Characterisation of an Antibody Relevant to the Neuropathology of Alzheimer Disease

Jakes, Ross; Harrington, Charles R.; Mg, Spillantini; Goedert, Michel; Klug, A

doi:10.1097/00002093-199505000-00009

Cited by 4 publications

(3 citation statements)

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“…Previously published work has documented the cross‐reactivity of certain beta‐amyloid (Aβ) antibodies with tau (Caputo et al . 1993), although this finding is somewhat controversial (Jakes et al . 1995).…”

Section: Resultsmentioning

confidence: 99%

Tau‐66: evidence for a novel tau conformation in Alzheimer's disease

Ghoshal¹,

Garcı́a-Sierra²,

Fu³

et al. 2001

Journal of Neurochemistry

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We have characterized a novel monoclonal antibody, Tau-66, raised against recombinant human tau. Immunohistochemistry using Tau-66 reveals a somatic-neuronal stain in the superior temporal gyrus (STG) that is more intense in Alzheimer's disease (AD) brain than in normal brain. In hippocampus, Tau-66 yields a pattern similar to STG, except that neuro®brillary lesions are preferentially stained if present. In mild AD cases, Tau-66 stains plaques lacking obvious dystrophic neurites (termed herein`diffuse reticulated plaques') in STG and the hippocampus. Enzyme-linked immunosorbent assay (ELISA) analysis reveals that Tau-66 is speci®c for tau, as there is no cross-reactivity with MAP2, tubulin, Ab 1240 , or Ab 1242 , although Tau-66 fails to react with tau or any other polypeptide on western blots. The epitope of Tau-66, as assessed by ELISA testing of tau deletion mutants, appears discontinuous, requiring residues 155±244 and 305± 314. Tau-66 reactivity exhibits buffer and temperature sensitivity in an ELISA format and is readily abolished by SDS treatment. Taken together these lines of evidence indicate that the Tau-66 epitope is conformation-dependent, perhaps involving a close interaction of the proline-rich and the third microtubule-binding regions. This is the ®rst indication that tau can undergo this novel folding event and that this conformation of tau is involved in AD pathology.

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Section: Resultsmentioning

confidence: 99%

Tau‐66: evidence for a novel tau conformation in Alzheimer's disease

Ghoshal¹,

Garcı́a-Sierra²,

Fu³

et al. 2001

Journal of Neurochemistry

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“…32 Other applications include intracellular imaging 33,34 and diagnostics. 35,36 There is therefore the need for experimental strategies to isolate antibodies that are suitable for intracellular expression. Indeed, not all antibodies tolerate the reducing conditions of the cell cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

The intracellular antibody capture technology (IACT): towards a consensus sequence for intracellular antibodies

Visintin

Settanni

Maritan

et al. 2002

Journal of Molecular Biology

131

115

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“…However, in light of the report by Caputo et al (1992a) on the cross reactivity of BR 88, it is possible that the antibodies used by Dooley et al (1992) and Refolo et al (1991) are cross reacting with tau or a tau-like protein with homology to amyloid. The recent report of Jakes et al (1994) takes issue with this interpretation.…”

Section: Discussionmentioning

confidence: 99%

Tau‐like immunoreactivity in Alzheimer and control skin fibroblasts

Matsuyama

Bondareff

1994

J of Neuroscience Research

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The presence of the microtubule-associated protein tau in skin fibroblasts derived from Alzheimer patients and normal controls was investigated using a panel of well-characterized anti-tau antibodies against epitopes spanning the tau protein from the amino to the carboxyl end. The antibodies immunolabeled a fine, fibrillar cytoplasmic network in all skin fibroblasts. Disruption of the microtubule network with colchicine did not affect the immunolabeling of the fibrillar network nor did treatment with cytochalasin B known to disrupt the microfilament network. Immunoelectron microscopy with the anti-tau antibodies revealed colocalization of the label with the 10 nm intermediate filaments. Furthermore, immunoblots found no reactivity against purified vimentin, suggesting that the antibodies recognize an intermediate filament-associated protein. The findings indicate the presence of tau or a protein with considerable homology to tau in fibroblasts associated with intermediate filaments and not microtubules.

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Characterisation of an Antibody Relevant to the Neuropathology of Alzheimer Disease

Cited by 4 publications

References 0 publications

Tau‐66: evidence for a novel tau conformation in Alzheimer's disease

Tau‐66: evidence for a novel tau conformation in Alzheimer's disease

The intracellular antibody capture technology (IACT): towards a consensus sequence for intracellular antibodies

Tau‐like immunoreactivity in Alzheimer and control skin fibroblasts

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