Zemlan, F. P., Rosenberg, W. S., Luebbe, P., Campbell, T. A., Dean, G. E., Weiner, N. E., Cohen, J. A., Rudick, R. A., & Woo, D. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720741.x · Cited by 187
“This fragment could also be labeled with the Mab PHF-1, which recognizes phosphorylated Ser of tau (Otvos et al., 1994; Zemlan and Dean, 1996).”
BackgroundPick's disease: hyperphosphorylated tau protein segregates to the somatoaxonal compartment
Probst, A., Tolnay, M., Langui, D., Goedert, M., & Spillantini, M. G. (1996) · Acta Neuropathologica · doi:10.1007/s004010050565 · Cited by 192
Self-citationBennecib, M., Gong, C.-X., Grundke-Iqbal, I., & Iqbal, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02203-1 · Cited by 184
Hamilton, R. H., Patel, S. V., Lee, E. B., Jackson, E. M., Lopinto, J., Arnold, S. E., Clark, C. M., Basil, A. K., Shaw, L. M. J., Xie, S. X., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22015 · Cited by 185
Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo
Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0327 · Cited by 187
“Using disease-associated phospho-specific antibodies to analyze the phosphorylation status of tau AP5 , we found that reactivity with AT270, PHF1, and Tau1 was unchanged compared with tau WT (Figure 6C).”
InfluentialMutant valosin‐containing protein causes a novel type of frontotemporal dementia
Schröder, R., Watts, G. D. J., Mehta, S. G., Evert, B. O., Broich, P., Fließbach, K., Pauls, K., Hans, V. H., Kimonis, V., & Thal, D. R. (2005) · Annals of Neurology · doi:10.1002/ana.20407 · Cited by 177
The role of tau kinases in Alzheimer's disease.
Dolan, P. J., & Johnson, G. V. W. (2010) · PubMed · Cited by 178
Sayas, C. L., Moreno-Flores, M. T., Ávila, J., & Wandosell, F. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37046 · Cited by 173
Amyloid-β signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease
Seward, M. E., Swanson, E., Norambuena, A., Reimann, A., Cochran, J. N., Li, R., Roberson, E. D., & Bloom, G. S. (2013) · Journal of Cell Science · doi:10.1242/jcs.1125880 · Cited by 178
“…CCR, have not been regarded as canonical AD phospho- tau sites, such as those recognized by the monoclonal antibodies, PHF-1 (pS396/pS404) (Otvos et al., 1994), AT8 (S199/pS202/ pS205) (Porzig et al., 2007), AT100 (pT212/pS214) (Zheng- Fischhöfer et al., 1998) or AT180 (pT231/pS235)…”
BackgroundSun, L., Liu, S. Y., Zhou, X. W., Wang, X. C., Liu, R., Wang, Q., & Wang, J. Z. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00697-8 · Cited by 168
Hu, Y., Xu, P., Pigino, G. F., Brady, S. T., Larson, J., & Lazarov, O. (2010) · The FASEB Journal · doi:10.1096/fj.09-136945 · Cited by 176
Eckermann, K., Mocanu, M.-M., Khlistunova, I., Biernat, J., Nissen, A., Hofmann, A., Schönig, K., Bujard, H., Haemisch, A., Mandelkow, E., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705282200 · Cited by 168
Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease
Liu, F., Zaidi, T., Iqbal, K., Grundke-Iqbal, I., Merkle, R. K., & Gong, C.-X. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02228-7 · Cited by 167
Lee, G. S., & Leugers, C. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00004-7 · Cited by 173
Repetitive mild traumatic brain injury augments tau pathology and glial activation in aged hTau mice
Ojo, J.-O., Mouzon, B., Greenberg, M. B., Bachmeier, C., Mullan, M., & Crawford, F. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182814cdf · Cited by 166
Lithium and valproic acid: parallels and contrasts in diverse signaling contexts
Gurvich, N. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00299-1 · Cited by 166
“In addition to MAP-1B, GSK-3b also phosphorylates the MAP tau (Lee, 1995; Lovestone et al., 1994; Mandelkow & Mandelkow, 1993; Otvos et al., 1994).”
BackgroundAlonso, A. D. C., Zaidi, T., Novák, M., Barra, H. S., Grundke, I., & Iqbal, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105365200 · Cited by 160
Serrano-Pozo, A., William, C. M., Ferrer, I., Uro-Coste, E., Delisle, M.-B., Maurage, C.-A., Hock, C., Nitsch, R. M., Masliah, E., Growdon, J. H., et al. (2010) · Brain · doi:10.1093/brain/awq056 · Cited by 159
Casein Kinase 1 Delta Phosphorylates Tau and Disrupts Its Binding to Microtubules
Li, G., Yin, H., & Kuret, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314116200 · Cited by 162
Chiasseu, M., Alarcón-Martínez, L., Belforte, N., Quintero, H., Dotigny, F., Destroismaisons, L., Velde, C. V., Panayi, F., Louis, C., & Polo, A. D. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0199-3 · Cited by 158
TauGene Mutation K257T Causes a Tauopathy Similar to Pick's Disease
Rizzini, C., Goedert, M., Hodges, J. R., Smith, M. J., Jakes, R., Hills, R., Xuereb, J. H., Crowther, R. A., & Spillantini, M. G. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.11.990 · Cited by 161
“AT100 recognizes tau phosphorylated at T212 and S214 (38), AT180 recognizes tau phosphorylated at T231 (39), 12E8 recognizes tau phosphorylated at S262 and/ or S356 (40), PHF1 recognizes tau phosphorylated at S396 and S404 (41) and AP422 recognizes tau phosphorylated at S422 (42).”
BackgroundSelf-citationTissue-nonspecific Alkaline Phosphatase Promotes the Neurotoxicity Effect of Extracellular Tau
Díaz-Hernández, M., Gómez‐Ramos, A., Rubio, A., Gómez‐Villafuertes, R., Naranjo, J. R., Miras‐Portugal, M. T., & Ávila, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145003 · Cited by 163
Activation of Caspase-6 in Aging and Mild Cognitive Impairment
Albrecht, S., Bourdeau, M., Bennett, D. A., Mufson, E. J., Bhattacharjee, M. B., & LeBlanc, A. C. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060974 · Cited by 155
Reduction of Nuak1 Decreases Tau and Reverses Phenotypes in a Tauopathy Mouse Model
Lasagna‐Reeves, C. A., de Haro, M., Hao, S., Park, J., Rousseaux, M. W. C., Al‐Ramahi, I., Jafar‐Nejad, P., Vilanova-Velez, L., See, L., Maio, A. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.022 · Cited by 154
Buée‐Scherrer, V., Condamines, O., Mourton-Gilles, C., Jakes, R., Goedert, M., Pau, B., & Delacourte, A. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(96)00003-4 · Cited by 161
“They allowed for the identif i c a t i o n o f a b n o r m a l l y p h o s p h o r y l a t e d sites [20] [21] [23] [28] [35] [42].”
BackgroundSelf-citationTauopathy with paired helical filaments in an aged chimpanzee
Rosen, R. F., Farberg, A. S., Gearing, M., Dooyema, J., M. Long, P., Anderson, D. C., Davis‐Turak, J., Coppola, G., Geschwind, D. H., Paré, J., et al. (2008) · Journal of Comparative Neurology · doi:10.1002/cne.21744 · Cited by 153
“Specificity was confirmed with Western blots of transfected cell lysates (Otvos et al., 1994).”
BackgroundMethodInfluentialLi, L., Sengupta, A., Haque, N., Grundke, I., & Iqbal, K. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.04.047 · Cited by 154
PKA modulates GSK‐3β‐ and cdk5‐catalyzed phosphorylation of tau in site‐ and kinase‐specific manners
Liu, F., Liang, Z., Shi, J., Yin, D., El-Akkad, E., Grundke, I., Iqbal, K., & Gong, C. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.033 · Cited by 149
“phosphorylated Ser396 than to phosphorylated Ser404 of tau [26].”
Background
Metadata
- Authors
- Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., & Lee, V. M.
- Affiliations
- The Wistar Institute (US)
- University of Pennsylvania (US)
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Otvos, L.
- ORCID
- Venue
- Journal of Neuroscience Research
- Publisher
- Wiley
- Published
- 1994-12-15
- Volume
- 39
- Issue
- 6
- Pages
- 669-673
- ISSN
- 0360-4012 (ISSN-L)
- 1097-4547
- OpenAlex
- W1984482388
- Semantic Scholar
- 4518f282e57a4d29fb281b9a658ed49720534f5d
- Cited by
- 488
- References
- 21
- Citations by year
- 2026: 14 · 2025: 27 · 2024: 14 · 2023: 11 · 2022: 13 · 2021: 11 · 2020: 13 · 2019: 13 · 2018: 6 · 2017: 13 · 2016: 16 · 2015: 12 · 2014: 7 · 2013: 24 · 2012: 23
- FWCI
- 7.47
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neuroscience Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag010670-02, 5p01ag009215-20)
- National Institute on Aging (AG09215, AG 10670)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tau hyperphosphorylation, paired helical filaments, Alzheimer's disease, epitope mapping, CHO cells
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Antibodies, Monoclonal, Epitopes, Enzyme-Linked Immunosorbent Assay, Cricetinae, Humans, Molecular Sequence Data, Peptides, Phosphorylation, Serine, Blotting, Western, CHO Cells, tau Proteins, DNA, Complementary
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