Literature DB >> 3137483

Processing of neurofilament proteins from perikaryal to axonal type.

I Toyoshima1, A Yamamoto, M Satake.   

Abstract

In previous studies, neuronal cell bodies, excised by hand from bovine spinal ganglia, were analyzed and heterogeneous intermediate and high molecular weight neurofilament proteins that differed in electrophoretic mobility from their axonal counterparts were demonstrated. In the present experiment, intermediate and high molecular weight neurofilament proteins of the axonal type were treated with alkaline phosphatase, and neurofilament proteins enriched in perikaryal type proteins were labeled with 32P. Results showed that neurofilament proteins were phosphorylated after their translation, in the perikarya and the proximal portion of the axon, and suggested that phosphorylation was responsible for the differences between axonal and perikaryal neurofilament proteins.

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Year:  1988        PMID: 3137483     DOI: 10.1007/bf00973278

Source DB:  PubMed          Journal:  Neurochem Res        ISSN: 0364-3190            Impact factor:   3.996


  8 in total

1.  Quantitative assay of compounds in isolated, fresh nerve cells and glial cells from control and stimulated animals.

Authors:  H HYDEN
Journal:  Nature       Date:  1959-08-08       Impact factor: 49.962

2.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

3.  The structure, biochemical properties, and immunogenicity of neurofilament peripheral regions are determined by phosphorylation state.

Authors:  M J Carden; W W Schlaepfer; V M Lee
Journal:  J Biol Chem       Date:  1985-08-15       Impact factor: 5.157

4.  Multiple phosphorylation sites in mammalian neurofilament polypeptides.

Authors:  J P Julien; W E Mushynski
Journal:  J Biol Chem       Date:  1982-09-10       Impact factor: 5.157

5.  Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ.

Authors:  L A Sternberger; N H Sternberger
Journal:  Proc Natl Acad Sci U S A       Date:  1983-10       Impact factor: 11.205

6.  The use of avidin-biotin interaction in immunoenzymatic techniques.

Authors:  J L Guesdon; T Ternynck; S Avrameas
Journal:  J Histochem Cytochem       Date:  1979-08       Impact factor: 2.479

7.  A comparison of in vitro- and in vivo-phosphorylated neurofilament polypeptides.

Authors:  J P Julien; W E Mushynski
Journal:  J Neurochem       Date:  1981-12       Impact factor: 5.372

8.  Slow posttranslational modification of a neurofilament protein.

Authors:  G S Bennett; C DiLullo
Journal:  J Cell Biol       Date:  1985-05       Impact factor: 10.539

  8 in total
  3 in total

1.  Heparin sulfate-like immunoreactivity in the spinal cord in motor neuron disease.

Authors:  T Kato; T Katagiri; Y Shikama; K Kurita; I Toyoshima; A Hirano; M Wada; H Sasaki
Journal:  Acta Neuropathol       Date:  1993       Impact factor: 17.088

2.  Calcitonin gene-related peptide immunoreactivity in spinal spheroids in motor neuron disease.

Authors:  T Kato; T Katagiri; A Hirano; T Kawanami; Y Shikama; K Kurita; H Sasaki; S Arai
Journal:  Acta Neuropathol       Date:  1991       Impact factor: 17.088

3.  Immunoreactivity for phosphorylated 200-kDa neurofilament subunit is heterogeneously expressed in human sympathetic and primary sensory neurons.

Authors:  J A Vega; J M Humara; F J Naves; I Esteban; M E Del Valle
Journal:  Anat Embryol (Berl)       Date:  1994-11
  3 in total

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