High-resolution imaging of protein phosphorylation in squid axons and synapse by electron energy loss spectroscopy.
Author(s) -
Roland Martinꝉ,
R. Door,
D. Breitig
Publication year - 1993
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/41.8.8331279
Subject(s) - neurofilament , axon , cytoskeleton , phosphorylation , synapse , biophysics , squid giant axon , squid , chemistry , biology , microbiology and biotechnology , neuroscience , cell , biochemistry , immunohistochemistry , ecology , immunology
We demonstrate that clusters of phosphorus atoms can be detected in energy loss spectroscopic images (ESI) of cytoskeletal proteins of squid axons. In series of images taken at four energy windows below and three windows above the phosphorus P-L2,3 ionization edge, signal-to-background intensity differences were analyzed by videodensitometry. A distinct increase of relative intensities was recorded above the phosphorus edge in neurofilaments of the peripheral giant axon and in those of the presynaptic terminal. A high level of neurofilament phosphorylation in the peripheral axon supports previous biochemical and immunochemical results, but our finding of phosphorylated neurofilaments in the presynaptic axon conflicts with these studies. Our method may be advantageous for analysis with high elemental and spatial resolution of the phosphorylation state of cytoskeletal protein molecules in situ.
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