Literature DB >> 2324739

Phosphate-dependent monoclonal antibodies to neurofilaments and Alzheimer neurofibrillary tangles recognize a synthetic phosphopeptide.

M P Coleman1, B H Anderton.   

Abstract

Five phosphate-dependent monoclonal antibodies to the neurofilament heavy polypeptide bound strongly to a phosphorylated synthetic peptide, which contains a single Lys-Ser-Pro sequence that occurs in human neurofilaments. Three of the antibodies label Alzheimer's disease neurofibrillary tangles and two do not, suggesting that in tangles an epitope similar to the peptide is available to some but not all of the antibodies. In addition, some antibodies were found to be more affected than others by enzymatic dephosphorylation of the antigen, but because all the antibodies bound the same synthetic phosphopeptide they do not bind to mutually exclusive phosphorylation sites. Instead the more phosphate-dependent antibodies might bind the phosphate group more directly, as suggested by their inhibition by inorganic phosphate and free phosphoserine.

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Year:  1990        PMID: 2324739     DOI: 10.1111/j.1471-4159.1990.tb01203.x

Source DB:  PubMed          Journal:  J Neurochem        ISSN: 0022-3042            Impact factor:   5.372


  9 in total

1.  The neurofilament antibody RT97 recognises a developmentally regulated phosphorylation epitope on microtubule-associated protein 1B.

Authors:  M Johnstone; R G Goold; I Fischer; P R Gordon-Weeks
Journal:  J Anat       Date:  1997-08       Impact factor: 2.610

2.  Functional domains on chemically modified tau protein.

Authors:  G A Farías; C Vial; R B Maccioni
Journal:  Cell Mol Neurobiol       Date:  1993-04       Impact factor: 5.046

3.  Immunological characterization of epitopes on tau of Alzheimer's type and chemically modified tau.

Authors:  G Farías; C González-Billault; R B Maccioni
Journal:  Mol Cell Biochem       Date:  1997-03       Impact factor: 3.396

4.  Phosphorylation-dependent epitopes of neurofilament antibodies on tau protein and relationship with Alzheimer tau.

Authors:  B Lichtenberg-Kraag; E M Mandelkow; J Biernat; B Steiner; C Schröter; N Gustke; H E Meyer; E Mandelkow
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-15       Impact factor: 11.205

5.  Regulation of neurofilament interactions in vitro by natural and synthetic polypeptides sharing Lys-Ser-Pro sequences with the heavy neurofilament subunit NF-H: neurofilament crossbridging by antiparallel sidearm overlapping.

Authors:  J P Gou; T Gotow; P A Janmey; J F Leterrier
Journal:  Med Biol Eng Comput       Date:  1998-05       Impact factor: 2.602

6.  Neurofilament tail phosphorylation: identity of the RT-97 phosphoepitope and regulation in neurons by cross-talk among proline-directed kinases.

Authors:  Ju-Hyun Lee; Tej K Pareek; Howard Jaffee; Barry Boland; K Yaragudri Vinod; Niranjana Amin; Ashok B Kulkarni; Harish C Pant; Ralph A Nixon
Journal:  J Neurochem       Date:  2008-07-04       Impact factor: 5.372

7.  The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and beta-amyloid in primary rat cortical neuronal cultures.

Authors:  D R Davis; J P Brion; A M Couck; J M Gallo; D P Hanger; K Ladhani; C Lewis; C C Miller; T Rupniak; C Smith
Journal:  Biochem J       Date:  1995-08-01       Impact factor: 3.857

8.  Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber.

Authors:  R A Nixon; P A Paskevich; R K Sihag; C Y Thayer
Journal:  J Cell Biol       Date:  1994-08       Impact factor: 10.539

9.  Local control of neurofilament accumulation during radial growth of myelinating axons in vivo. Selective role of site-specific phosphorylation.

Authors:  I Sánchez; L Hassinger; R K Sihag; D W Cleveland; P Mohan; R A Nixon
Journal:  J Cell Biol       Date:  2000-11-27       Impact factor: 10.539

  9 in total

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