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A Shimamura

Publications and source records attributed to A Shimamura.

63 records · Page 4Linked to original sources
PubMed1982

Comparative study of ultrastructures of the lateral-line organs and the palatal taste organs in the African clawed toad, Xenopus laevis.

The fine structure of the lateral-line organ and the palatal taste organ in the African clawed toad, Xenopus laevis, was examined by means of electron microscopy. The lateral-line organ consisted of hair and accessory cells. The apical surface of a hair cell was studded with one kinocilium and 20 to 40 stereocilia. Synaptic bodies and subsynaptic cisternae were found in the cytoplasm of a hair cell adjacent to the synaptic contacts with the afferent and the efferent nerve endings, respectively. Crystalline bodies were observed in both the nucleoplasm and the cytoplasm of almost all hair cells. The palatal taste organ consisted of three types of cells: the taste, sustentacular, and the Merkel cells. The taste cells contained numerous dense-cored vesicles which accumulated in close association with both the afferent synapses and the basal plasma membrane. The possibility was raised from the ultrastructural results that these vesicles had dual functions as both neurotransmitter and hormone. The existence of Merkel cells in the palatal taste organ suggested that this organ might function not only as a chemoreceptor but also as a mechanoreceptor. In spite of possible chemosensory function of the lateral-line organ in Xenopus, its ultrastructure was significantly different from that of the typical gustatory organ, the palatal taste organ, in this animal.

Animals↗
PubMed1979

The occurrence of ciliated and mucous cells in the peripapillary trench of the rat tongue.

Ciliated cells surrounded by mucous cells were found near the base of the peripapillary trench of the rat circumvallate papilla. The ciliated cells occurred singly or in small groups. Each cilium showed the nin plus two filament pattern characteristic of motile cilia. We consider that these cells function in wetting the taste pores, circulating saliva containing tastants and removal of debris from the papillary trench.

Animals↗
PubMed1979

Effect of salts on water-insoluble glucan formation by glucosyltransferase of Streptococcus mutans.

The formation of water-insoluble glucan by extracellular glucosyltransferase from Streptococcus mutans 6715 found to be greatly stimulated by various mono- or divalent cations. An enzyme preparation, obtained by ethanol fractionation, was able to catalyze the formation of water-insoluble glucan from sucrose in the presence of monovalent cations above 100mM or divalent cations above 20 mM at neutral pH. As the concentration of monovalent and divalent cations was reduced to below 10 mM and 1 mM, respectively, the formation of insoluble glucan decreased to a negligible amount. High concentrations of these cations were found to stimulate the formation of insoluble glucan in the following ways: (i) it increased the activity of total glucosyltransferase up to 1.6- and 2.7-fold in the absence and presence of a primer dextran, respectively, and (ii) it changed the formation of soluble glucan to insoluble. It was postulated that one of the essential factors for the formation of insoluble glucan would be to keep more than two water-soluble glucan chains close to enzyme aggregates and that such interaction could be enhanced by the presence of high cation concentrations.

Carbohydrate Metabolism↗
PubMedDate not supplied

Ribosomal S6 kinase 1 (RSK1) activation requires signals dependent on and independent of the MAP kinase ERK.

BACKGROUND: The rsk1 gene encodes the 90 kDa ribosomal S6 kinase 1 (RSK1) protein, which contains two kinase domains. RSK1, which is involved in regulating cell survival and proliferation, lies at the end of the signaling cascade mediated by the extracellular signal-regulated kinase (ERK) subfamily of mitogen-activated protein (MAP) kinases. ERK activation and subsequent phosphorylation of the RSK1 carboxy-terminal catalytic loop stimulates phosphotransferase activity in the RSK1 amino-terminal kinase domain. When activated, RSK1 phosphorylates both nuclear and cytoplasmic substrates through this amino-terminal catalytic domain. It is thought that stimulation of the ERK/MAP kinase pathway is sufficient for RSK1 activation, but how ERK phosphorylation activates the RSK1 amino-terminal kinase domain is not known. RESULTS: The individual isolated RSK1 kinase domains were found to be under regulatory control. In vitro kinase assays established that ERK phosphorylates RSK1 within the carboxy-terminal kinase domain, and the phosphoinositide-dependent kinase 1 (PDK1) phosphorylates RSK1 within the amino-terminal kinase domain. In transiently transfected HEK 293E cells, PDK1 alone stimulated phosphotransferase activity of an isolated RSK1 amino-terminal kinase domain. Nevertheless, activation of full-length RSK1 in the absence of serum required activation by both PDK1 and ERK. CONCLUSIONS: RSK1 is phosphorylated by PDK1 in the amino-terminal kinase-activation loop, and by ERK in the carboxy-terminal kinase-activation loop. Activation of phosphotransferase activity of full-length RSK1 in vivo requires both PDK1 and ERK. RSK1 activation is therefore regulated by both the mitogen-stimulated ERK/MAP kinase pathway and a PDK1-dependent pathway.

3-Phosphoinositide-Dependent Protein Kinases↗