scholarly journals Electron microscope localization of acetylcholinesterase and butyrylcholinesterase in the ciliary ganglion of the cat.

1984 ◽  
Vol 32 (8) ◽  
pp. 849-861 ◽  
Author(s):  
R Davis ◽  
G B Koelle ◽  
U J Sanville
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Superior Cervical Ganglion ◽  
Extracellular Space ◽  
Plasma Membranes ◽  
Ganglion Cells ◽  
Ciliary Ganglion ◽  
Cervical Ganglion ◽  
High Concentrations

Ciliary ganglia (CG) of cats were stained for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) by the bis-(thioacetoxy) aurate (I), or Au(TA)2, method for examination by electron microscopy. Acetylcholinesterase was localized along the axolemmas of the preganglionic fibers and their terminals and on the plasmalemmas of the perikarya and dendrites of the ganglion cells, as in the cat superior cervical ganglion (SCG). In contrast to the SCG, AChE was also found in significant amounts in the rough endoplasmic reticulum of the CG cells and dendrites, and in varying but high concentrations in channels of extracellular space in the complex capsular region surrounding the perikarya and dendrites. Butyrylcholinesterase was confined chiefly to the dendritic and perikaryonal plasma membranes of the ganglion cells, as in the SCG. Lysosomes and mitochondria were stained chiefly for non-cholinesterase enzymes, as indicated by the physostigmine-treated controls. The significance of these distributions is discussed.

scholarly journals Electron microscope localization of acetylcholinesterase and butyrylcholinesterase in the superior cervical ganglion of the cat. I. Normal ganglion.

1978 ◽  
Vol 78 (3) ◽  
pp. 785-809 ◽  
Author(s):  
R Davis ◽  
G B Koelle
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
Superior Cervical Ganglion ◽  
Plasma Membranes ◽  
Ganglion Cells ◽  
Stellate Ganglion ◽  
Trophic Factor ◽  
Enzyme Localization ◽  
Cervical Ganglion

The distributions of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) in the superior cervical ganglion (SCG) of the cat were determined by electron microscopy (EM) with the bis-(thioacetoxy)aurate (I), or Au(TA)2, method. Before the infusion of fixative, one of the enzymes was selectively, irreversibly inactivated in vivo, as confirmed by light microscope (LM) examination of sections of the stellate ganglion stained by the more specific copper thiocholine method. Physostigmine-treated controls, for inhibition of AChE or BuChE, were stained concomitantly with tissue for enzyme localization by the Au(TA)2 method for EM examination in each experiment. It was concluded that most of the AChE of the cat SCG is present in the plasma membranes of the preganglionic axons and their terminals, and in the dendritic and perikaryonal plasma membranes of the postsynaptic ganglion cells. BuChE is confined largely to the postsynaptic neuronal plasma membranes. Reasons for the discrepancies between the localizations found by the present direct EM observations and those deduced earlier from LM comparisons of normal and denervated SCG are discussed. It is proposed that a trophic factor released by the preganglionic terminals is probably required for the synthesis of postsynaptic neuronal AChE, and that BuChE may serve as a precursor of AChE at that site.

scholarly journals Laminin in cultured mouse C1300 neuroblastoma cells: immunocytochemical localization by pre- and postembedding electron microscope procedures.

1983 ◽  
Vol 31 (6) ◽  
pp. 755-764 ◽  
Author(s):  
P Liesi
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Plasma Membranes ◽  
Neuroblastoma Cells ◽  
Immunocytochemical Localization ◽  
Adhesion Protein ◽  
Antibody Method ◽  
Ultrathin Sections ◽  
Intercellular Connections

Laminin was localized in cultured mouse C1300 neuroblastoma cells by applying the peroxidase-antiperoxidase technique in preembedding electron microscopy. The results were compared to those obtained by indirect immunofluorescence and by the colloidal gold second antibody method on Epon-embedded ultrathin sections. Laminin was found in the cell membranes and within the rough endoplasmic reticulum as well as in intracytoplasmic vacuoles. Plasma membranes of the neuroblastoma cells showed a patchy localization of laminin that was apparently involved in cell-to-substrate attachment and in gap junction-like intercellular connections. Under normal conditions, the Golgi cisternae contained no laminin. Pretreatment of cells with micromolar concentrations of monensin, however, lead to an accumulation of laminin within the Golgi cisternae. These results support a role for laminin as an adhesion protein in cultured neuroblastoma cells and indicate that laminin is transported through the Golgi complex.

scholarly journals Detection of sialic acid residues in the axonal reticulum of rat superior cervical ganglion cells by lectin-gold cytochemistry.

1990 ◽  
Vol 38 (10) ◽  
pp. 1445-1449 ◽  
Author(s):  
J R Quatacker ◽  
W G Annaert ◽  
W P De Potter
Keyword(s):  
Sialic Acid ◽  
Superior Cervical Ganglion ◽  
Plasma Membranes ◽  
Ganglion Cells ◽  
Ricinus Communis ◽  
Neuronal Cell ◽  
Thin Sections ◽  
Trans Golgi Network ◽  
Cervical Ganglion ◽  
Golgi Network

Highly glycosylated compounds have been demonstrated in the axonal reticulum elements of the superior cervical ganglion cells of the rat, and this is considered to suggest a connection of the reticulum with the trans Golgi side. In the present study, the axonal reticulum and the Golgi elements were further characterized by post-embedding methods of lectin-gold cytochemistry to determine their carbohydrate residues and to see, more specifically, if sialic acid residues could be detected in the axonal reticulum elements. Therefore, the affinity of neuronal cell structures for Limax flavus agglutinin (LFA), wheat germ agglutinin (WGA), and Ricinus communis agglutinin I (RCA-I) was tested in ultra-thin sections of glycolmethacrylate-embedded material, counterstained with phosphotungstic acid (PTA) at low pH. The trans Golgi network, the Golgi-associated axonal reticulum, the reticulum within axons, the large dense-cored vesicles, and the plasma membranes were reactive for all three lectins used. We conclude that the axonal reticulum elements carry sialic acid residues, relating them to the trans Golgi network. The present results support the concept that the axonal reticulum is an extension of the trans network of the Golgi apparatus specialized for neurosecretion.

scholarly journals Electron microscope localization of acetylcholinesterase and butyrylcholinesterase in the superior cervical ganglion of the cat. II. Preganglionically denervated ganglion.

1981 ◽  
Vol 88 (3) ◽  
pp. 581-590 ◽  
Author(s):  
R Davis ◽  
G B Koelle
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membranes ◽  
Ganglion Cells ◽  
Myelinated Fibers ◽  
Low Concentrations ◽  
Cervical Ganglion ◽  
Cervical Ganglia ◽  
Previous Identification ◽  
Total Disappearance ◽  
Microscopic Findings

Cat superior cervical ganglia (SCG), denervated preganglionically 6-8 d previously, were stained for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) by the bis-(thioacetoxy)aurate (I), or Au(TA)2, method and compared by electron microscopy with normal SCG described previously (Davis, R., and G. B. Koelle. 1978. J. Cell Biol. 78:785-809). In confirmation of earlier light microscopic findings by the highly specific copper thiocholine method, there was nearly a total disappearance of AChE from the ganglion; no myelinated or unmyelinated axons with AChE-stained axolemmas were found, and only occasional traces of AChE staining were noted at dendritic and perikaryonal plasma membranes. Considerable staining for BuChE persisted at the latter sites, however. As in the normal SCG, physostigmine-resistant staining, caused by noncholinesterase enzymes plus the possible presence of very low concentrations of AChE or BuChE, was noted at external mitochondrial membranes, elements of the endoplasmic reticulum of neurites and Schwann cells, and also in lysosomes. These findings confirm the previous identification of AChE-stained myelinated fibers in the normal SCG as preganglionic and of the unstained myelinated fibers as postganglionic. It is proposed that the maintenance of AChE at postsynaptic sites in normal ganglia is caused by the release of a trophic factor(s) from presynaptic terminals. The source of the postsynaptic BuChE, which is apparently completely absent from the endoplasmic reticulum of the ganglion cells, remains unexplained.

Copper Localization in Cirrhotic Rat Liver by Scanning Electron Microscopy

1969 ◽  
Vol 27 ◽  
pp. 38-39 ◽  
Author(s):  
J. C. Russ ◽  
E. McNatt
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Copper Acetate ◽  
Lead Citrate ◽  
Dense Bodies ◽  
Transmission Electron ◽  
Electron Mode ◽  
Scanning Electron

In order to study the retention of copper in cirrhotic liver, rats were made cirrhotic by carbon tetrachloride inhalation twice weekly for three months and fed 0.2% copper acetate ad libidum in drinking water for one month. The liver tissue was fixed in osmium, sectioned approximately 2000 Å thick, and stained with lead citrate. The section was examined in a scanning electron microscope (JEOLCO JSM-2) in the transmission electron mode.Figure 1 shows a typical area that includes a red blood cell in a sinusoid, a disse, and a portion of the cytoplasm of a hepatocyte which contains several mitochondria, peribiliary dense bodies, glycogen granules, and endoplasmic reticulum.

scholarly journals ELECTRON MICROSCOPY OF CENTRIFUGED HYPHAE OF NEUROSPORA

1961 ◽  
Vol 9 (3) ◽  
pp. 609-617 ◽  
Author(s):  
M. Zalokar
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Optical Microscope ◽  
Granular Structure ◽  
Cell Physiology ◽  
Cell Structures ◽  
Light Area ◽  
Fat Bodies

Normal and centrifuged hyphae of Neurospora were studied with the electron microscope. The following cell structures could be identified: nuclei with nucleoli, mitochondria, endoplasmic reticulum, ribosomes, glycogen, fat bodies, vacuoles, and vesicles with an inner canalicular system, of unknown nature. In centrifuged hyphae, the glycogen layer appeared as a light area, with a slight indication of granular structure. The ribosome layer consisted of densely packed ribosomes without any membranes. The mitochondrial layer contained spaces filled with ribosomes. The nuclei were loosely packed, with endoplasmic reticulum between them. The "enchylema" layer was composed of vesicles belonging to the endoplasmic reticulum. The vacuolar layer was poorly preserved and consisted of double-walled vesicles. Fat appeared as stellate osmiophilic droplets. These observations were compared with previous observations under the optical microscope and their meaning for cell physiology was discussed.

scholarly journals Rapid isolation of plasma membranes in high yield from cultured fibroblasts

1977 ◽  
Vol 168 (2) ◽  
pp. 187-194 ◽  
Author(s):  
D Thom ◽  
A J Powell ◽  
C W Lloyd ◽  
D A Rees
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Plasma Membranes ◽  
Membrane Vesicles ◽  
High Yield ◽  
Chemical Compositions ◽  
Differential Centrifugation ◽  
Rapid Preparation ◽  
Cultured Fibroblasts ◽  
Good Agreement

1. A method was developed which allows the rapid preparation of pure plasma membranes in high yield from cultured fibroblasts. 2. Cells are lysed in hypo-osmotic borate/EDTA and, after differential centrifugation, the membranes collected by centrifugation on a sucrose barrier. 3. Electron microscopy of the isolated material shows large membrane vesicles essentially free from contaminating organelles. 4. There is no detectable activity of the endoplasmic-reticulum enzyme marker, NADH2—lipoamide oxidoreductase (EC 1.6.4.3), and that of succinate dehydrogenase (EC 1.3.99.1), a marker for mitochondria, is substantially decreased. Chemical compositions are in good agreement with previous observations. 5. This study confirms the usefulness of applied isotopic markers for isolating plasma membranes.

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