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A Seto-Ohshima

Publications and source records attributed to A Seto-Ohshima.

27 records · Page 2Linked to original sources
PubMed1988

[Calmodulin and neuron: immunohistochemical studies].

Calmodulin is present in higher concentrations in brain tissues. The content rapidly increased during the 2nd postnatal week in rat brain. Although the protein is ubiquitous in all eukaryotic cells, immunohistochemical studies have revealed that calmodulin is mainly localized in the neurons, exhibiting a similar distribution to that of gamma-type neuron-specific enolase. In the mouse retina, both calmodulin and gamma-enolase were found to be localized in optic nerves, ganglion cells, and inner and outer plexiform layers. The development study showed that gamma-enolase increased in the 2nd postnatal week and that the levels of calmodulin did not significantly change in that stage. In the mouse retina with an inherited retinal dysplasia (C3H), in which all the photoreceptor cells degenerate during the 2nd and 3rd postnatal weeks, calmodulin-specific staining decreased in the residual layers. Calmodulin is also enriched in mammalian testes. In the mouse testis, levels of calmodulin were high in the spermatocytes and in the spermatids, as compared to the level in spermatozoa. This suggests that the large amount of calmodulin in the testis may be associated with miotic divisions and/or spermatogenesis. Immunocytochemical staining of calmodulin in C6 glioma cells and PC12 pheochromocytoma cells showed a high level of calmodulin to be localized on the half spindles between poles and chromosomes in mitotic cells. The protein was also shown to be localized on fibrous structures in the interphase of those cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1987

The effect of axotomy and denervation on calmodulin content in the superior cervical sympathetic ganglion of the rat.

Calmodulin (CaM) in the superior cervical sympathetic ganglion (SCG) of the rat and its changes after transection of the pre- or postganglionic nerves were studied biochemically and immunohistochemically. The concentration of CaM in the SCG was assayed using the extent of activation of CaM-dependent adenylate cyclase from bovine neural retina. In the SCG, CaM concentration was 4.5 micrograms/mg protein, a level similar to that in another peripheral ganglion, the nodose ganglion (4.9 micrograms/mg protein). Following denervation of the SCG, the total amount of ganglionic CaM did not change significantly within a week. On the other hand, CaM content per ganglion increased gradually 3 days after axotomy. Immunohistochemical examination revealed that CaM in unoperated SCG is present both in the neuronal fibers and in the cell soma of sympathetic neurons. But the intensity of the staining with CaM-antibody in the cytoplasmic soma varied among cells. The gross profile of the CaM immunostaining seemed to be unchanged one week after either denervation or axotomy, but the immunoelectron microscopic study showed heavy staining of the innercellular membranes of irregular shape in the axotomized SCG.

Adenylyl Cyclases↗
PubMed1987

The early expression of immunoreactivity for calmodulin in the nervous system of mouse embryos.

Calmodulin (CaM) is a major calcium-binding protein in the brain, where its immunoreactivity is mainly localized in the neurons. In this study, ontogenical changes in the distribution of CaM in the nervous system of mouse embryos were investigated immunohistochemically using a specific antibody against CaM and an indirect immunoenzyme method. Immunoreactive staining was first observed in the marginal layer of the cranial neural tube after 9.5 days of gestation; thereafter, the amount of stained structures increased rapidly. Particularly intense staining was observed in the long neuronal processes extending from or into the brain and spinal cord primordia. Intense immunostaining was also observed in the optic nerve layer of early retinae from 12.5 days of gestation. The appearance of CaM immunoreactivity is thus an early event during neuronal differentiation, apparently concomitant with the initiation of axon extension and the appearance of neurofilament proteins.

Animals↗
PubMed1984

Forskolin suppresses seizures induced by pentylenetetrazol in mice.

Forskolin, an adenylate cyclase activator when injected s.c. (1 mg/kg) in mice, caused an elevation of cAMP in the forebrain and cerebellum of up to 170% and 130%, respectively. The treatment was found to prevent seizures induced by pentylenetetrazol. This suppression had subsided 30 min after the injection, when cAMP level was again normal in the cerebellum but still elevated in the forebrain.

Adenylyl Cyclases↗
PubMed1984

Immunohistochemical appearance of calmodulin in the developing brain: a comparison with neuron specific enolase.

Calmodulin is a small, acidic, calcium-binding protein thought to regulate many cellular functions. In the brain of the adult mouse, calmodulin was found immunohistochemically to localize mainly in the neurons. In the developing brain, the immunoreactivity to anti-calmodulin antibody appeared early in the cells in the low brain stem but late in the cerebral cortex, hippocampus, and cerebellum, except for the deep cerebellar nuclei. The cells in the major proliferative layer present during early development, such as the matrix cells in the cerebral cortex and the cells in the external granular layer in the cerebellum, did not show the immunoreactivity. In the cerebral cortex, the migrating cells and the cells in the cortical plate were also negative while the deep cortical cells, which had probably settled in their final position, became positive. The comparison of these results with the immunohistochemical appearance of neuron specific enolase, a characteristic protein in the brain, suggested that calmodulin appeared with some maturation of the neurons as neuron specific enolase.

Animals↗
PubMed1983

Immunohistochemical localization of calmodulin in mouse brain.

Calmodulin is a well-known calcium-binding protein which is ubiquitous in the plant and animal kingdoms and regulates many cellular processes. In this paper, the distribution of calmodulin in mouse brain was studied immunohistochemically using specific anti-calmodulin IgG which was raised in the rabbit by immunization with native calmodulin. Immunoreactive staining was observed in the cells in almost all areas of the brain, but its intensity varied. Some areas were stained heavily even in the presence of high concentration of NaCl. These differed from those stained immunohistochemically with antibody against other calcium-binding proteins, parvalbumin or vitamin D-dependent calcium-binding protein.

Animals↗
PubMed1983

Production of antibodies to calmodulin in rabbits and enzyme immunoassays for calmodulin and anti-calmodulin.

The production of anti-calmodulin antibodies in rabbit was examined with the use of performic acid-oxidized calmodulin from bovine brain or an emulsion of native calmodulin and methylated bovine serum albumin as the antigen. The antibodies in rabbit sera were determined serially by means of a sensitive enzyme immunoassay method that uses a mini-column of goat (anti-rabbit IgG) IgG-coupled Sepharose 4B for separation. The antibodies could be produced in rabbits with either antigen. Although the native calmodulin with methylated bovine serum albumin seemed to be a better antigen, the titer of antiserum was not raised to levels detectable in the double immunodiffusion test. Monospecific antibodies were purified from the antiserum, and a competitive enzyme immunoassay method for the assay of calmodulin was developed with the use of the column-separation technique employed in the assay of anti-calmodulin. The method could determine from 10 ng to 10 micrograms (0.6 pmol to 0.6 nmol) of rat calmodulin and gave no cross-reaction with S-100 protein. Calmodulin contents in rat brain determined by the present method were consistent with those measured by the bioassay using calmodulin-deficient phosphodiesterase.

Animals↗