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A I Matus

Publications and source records attributed to A I Matus.

5 recordsLinked to original sources

Immunohistochemical localization of neurofilament antigen in rat cerebellum.

The distribution of neurofilaments in the rat cerebellar cortex was studied by immunoperoxidase histochemistry using an antiserum raised against neurofilaments isolated from brain (anti-NF). In light microscope preparations, this antiserum selectively stained known neurofilament-containing structures. Staining was most intense in myelinated axons of the white matter and in the terminal branches of basket cell axons. No staining was apparent in either neuronal or glial cell bodies or in glial cell processes. These findings were confirmed in electron microscopic preparations of the same material. Neurofilaments stained by the antiserum were abundant in basket cell axons and also occurred in small bundles in mossy fibre terminals. Adjacent microtubules were not stained by the antiserum. There was no evidence of stained cytoplasmic filaments in glial cell processes. Thus it appears that neurofilaments contain unique antigens which do not occur in either microtubules or in glial cytoplasmic filaments. The antiserum did not induce staining of synaptic junctional structures, a result which contradicts previous suggestions that neurofilaments are structural components of synaptic densities.

Animals

Morphology and molecular composition of isolated postsynaptic junctional structures.

The solubilization of isolated brain synaptosomal plasma membranes by various detergents was studied and in each case found to depend upon detergent concentration. By using conditions sufficient to extract maximally protein and phospholipid from the membranes, postsynaptic junctional particles were isolated with each of four detergents and their ultrastructural appearances and protein contents compared. Two basic structural forms were identified. One, isolated with Triton X-100, consists of a planar array of dense-staining particles ca. 20 nm in diameter. It resembles the postsynaptic density seen in undigested synaptosomal plasma membranes. The other, isolated with sodium deoxycholate, contains less protein. It has the same overall shape and dimensions as the postsynaptic density, but consists of a branching network of short 5 nm fibres (the postsynaptic junctional lattice) making up an array of contiguous polygons, each ca. 20 nm across. The interior of these polygonal elements seems to be hydrophobic since it cannot be penetrated by metallic salts used for negative staining. It is suggested that the dense-staining 20 nm subunits observed at the postsynaptic junctional site may be composed of hydrophobic proteins inserted into the hollow cores of the lattice polygons. Electrophoretic analysis of the proteins present in the various postsynaptic junctional preparations identified two major common components with molecular masses of 275000 and 47500. The latter is tentatively identified as actin. Components comigrating respectively with alpha- and beta-tubulin are present, and the relation of the lattice structure to subjacent microtubules is discussed.

Animals