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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 92 (1990), S. 137-146 
    ISSN: 1573-4919
    Keywords: myoblast ; glycoprotein ; cell fusion ; ketoconazole
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The effect of ketoconazole on the fusion of L6 myoblasts was studied. Ketoconazole was a potent inhibitor of myoblast fusion at concentrations as low as 0.1 μM, but fusion was restored when the inhibitor was removed. The inhibitor resulted in decreased binding of conA and WGA to cell surface oligosaccharides showing that it was inhibiting N-linked cell surface glycoproteins. Inhibition of fusion by ketoconazole was accompanied by reduced creatine phosphokinase activities showing that it is affecting biochemical differentiation. Incorporation of labelled mannose from GDP-mannose into lipid-sugar and lipid-oligosaccharide complexes involved in the synthesis of N-linked oligosaccharides was also inhibited by ketoconazole, but the inhibition was reversed by addition of exogenous dolichol phosphate to the incorporation mixture. The main conclusion from these studies was that ketoconazole inhibited fusion of L6 myoblasts by affecting the synthesis of dolichol-phosphate required for the synthesis of lipid-oligosaccharides needed for the synthesis of fusogenic cell surface N-linked glycoproteins.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 241 (1995), S. 439-450 
    ISSN: 0003-276X
    Keywords: Golgi ; TGN ; Inflammation ; Acute phase response ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Background: During the acute phase response to inflammation, the Golgi apparatus of rat hepatocytes processes an increased quantity of glycoproteins, in the form of acute phase reactants.Methods: The compartmental organization of the hepatocyte Golgi of control and 24 hour inflamed rats was studied, using transmission electron microscopic techniques, including cytochemistry, to detect nicotinamide adenine dinucleotide phosphatase (NADPase), thiamine pyrophosphatase (TPPase), and cytidine monophosphatase (CMPase) activity.Results: In inflamed rats, individual Golgi stacks were enlarged, but retained their organization into four compartments:1) a phosphatase negative, perforated cis-element, 2) two mid-saccules which sometimes were positive for NADPase, 3) one or occasionally two NADPase and TPPase positive trans-saccules, and 4) a tubulovesicular trans-Golgi network (TGN) which was NADPase reactive and contained a spotty TPPase reaction product. Two of these compartments were noticably altered in response to inflammation. The two mid-saccules were consistently and uniformly dilated. The TGN was altered to the point of being difficult to recognize and had acquired CMPase reactivity. In control rats the TGN consisted of anastomosing tubules forming cage-like structures; secretory granules containing lipoprotein particles pinched off from these. In inflamed rats, most of the cage-like TGN structures had been replaced with an extensive vesicular syncytium which produced secretory granules with a granulofilamentous content.Conclusions: In hepatocytes from inflamed rats an apparent switch had occured in the type of secretory material processed by the Golgi apparatus. Furthermore, the inflammation-induced increase in the size of individual Golgi stacks apparently was not due to a parallel increase in size of all Golgi saccules. Rather, saccules within given Golgi compartments responded in a characteristic and specific manner to the increase in glycoprotein processing that occurs during inflammation. © 1995 Wiley-Liss, Inc.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4986
    Keywords: sialyltransferase ; glycorprotein ; baculovirus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Values ofK m were determined for three purified sialyltransferases and the corresponding recombinant enzymes. The enzymes were Galβ1-4GlcNAc α2-6sialyltransferase and Galβ1-3(4)GlcNAc α2-3sialyltransferase from rat liver; these enzymes are responsible for the attachment of sialic acid to N-linked oligosaccharide chains; and the Galβ1-3GalNAc α2-3sialyltransferase from porcine submaxillary gland that is responsible for the attachment of sialic acid to O-linked glycoproteins and glycolipids. A procedure for the large scale expression of active sialyltransferases from recombinant baculovirus-infected insect cells is described. For the liver enzymes values ofK m were determined using rat and human asialoα1 acid glycoprotein andN-acetyllactosamine as variable substrates; lacto-N-tetraose was also used with the Galβ1-3(4)GlcNAc α2-3sialyltransferase. Antifreeze glycorprotein was used as the macromolecular acceptor for the porcine enzyme. Values forK m were also determined using CMP-NeuAc as the variable substrate.
    Type of Medium: Electronic Resource
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