Immunocytochemical localization of S-100 protein and calmodulin in C6 glioma cells.

Sano, Mamoru; Kato, Kanefusa; Seto‐Ohshima, Akiko; Mizutani, Akira

doi:10.1267/ahc.17.251

Cited by 5 publications

(4 citation statements)

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“…In our studies, Sloop was localized to a small perinuclear region of the cytoplasm in interphase C6 cells and portions of the spindle apparatus in mitotic C6 cells. Our results on S 1 OOp immunolocalization are different from a previous report on S 100 localization in C6 cells (Sano et al, 1984) that found SlOO to be located primarily in the nucleus of interphase cells and the chromosomes of mitotic cells. These differences in SlOO staining patterns may be the result of different immunolocalization procedures (immunoperoxidase versus immunofluorescence), fixation times (90 versus 20 min), the specificity of the different S 100 antibodies, and/or the particular clone of C6 cells used in the studies.…”

Section: Discussioncontrasting

confidence: 99%

Levels and Distribution of the Calcium‐Modulated Proteins S100 and Calmodulin in Rat C6 Glioma Cells

Zimmer

Eldik

1988

Journal of Neurochemistry

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To understand better the mechanisms involved in the transduction of a calcium signal into an intracellular response via multiple calcium-modulated proteins, we have examined the calcium-modulated proteins, S100 and calmodulin, and their intracellular targets in rat C6 glioma cells. Subconfluent, confluent, and postconfluent C6 cells contain predominantly, if not exclusively, the S100 beta polypeptide. The level of S100 beta in C6 cells increases approximately 20-fold from subconfluency to postconfluency whereas the level of calmodulin increases only about two-fold. The subcellular distribution of S100 beta and calmodulin in mitotic cells is similar. However, the subcellular distribution of these proteins in interphase cells is different and appears to change with cell density. Gel overlay analysis demonstrated that the S100- and calmodulin-binding protein profiles are significantly different and that some of the binding proteins appear to change in intensity with cell density. These data demonstrate that S100 beta is the predominant S100 polypeptide in C6 cells and suggest that changes in S100 beta and S100 beta-binding proteins may be involved in regulating S100-mediated intracellular processes in C6 cells. Our studies also suggest that the levels of S100 and calmodulin may be differentially regulated in C6 cells.

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Section: Discussioncontrasting

confidence: 99%

Levels and Distribution of the Calcium‐Modulated Proteins S100 and Calmodulin in Rat C6 Glioma Cells

Zimmer

Eldik

1988

Journal of Neurochemistry

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“…The reason is not clear, because the physiological function of the protein remains to be clarified. Sano et al (1984) reported that S 100 was present as an intense granular reaction product in the nuclei of C6 cells, and concentrated on the chromosomes in all phases of the mitotic processes. Seliefreund et al (1991) indicated that beta-S100 is a neurotrophic protein contributing to glial cell proliferation in both C6 cells and primary astrocytes.…”

Section: Comparison Of Response Pattern Ofbeta-slo0 In C6 Cells With mentioning

confidence: 99%

Neuron and glial cell marker proteins as indicators of heavy metal-induced neurotoxicity in neuroblastoma and glioma cell lines

et al. 1993

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The sensitive and specific biochemical indicators for assessing chemical-induced neurotoxic insults in cell culture models have not been sufficiently explored. This study was designed to assess the usefulness of glia-specific beta-S100 protein and neuron-specific enolase (NSE) as indices of in vitro neurotoxicity of heavy metals. Glioma C6 and neuroblastoma N18TG-2 cells were grown in Dulbecco's modified Eagle's medium containing various concentrations of mercuric chloride (HgCl2) or cadmium chloride (CdCl2) for 5 days. Toxic response patterns of the neurospecific endpoints (beta-S100 and NSE), which were monitored with enzyme immunoassays, were compared with those of the non-neurospecific endpoints such as cell viability, total cellular protein, lactate dehydrogenase (LDH) activity, and cumulative glucose consumption in the two cell lines. Both HgCl2 and CdCl2 produced dose-dependent inhibition of neurospecific endpoints and non-specific endpoints. However, by ranking the EC50 values (effective concentration producing half-maximal inhibition) for various endpoints, the lowest values were found for beta-S100 in C6 cells, and for NSE in N18TG-2 cells. In lower and intermediate concentrations, the inhibitory effects of the heavy metals on the content of beta-S100 and NSE occurred in the absence of any detectable effect on intracellular LDH activity, and independently of total cellular protein inhibition. The sensitive and excess responses of the neurospecific endpoints relative to that of the non-specific endpoints may reflect the specific neurotoxic insults of the heavy metals on the cultured cells.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Following conventional deparaffinization and rehydration, the sections were stained with a specific anti-calmodulin antibody by indirect immunoperoxidase method or indirect immunofluorescent method. In the former case, the sections were treated as described previously in the studies on cultured cells (9) . The sections with many red cells were pretreated with methanol for 30 min and 0.01 % hydrogen peroxide for another 30 min to eliminate the pseudoreaction.…”

Section: Methodsmentioning

confidence: 99%

Characteristic localization of calmodulin in human tissues: Immunohistochemical study in the paraffin sections.

Seto‐Ohshima

Sano

Mizutani

1985

Acta Histochem. Cytochem

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Immunocytochemical localization of S-100 protein and calmodulin in C6 glioma cells.

Cited by 5 publications

References 20 publications

Levels and Distribution of the Calcium‐Modulated Proteins S100 and Calmodulin in Rat C6 Glioma Cells

Levels and Distribution of the Calcium‐Modulated Proteins S100 and Calmodulin in Rat C6 Glioma Cells

Neuron and glial cell marker proteins as indicators of heavy metal-induced neurotoxicity in neuroblastoma and glioma cell lines

Characteristic localization of calmodulin in human tissues: Immunohistochemical study in the paraffin sections.

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