Localization of S-100 protein in isolated nerve cells by immunoelectron microscopy

Hansson, Hans‐Arne; Hydén, Holger; Rönnbäck, Lars

doi:10.1016/0006-8993(75)90357-1

Cited by 27 publications

(4 citation statements)

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“…However, spherules with anti-23-100 antiserum were mostly unevenly distributed over the cell surfaces, meaning that parts of the membranes did not bind the spherules. This is in accordance with the results of the studies on S-100 on neuronal cell membranes, using immunofluorescence (Hyd6n and Ronnback, 1975) and immuno-electron microscopy (Hansson et al, 1975).…”

Section: Bloodsupporting

confidence: 91%

The brain‐specific S‐100 protein on neuronal cell membranes

Hydén

Rönnbäck

1978

J. Neurobiol.

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The S-100 protein has been localized to the neuronal plasma membranes of isolated Deiters' neurons by fluorescence microscopy using fluorescein-conjugated antiserum to the protein and by immunoelectron microscopy using peroxidase-conjugated anti-S-100 antiserum. In the present study this is shown also by incubating neurons with Sepharose 4B or methylacrylate spherules to which were coupled anti-S-100 antibodies. The specificity of the antiserum is discussed in the text. The technique described can be used to study the topography of antigenic characteristics of nerve cells by using antisera insolubilized on spherules of suitable size.

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Section: Bloodsupporting

confidence: 91%

The brain‐specific S‐100 protein on neuronal cell membranes

Hydén

Rönnbäck

1978

J. Neurobiol.

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“…The procedure which was finally adopted gave reproducible reaction patterns and good morphology. Since the staining pattern was similar in tissue sections, in nerve and neuroglial fractions obtained after centrifugation, in fractionated cells, and in free-hand dissected neurons (21), it is unlikely that redistribution of soluble S-100 protein occurred. In addition, although part of the soluble S-100 protein leaks from neuronal and glial cells in suspension, the complement fixation studies showed that a considerable portion was retained in the nerve and dial cell fractions.…”

Section: Discussionmentioning

confidence: 94%

Cellular and subcellular distribution of the S‐100 protein in rabbit and rat central nervous system

Haglid

Hamberger

Hansson

et al. 1976

J of Neuroscience Research

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The cellular and subcellular distribution of the S-100 protein in rabbit and rat central nervous system was studied both quantitatively and qualitatively. Microcomplement fixation estimations on bulk-prepared neuronal and glial cells showed at least five to six times higher amounts of water-soluble S-100 in glial cell-enriched fractions as compared to fractions enriched in neuronal perikarya. Nerve cell fractions contained a higher percent of tissue-bound S-100 protein. High levels of S-100 protein were found in mitochondria and soluble protein fractions. Immunoelectron microscope investigations demonstrated S-100 protein in neuronal structures, such as the postsynaptic membrane and part of the plasma membrane. Among glial cells the astrocytic filaments contained high levels of S-100 protein. S-100 was also found in most subcellular membranes of astrocytes and oligodendrocytes.

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“…More recently it has been demonstrated that S100a0, a dimer made up of 2 alpha subunits and which accounts for < 5% of total $100, is localized principally in neurons, while alpha/beta and beta/beta dimers (S100a and S100b, respectively) are located in glia (Isobe et al, 1984). This differential localization may account for some early reports of $100 immunoreactivity in neurons (Haglid et al, 1974;Hansson et al, 1975).…”

Section: Introductionmentioning

confidence: 86%

S100 is preferentially distributed in myelin-forming Schwann cells

1990

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In order to elucidate the role of S100 protein in vivo we used postembedding electron microscopical immunocytochemistry with commercially available antibodies to S100, and secondary antibodies conjugated to colloidal gold to determine the distribution of S100 protein in the sciatic nerve and the cervical sympathetic trunk of the rat. We found that S100 immunoreactivity in Schwann cells was differentially distributed. The amount of S100 immunoreactivity in myelinated fibres appeared to correlate directly with the thickness of the myelin sheath formed by the Schwann cell. Unmyelinated fibres were identical to the small myelinated fibres in S100 immunoreactivity. Within the Schwann cells, the immunoreactivity was seen in the nucleus and in the perikaryal cytoplasm, as well as in the Schmidt-Lanterman clefts and in the paranodal loops at the node of Ranvier, but not in the myelin itself. Using these antibodies we did not see reproducible or convincing intra-axonal immunoreactivity in normal nerve. These results suggest that in Schwann cells S100 expression may be related to axon diameter and degree of myelination. Future studies of S100 expression in development or in response to injury may clarify the role of S100 in Schwann cell biology.

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Localization of S-100 protein in isolated nerve cells by immunoelectron microscopy

Cited by 27 publications

References 10 publications

The brain‐specific S‐100 protein on neuronal cell membranes

The brain‐specific S‐100 protein on neuronal cell membranes

Cellular and subcellular distribution of the S‐100 protein in rabbit and rat central nervous system

S100 is preferentially distributed in myelin-forming Schwann cells

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