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 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 Advancing Age Alters the Contribution of Calcium Release From Smooth Endoplasmic Reticulum Stores in Superior Cervical Ganglion Cells

2009 ◽  
Vol 64A (1) ◽  
pp. 34-44 ◽  
Author(s):  
E. J. Behringer ◽  
C. K. Vanterpool ◽  
W. J. Pearce ◽  
S. M. Wilson ◽  
J. N. Buchholz
Keyword(s):  
Endoplasmic Reticulum ◽  
Superior Cervical Ganglion ◽  
Calcium Release ◽  
Ganglion Cells ◽  
Smooth Endoplasmic Reticulum ◽  
Cervical Ganglion

Nucleotide depletion increases trafficking of gentamicin to the Golgi complex in LLC-PK1 cells

2002 ◽  
Vol 283 (6) ◽  
pp. F1422-F1429 ◽  
Author(s):  
Ruben M. Sandoval ◽  
Robert L. Bacallao ◽  
Kenneth W. Dunn ◽  
Jeffrey D. Leiser ◽  
Bruce A. Molitoris
Keyword(s):  
Cell Culture ◽  
Golgi Complex ◽  
Lens Culinaris ◽  
Ricinus Communis ◽  
Physiological State ◽  
Complex Mechanism ◽  
Trans Golgi Network ◽  
Golgi Network ◽  
Texas Red ◽  
Number Of Cells

Having shown rapid trafficking of aminoglycosides to the Golgi complex in cell culture, we focused on the injurious interaction that occurs when gentamicin administration is preceded by renal ischemia. Using Texas red-labeled gentamicin as a tracer, we determined that 15 min of cellular nucleotide depletion did not significantly increase subsequent uptake. However, cells previously depleted of nucleotides accumulated significantly more Texas red-labeled gentamicin within a dispersed Golgi complex. Using Ricinus communis and Lens culinaris lectins, which label specific compartments of the Golgi complex ( trans-Golgi network/ trans and medial/ cis compartments, respectively), we determined that the medial/ cis compartment dispersed after 15 min of nucleotide depletion but the trans-Golgi network/ trans compartment remained unaffected. An increase in the number of cells exhibiting disrupted medial/ cis-Golgi morphology after repletion in physiological media containing gentamicin was also seen. In summary, the increase in nephrotoxicity seen when ischemia precedes aminoglycoside uptake may be part of a complex mechanism initially involving increased Golgi accumulation and prolonged Golgi dispersion. The Golgi complex must then endure the effects of gentamicin accumulated in larger quantities in an aberrant physiological state.

scholarly journals Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus.

1988 ◽  
Vol 106 (3) ◽  
pp. 617-628 ◽  
Author(s):  
J R Duncan ◽  
S Kornfeld
Keyword(s):  
Sialic Acid ◽  
Golgi Apparatus ◽  
Chinese Hamster ◽  
Murine Lymphoma ◽  
Trans Golgi Network ◽  
Intracellular Movement ◽  
Golgi Region ◽  
Golgi Compartment ◽  
Mannose 6 Phosphate ◽  
Golgi Network

We have used Chinese hamster ovary (CHO) cells and a murine lymphoma cell line to study the recycling of the 215-kD and the 46-kD mannose 6-phosphate receptors to various regions of the Golgi to determine the site where the receptors first encounter newly synthesized lysosomal enzymes. For assessing return to the trans-most Golgi compartments containing sialyltransferase (trans-cisternae and trans-Golgi network), the oligosaccharides of receptor molecules on the cell surface were labeled with [3H]galactose at 4 degrees C. Upon warming to 37 degrees C, the [3H]galactose residues on both receptors were substituted with sialic acid with a t1/2 approximately 3 hrs. Other glycoproteins acquired sialic acid at least 8-10 times slower. Return of the receptors to the trans-Golgi cisternae containing galactosyltransferase could not be detected. Return to the cis/middle Golgi cisternae containing alpha-mannosidase I was measured by adding deoxymannojirimycin, a mannosidase I inhibitor, during the initial posttranslational passage of [3H]mannose-labeled glycoproteins through the Golgi, thereby preserving oligosaccharides which would be substrates for alpha-mannosidase I. After removal of the inhibitor, return to the early Golgi with subsequent passage through the Golgi complex was measured by determining the conversion of the oligosaccharides from high mannose to complex-type units. This conversion was very slow for the receptors and other glycoproteins (t1/2 approximately 20 h). Exposure of the receptors and other glycoproteins to the dMM-sensitive alpha-mannosidase without movement through the Golgi apparatus was determined by measuring the loss of mannose residues from these proteins. This loss was also slow. These results indicate that both Man-6-P receptors routinely return to the Golgi compartment which contains sialyltransferase and recycle through other regions of the Golgi region less frequently. We infer that the trans-Golgi network is the major site for lysosomal enzyme sorting in CHO and murine lymphoma cells.

scholarly journals A cytochemical study of lectin receptors on isolated chick neural retina neurons in vitro

1982 ◽  
Vol 53 (1) ◽  
pp. 1-20
Author(s):  
J.A. Bee
Keyword(s):  
Sialic Acid ◽  
Cell Body ◽  
Growth Cone ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Neuronal Cell ◽  
Cytochemical Study ◽  
Lectin Receptors ◽  
Dolichos Biflorus ◽  
Dolichos Biflorus Agglutinin

The cell body, neurite and growth cone of isolated retinal neurons have been compared on the basis of their ability to bind a number of fluorescently labelled lectins, each possessing a unique carbohydrate specificity. The susceptibility of the respective binding patterns following pretreatment of these fixed cells with either neuraminidase or trypsin was also investigated. Neuronal cell bodies displayed the most intense binding of each lectin, with localization of limulin binding (specific for sialic acid) predominantly to the neurite hillock, the point on the cell body from which the neurite projects. Limulin binding was almost totally abolished by pretreatment with either neuraminidase or trypsin. In contrast to the cell body, limulin binding to the neurite or growth cone was not detected. These regions of the cell apparently possessed sialic acid, however, since pretreatment with neuraminidase reduced wheat germ agglutinin binding (to N-acetylglucosamine) and markedly enhanced Dolichos biflorus agglutinin binding (to N-acetylgalactosamine) to both the neurite and growth cone. The initially low binding of Dolichos biflorus agglutinin to the neurite and growth cone was slightly enhanced by pretreatment with trypsin. Uniformly low levels of binding of either Ricinus communis agglutinin 60 (galactose, N-acetylgalactosamine) or R. communis agglutinin 120 (galactose) was observed over the entire neuron. R. communis agglutinin 120 binding was not enhanced by pretreatment with neuraminidase. Receptors for either concanavalin A (mannose, glucose) or Ulex europaeus agglutinin I (fucose) were abundant over the entire nerve cell with the former exhibiting more marked trypsin sensitivity. From these data, it is apparent that the repertoire of lectin binding sites of the neurite and growth cone of these differentiating nerve cells differs markedly from that of the cell body, which itself demonstrates some degree of regionalization.

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