Gene/Protein Disease Symptom Drug Enzyme Compound
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Changes in ultrastructure and cytoskeletal organization by avian oxyntic cells, at the onset of HCl secretion, were analysed. Cells in resting state, induced by fasting and cimetidine, were compared with histamine stimulated secreting cells. Ultrastructural studies were done by transmission electron microscopy; the distribution of prekeratin, myosin, and filamin-like protein, by immunofluorescence; and that of F-actin using FITC-phalloidin. Resting cells show short pericellular clefts. These are increasingly deepened in secreting cells by a reorganization of the lateral cell borders involving displacement of the junctional complexes toward the cell base and incorporation of the tubular system to the luminal plasma membrane. In secreting cells, the processes of the secretory surface are concentrated in a pericellular groove. Histamine stimulation induces a drastic redistribution of cytoskeletal proteins. In chicken oxyntic cells, in addition to the F-actin cytoskeleton associated with the membranes of the secretory surface, there is a cytoskeletal ring containing F-actin, myosin, and a filamin-like protein, located at the level of the junctional complexes. In resting cells, filaments and masses of cytoskeletal matrix are associated with the zonula adherens. In secreting cells, the junctional complexes maintain their association with the filamentous ring, while the amorphous matrix is replaced by microfilaments that support the processes of the luminal surface. Intermediate filaments form a peripheral ring probably associated with the zonula adherens, and project from the ring toward the cell cytoplasm. Thus, with the onset of HCl secretion, the apical cytoskeletal ring of resting cells displaces toward the cell base. A role for this cytoskeletal ring in the changes in shape parallel to HCl secretion is discussed.
Anat Rec 1990 Oct
PMID:Redistribution of membranes and cytoskeletal proteins in chicken oxyntic cells during the HCl secretory cycle: ultrastructural and immunofluorescence study. 170 Jun 49

The cholinergic and histaminergic projections have important neuromodulatory functions in the ascending visual pathways, so we compared the pattern and mode of innervation of the two projections in the lateral geniculate complex (dorsal lateral geniculate nucleus and pregeniculate nucleus) of the macaque monkey. Brain tissue from macaques was immunoreacted by means of antibodies to choline acetyltransferase (ChAT) or to histamine and processed for light and electron microscopy. A dense plexus of thin, highly branched ChAT-immunoreactive axons laden with varicosities was found in all layers of the dLGN including the koniocellular laminae and in the pregeniculate nucleus. ChAT label was more dense in magnocellular layers 1 and 2 than in parvocellular layers 3-6 and relatively sparse in the interlaminar zones. Varicosities associated with the cholinergic axons had an average of three conventional asymmetric synapses per varicosity, and these appeared to contact dendrites of both thalamocortical cells and interneurons. Histamine-immunoreactive axons were distributed homogeneously throughout all laminar and interlaminar zones of the dLGN, but were denser in the pregeniculate nucleus than in the dLGN. Histaminergic axons branched infrequently and were typically larger in caliber than cholinergic axons. The overwhelming majority of varicosities were found en passant and rarely displayed conventional synapses, despite the abundance of synaptic vesicles, and were not associated preferentially with specific cellular structures. The innervation of the macaque dLGN complex by cholinergic and histaminergic systems is consistent with their proposed role in state dependent modulation of thalamic activity. The dense and highly synaptic innervation by cholinergic axons supports the proposal of additional involvement of these axons in functions related to eye movements.
Anat Rec 1999 07 01
PMID:Comparison of cholinergic and histaminergic axons in the lateral geniculate complex of the macaque monkey. 1041 96