Inhibitors of the Biosynthesis and Processing of N-Linked Oligosaccharide

References

• Kornfeld R., Kornfeld S. Comparative aspects of glycoprotein structure Annual Review of Biochemistry, E. S. Snell, P. Boyer, A. Meister, C. C. Richardson. Annual Review, Palo Alto, Calif. 1976; Vol. 45: 217
   Google Scholar
• Wagh P. V., Bahl O. P. Sugar residues on protein. CRC Crit. Rev. Biochem. 1981; 10: 307
   PubMed Web of Science ®Google Scholar
• Schachter H., Roseman S. Mammalian glycosyltransferase. The Biochemistry of Glycoproteins and Proteoglycans, W. J. Lennarz. Plenum Press, New York 1980; 85
   Google Scholar
• Beyer T. A., Sadler J. E., Rearick J. I., Paulson J. C., Hill R. L. Glycosyltransferases and their use in assessing oligosaccharide structure and structure/function relationship. Adv. Enzymol. 1981; 52: 23
   PubMedGoogle Scholar
• Elbein A. D. The role of lipid-linked saccharides in the biosynthesis of complex carbohydrates, in Annual Review of Plant Physiology, W. R. Briggs, P. B. Green, R. L. Jones. Annual Review, Palo Alto, Calif. 1979; Vol. 30: 239
   Google Scholar
• Struck D. S., Lennarz W. J. The function of saccharide-lipids in synthesis of glycoprotein. The Biochemistry of Glycoproteins and Proteoglycans, W. J. Lennarz. Plenum Press, New York 1980; 35
   Google Scholar
• Staneloni R. J., Leloir L. F. The biosynthetic pathway of the asparagine-linked oligosaccharides of glycoprotein. CRC Crit. Rev. Biochem. 1982; 12: 289
   PubMed Web of Science ®Google Scholar
• Li E., Tabas I., Kornfeld S. The synthesis of complex-type oligosaccharides. I. Structure of the lipid-linked oligosaccharide precursor of the complex type oligosaccharides of vesicular stomatitis virus G-protei. J. Biol. Chem. 1978; 253: 7762
   PubMed Web of Science ®Google Scholar
• Lui T., Stetson B., Turco S. J., Hubbard S. C., Robbins P. W. Arrangement of the glucose residues in the lipid-linked oligosaccharide precursor of asparaginyl oligosaccharide. J. Biol. Chem. 1979; 254: 4554
   PubMed Web of Science ®Google Scholar
• Kiely M., McKnight G. S., Schimke R. Studies on the attachment of carbohydrate to ovalbumin nascent chains in hen oviduc. J. Biol. Chem. 1976; 251: 5490
   PubMed Web of Science ®Google Scholar
• Rodriguez Boulan E., Kreibach G., Sabatini G. G. Spatial orientation of glycoproteins in membranes of rat liver rough microsomes. I. Localization of lectin-binding sites in microsomal membrane. J. Cell. Biol. 1978; 78: 874
   PubMed Web of Science ®Google Scholar
• Lingappa V. R., Lingappa J. R., Prasad R., Ebner K., Blobel G. Complex cell-free synthesis, segregation, and core glycosylation of a secretory protei. Proc. Natl. Acad. Sci. U.S.A. 1978; 75: 2338
   PubMed Web of Science ®Google Scholar
• Das R. C., Heath E. C. Dolichyldiphosphoryloligosaccharide-protein oligosaccarhyl transferase: solubilization, purification, and propertie. Proc. Natl. Acad. Sci., U.S.A. 1980; 77: 3811
   PubMed Web of Science ®Google Scholar
• Rothman J. E., Lodish H. I. Synchronized, transmembrane insertion and glycosylation of a nascent membrane protei. Nature 1977; 269: 775
   PubMed Web of Science ®Google Scholar
• Czicki V., Lennarz W. J. Localization of the enzyme system for glycosylation of proteins via the lipid-linked pathway in rough endoplasmic reticulu. J. Biol. Chem. 1977; 252: 7901
   PubMed Web of Science ®Google Scholar
• Vargas I., Carminatti H. Glycosylation of endogenous proteins of the rough and smooth microsomes by a lipid-sugar intermediat. Mol. Cell. Biochem. 1977; 16: 171
   PubMed Web of Science ®Google Scholar
• Parodi A. J., Martin-Barrientos J. Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membrane. Biochem. Biophys. Acta 1977; 500: 80
   PubMed Web of Science ®Google Scholar
• Grinna L. S., Robbins P. W. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharide. J. Biol. Chem. 1979; 254: 8814
   PubMed Web of Science ®Google Scholar
• Hunt L. A., Etchison J. R., Summers D. F. Oligosaccharide chains are trimmed during synthesis of the envelope glycoprotein of vesicular stomatitis viru. Proc. Natl. Acad. Sci. U.S.A. 1978; 75: 754
   PubMed Web of Science ®Google Scholar
• Ugalde R. A., Staneloni R. J., Leloir L. F. Action of glycosidase on the saccharide moiety of the glucose-contining dolichyl diphosphate oligosaccharid. FEBS Lett. 1978; 91: 209
   PubMed Web of Science ®Google Scholar
• Chen W. W., Lennarz W. J. Enzymatic excision of glucosyl units linked to the oligosaccharide chain of glycoprotein. J. Biol. Chem. 1978; 253: 5780
   PubMed Web of Science ®Google Scholar
• Michael J. M., Kornfeld S. Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharide. Arch. Biochem. Biophys. 1980; 199: 249
   PubMed Web of Science ®Google Scholar
• Scher M. G., Waechter C. J. A glucosylated oligosaccharide lipid intermediate in calf brain. Evidence for the transfer of the oligosaccharide into membrane glycoprotein and subsequent removal of glucosyl residue. J. Biol. Chem. 1979; 254: 2630
   PubMed Web of Science ®Google Scholar
• Elting J. J., Chen W. W., Lennarz W. J. Characterization of a glucosidase involved in the initial step of the processing of oligosaccharide chain. J. Biol. Chem. 1980; 255: 2325
   PubMed Web of Science ®Google Scholar
• Kilker R. D., Jr., Saunier B., Tkacz J. S., Herscovics A. Partial purification from Saccharomyces cerevesiae of a soluble glucosidase which removes terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J. Biol. Chem. 1982; 256: 5299
   Web of Science ®Google Scholar
• Grinna L. S., Robbins R. W. Substrate specificities of rat liver microsomal glucosidases which process glycoprotein. J. Biol. Chem. 1980; 255: 2255
   PubMed Web of Science ®Google Scholar
• Burns P. M., Touster O. Purification and characterization of glucosidase II, an endoplasmic reticulum hydrolase involved in glycoprotein biosynthesi. J. Biol. Chem. 1982; 257: 9991
   Google Scholar
• Hubbard S. C., Ivatt R. C. Synthesis and processing of asparagine-linked oligosaccharide. Annual Review of Biochemistry, E. S. Snell, P. Boyer, A. Meister, C. C. Richardson. Annual Review, Palo Alto, Calif. 1981; Vol. 50: 555
   Google Scholar
• Opheim D. J., Touster O. Lysosomal α-d-mannosidases of rat liver. Purification and comparison with the Golgi and cytosolic α-d-mannosidase. J. Biol. Chem. 1978; 253: 1017
   PubMed Web of Science ®Google Scholar
• Tulsiani D. P. R., Opheim D. J., Touster O. Purification and characterization of α-d-mannosidases from rat liver Golgi membrane. J. Biol. Chem. 1977; 252: 3227
   PubMedGoogle Scholar
• Tabas I., Kornfeld S. Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharide. J. Biol. Chem. 1979; 254: 11655
   PubMed Web of Science ®Google Scholar
• Forsee W. T., Schutzbach J. Purification and characterization of a phospholipid-dependent α-mannosidase from rabbit live. J. Biol. Chem. 1981; 256: 6577
   PubMedGoogle Scholar
• Tabas I., Kornfeld S. The synthesis of complex-type oligosaccharides. III. Identification of an α-mannosidase activity involved in a late stage of processing of complex-type oligosaccharide. J. Biol. Chem. 1978; 253: 7779
   PubMed Web of Science ®Google Scholar
• Narasimhan S., Stanley P., Schachter H. Control of glycoprotein synthesis. Lectin-resistant mutants containing only one of two distinct N-acetylglucosaminyl-transferase activitie. J. Biol. Chem. 1977; 252: 3926
   PubMedGoogle Scholar
• Harpaz H., Schachter N. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine: α-d-mannoside, β-2-N-acetylglucosaminyl-transferase I separation from UDP-N-acetylglucosamine:α-d-mannoside β-2-N-acetylglucosaminyl-transferase II. Partial purification and substrate specificit. J. Biol. Chem. 1980; 255: 4885
   PubMed Web of Science ®Google Scholar
• Takatsuki A., Arima K., Tamura J. Tunicamycin, a new antibiotic. I. Isolation and characterization of tunicamyci. J. Antibiot. 1971; 24: 215
   PubMed Web of Science ®Google Scholar
• Takatsuki A., Tamura G. Effect of tunicamycin on the synthesis of macromolecules in cultures of chick embryo fibroblasts infected with Newcastle disease viru. J. Antibiot. 1971; 24: 785
   PubMed Web of Science ®Google Scholar
• Takatsuki A., Tamura G. Tunicamycin; a new antibiotic. II. Some biological properties of the antiviral activity of tunicamyci. J. Antibiot. 1971; 24: 224
   PubMed Web of Science ®Google Scholar
• Takatsuki A., Kawamura K., Okina M., Kodama Y., Ito T., Tamura G. The structure of tunicamyci. Agric. Biol. Chem. 1977; 41: 2307
   Web of Science ®Google Scholar
• Ito T., Kodama Y., Kawamura K., Suzuki K., Takatsuki A., Tamura G. The structure of tunicaminyl uracil, a degradation product of tunicamyci. Agric. Biol. Chem. 1977; 41: 2303
   Web of Science ®Google Scholar
• Ito T., Takatsuki A., Kawamura K., Sato K., Tamura G. Isolation and structures of components of tunicamyci. Agric. Biol. Chem. 1980; 44: 695
   Web of Science ®Google Scholar
• Mahoney W. C., Duskin D. Separation of tunicamycin homologues by reverse phase high performance liquid chromatograph. J. Chromatogr. 1980; 198: 506
   PubMed Web of Science ®Google Scholar
• Keenan R. W., Hamill R. L., Occolowitz J. L., Elbein A. D. Biological activities of isolated tunicamycin and streptovirudin fraction. Biochemistry 1980; 70: 2968
   Google Scholar
• Tkacz J. S., Lampen J. O. Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf liver microsome. Biochem. Biophys. Res. Commun. 1975; 65: 248
   PubMed Web of Science ®Google Scholar
• Takatsuki A., Kohno K., Tamura G. Inhibition of biosynthesis of polyisoprenyl sugars in chick embryo microsomes by tunicamyci. Agric. Biol. Chem. 1975; 39: 2089
   Web of Science ®Google Scholar
• Struck D. K., Lennarz W. T. Evidence for the participation of saccharide lipids in synthesis of the oligosaccharide chain of ovalbumi. J. Biol. Chem. 1977; 252: 1007
   PubMed Web of Science ®Google Scholar
• Lehle L., Tanner W. The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivative. FEBS Lett. 1976; 71: 167
   Web of Science ®Google Scholar
• Heifetz A., Kennan R. W., Elbein A. D. Mechanism of action of tunicamycin on the UDP-GlcNAc: dolichyl-phosphate GlcNAc-1-phosphate transferas. Biochemistry 1979; 18: 2186
   PubMed Web of Science ®Google Scholar
• Keller R. K., Boon D. Y., Crum F. C. N-acetylglucosamine-1-phosphate transferase from hen oviduct: solubilization characterization and inhibition by tunicamyci. Biochemistry 1979; 18: 3946
   PubMed Web of Science ®Google Scholar
• Takatsuki A., Tamura G. Inhibition of glucoconjugate biosynthesis by tunicamyci. Tunicamycin, G. Tamura. Japan Scientific Societies Press, Tokyo 1982; 35
   Google Scholar
• Elbein A. D., Occolowitz J. L., Hamill R. L., Eckardt K. Streptovirudins of series I and II; Chemical and biological propertie. Biochemistry 1981; 20: 4210
   PubMed Web of Science ®Google Scholar
• Tkacz J. S. Tunicamycin and related antibiotics, in Antibiotics V. I., Modes and Mechanisms of Microbial Growth Inhibitors. Springer Verlag, in press.
   Google Scholar
• Elbein A. D. The tunicamycins, useful tools for glycoprotein studie. Trends Biochem. Sci. 1981; 6: 219
   Google Scholar
• Eckardt K., Thrum N., Bradler G., Tonew E., Tonew M. Streptovirudins, new antibiotics with antibacterial and antiviral activity. II. Isolation chemical characterization and biological activity of streptovirudin. J. Antibiot. 1975; 28: 274
   PubMed Web of Science ®Google Scholar
• Tkacz J. S., Wong A. Comparison of the biological and chemical properties of tunicamycin and mycospocidi. Fed. Proc. 1978; 37: 1766
   Google Scholar
• Mizano M., Shimojima Y., Sugawara T., Takeda I. An antibiotic 2401. J. Antibiot. 1971; 24: 896
   PubMedGoogle Scholar
• Kenig M., Reading C. Holomycin and an antibiotic (mm19290) related to tunicamycin, metabolites o. Streptomyces clavuligerus, J. Antibiot. 1979; 32: 549
   PubMed Web of Science ®Google Scholar
• Tkacz J. S. Antibiotics of the tunicamycin famil. Fed. Proc. 1980; 39: 1830
   Google Scholar
• Elbein A. D., Gafford T., Kang M. S. Inhibition of lipid-linked saccharide synthesis: Comparison of tunicamycin, streptovirudin, and antibiotic 2401. Arch. Biochem. Biophys. 1979; 196: 311
   PubMed Web of Science ®Google Scholar
• Hasilik A., Tanner W. Carbohydrate moiety of carboxypeptidase Y and perturbation of its biosynthesi. Eur. J. Biochem. 1978; 91: 567
   PubMedGoogle Scholar
• Schwaiger H., Tanner W. Effects of gibberellic acid and of tunicamycin on glycosyl-transferase activities and on α-amylase secretion in barle. Eur. J. Biochem. 1979; 102: 375
   PubMedGoogle Scholar
• Hickman S., Kulczycki A., Jr., Lynch R. G., Kornfeld S. Studies of the mechanism of tunicamycin inhibition of IgA and IgE secretion by plasma cell. J. Biol. Chem. 1977; 252: 4402
   PubMed Web of Science ®Google Scholar
• Seagar M. J., Miquelis R. D., Simon C. Inhibitory effects of tunicamycin and 2-deoxyglucose on thyroglobulin synthesi. Eur. J. Biochem. 1980; 113: 91
   PubMedGoogle Scholar
• Leavitt R., Schlesinger S., Kornfeld S. Impaired intracellular migration and altered solubility of non-glycosylated glycoproteins of vesicular stomatitis virus and Sindbis viru. J. Biol. Chem. 1977; 252: 9018
   PubMed Web of Science ®Google Scholar
• Olden K., Pratt R. M., Yamada K. M. Role of carbohydrate in protein secretion and turnover: Effects of tunicamycin on the major cell surface glycoprotein of chick embryo fibroblast. Cell 1978; 13: 461
   PubMed Web of Science ®Google Scholar
• Olden K., Pratt R. M., Yamada K. M. Selective cytoxicity of tunicamycin for transformed cell. Int. J. Cancer 1979; 24: 60
   PubMed Web of Science ®Google Scholar
• Schwarz R. T., Rohrschneider J. M., Schmidt M. F. G. Suppression of glycoprotein formation of Semliki Forest influenza, and avian sarcoma virus by tunicamyci. J. Virol. 1976; 19: 782
   PubMed Web of Science ®Google Scholar
• Schultz A. M., Oroszlan S. Tunicamycin inhibits glycosylation of precursor polypeptide encoded by env Gen. Biochem. Biophys. Res. Commun. 1979; 86: 1206
   PubMed Web of Science ®Google Scholar
• Weintraub B. D., Stannard B. S., Linnekin D., Marshall M. Relationship of glycosylation to de novo thyroid-stimulating hormone biosynthesis and secretion by mouse pituitary tumor cell. J. Biol. Chem. 1980; 255: 5715
   PubMed Web of Science ®Google Scholar
• Edwards K., Nagashina M., Dryburgh H., Wykes A., Schreiber G. Secretion of proteins from liver cells is suppressed by the proteinase inhibitor N-α-tosyl-l-lysyl-chloromethane, but not by tunicamycin, an inhibitor of glycosylatio. FEBS Lett. 1979; 100: 269
   PubMed Web of Science ®Google Scholar
• Struck D. K., Siuta P. R., Lane M. D., Lennarz N. J. Effect of tunicamycin on the secretion of serum proteins by primary cultures of rat and chick hepatocyte. J. Biol. Chem. 1978; 253: 5332
   PubMed Web of Science ®Google Scholar
• Mizrahi A., O'Malley J. A., Carter W. A., Takatsuki A., Tamura G., Sulkowski E. Glycosylation of interferons: Effects of tunicamycin on human immune interfero. J. Biol. Chem. 1978; 253: 7612
   PubMed Web of Science ®Google Scholar
• Fujisuwa J. I., Iwakura Y., Kawade Y. Non-glycosylated mouse l-cell interferons produced by the action of tunicamyci. J. Biol. Chem. 1978; 253: 8677
   PubMedGoogle Scholar
• Hickman S., Kornfeld S. Effect of tunicamycin on IgM, IgA, and IgG secretion by mouse plastocytoma cell. J. Immunol. 1978; 121: 990
   PubMed Web of Science ®Google Scholar
• Keller R. K., Swank G. D. Tunicamycin does not block ovalbumin secretion in the oviduc. Biochem. Biophys. Res Commun. 1978; 85: 762
   PubMed Web of Science ®Google Scholar
• Cox G. S. Synthesis of the glycoprotein hormone α-subunit and placental alkaline phosphatase by Hela cells: Effects of tunicamycin, 2-deoxyglucose and sodium butyrat. Biochemistry 1981; 20: 4893
   PubMed Web of Science ®Google Scholar
• Bielinska M., Grant G. A., Boime I. Processing of placental peptide hormones synthesized in lysates containing membranes derived from tunicamycin-treated ascites tumor cell. J. Biol. Chem. 1978; 253: 7117
   PubMed Web of Science ®Google Scholar
• Anishi H. R., Tkacz J. S., Lampen J. O. Glycoprotein nature of yeast alkaline phosphatase: Formation of active enzyme in the presence of tunicamyci. J. Biol. Chem. 1979; 254: 11943
   PubMed Web of Science ®Google Scholar
• Gibson R., Schlesinger S., Kornfeld S. The non-glycosylated glycoprotein of vesicular stomatitis virus is temperature-sensitive and undergoes intracellular aggregation at elevated temperature. J. Biol. Chem. 1979; 254: 3600
   PubMed Web of Science ®Google Scholar
• Gibson R., Kornfeld S., Schlesinger S. A role for oligosaccharides in glycoprotein biosynthesi. Trends Biochem. Sci. 1980; 5: 290
   Web of Science ®Google Scholar
• Datema R., Schwarz R. Inhibitors of glycoprotein synthesi. Adv. Carbohydr. Chem. Biochem., in press.
   Google Scholar
• Kaluza G., Schmidt M. F. G., Schlotissek C. Effect of 2-deoxyglucose on the multiplication of Semliki Forest virus and the reversal of the block by mannos. Virology 1973; 54: 179
   PubMed Web of Science ®Google Scholar
• Datema R., Schwarz R. Formation of dolichol monophosphate 2-deoxyglucose and its interference with the glycosylation of mannoproteins in yeas. Eur. J. Biochem. 1976; 67: 239
   PubMedGoogle Scholar
• Datema R., Schwarz R. Formation of 2-deoxyglucose-containing lipid-linked oligosaccharides. Interference with glycosylation of glycoprotein. Eur. J. Biochem. 1978; 90: 505
   PubMedGoogle Scholar
• Datema R., Pont Lezica R., Robbins P. W., Schwarz R. Deoxyglucose inhibition of protein glycosylation: Effects of nucleotide deoxysugars on the formation of glucosylated lipid intermediate. Arch. Biochem. Biophys. 1981; 206: 65
   PubMed Web of Science ®Google Scholar
• Eagon P. K., Heath E. C. Glycoprotein biosynthesis in myeloma cells. Characterization of non-glycosylated immunoglobulin light chain secreted in the presence of 2-deoxy-d-glucos. J. Biol. Chem. 1977; 252: 2372
   PubMed Web of Science ®Google Scholar
• Datema R., Schwarz R., Jankowski A. W. Fluoroglucose inhibition of protein glycosylation in vivo. Inhibition of mannose and glucose incorporation into lipid-linked oligosaccharide. Eur. J. Biochem. 1980; 109: 331
   PubMedGoogle Scholar
• Schmidt M. F. G., Schwarz R. T., Ludwig H. Fluorosugars inhibit biological properties of different enveloped viruse. J. Virol. 1976; 18: 819
   PubMed Web of Science ®Google Scholar
• Schwarz R. T., Schmidt M. F. G., Answer V., Klenk H. D. Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugar. J. Virol. 1977; 23: 217
   PubMed Web of Science ®Google Scholar
• Datema R., Schwarz R. T. Interference with glycosylation of glycoproteins. Inhibition of formation of lipid-linked oligosaccharide. in vivo, Biochem. J. 1979; 184: 113
   PubMed Web of Science ®Google Scholar
• Koch V., Schwarz R. T., Scholtissek C. Glucosamine itself mediates reversible inhibition of protein glycosylation. A study of glucosamine metabolism at inhibitory concentrations in influenza virus-infected cell. Eur. J. Biochem. 1979; 94: 515
   PubMedGoogle Scholar
• Pan Y. T., Elbein A. D. The formation of lipid-linked oligosaccharides in Madin-Darby canine kidney cells. Changes in oligosaccharide profiles induced by glucosamin. J. Biol. Chem. 1982; 257: 2795
   PubMed Web of Science ®Google Scholar
• Pan Y. T., Elbein A. D., unpublished observations.
   Google Scholar
• Heinemann B., Kaplan M. A., Muir R. D., Hooper I. R. Amphomycin, a new antibioti. Antibiot. Chemother. 1953; 111: 1239
   Google Scholar
• Bodansky M., Sigler G. F., Bodansky A. Structure of the peptide antibiotic Amphomyci. J. Am. Chem. Soc. 1973; 95: 2352
   PubMed Web of Science ®Google Scholar
• Tanaka H., Oiwa R., Matsukura S., Inokoshi J., Omura S. Studies on bacterial cell wall inhibitors. X. Properties of phospho-N-acetylmuramoyl-pentapeptide transferase in peptidoglycan synthesis of Bacillus megalerium and its inhibition by Amphomyci. J. Antibiot. 1982; 35: 1216
   PubMed Web of Science ®Google Scholar
• Shoji T. Recent chemical studies on peptide antibiotics from the genus Bacillu. Adv. Appl. Microbiol. 1978; 24: 187
   PubMedGoogle Scholar
• Kang M. S., Spencer J. P., Elbein A. D. Amphomycin inhibition of raannose and GlcNAc incorporation into lipid-linked saccharide. J. Biol. Chem. 1978; 253: 8860
   PubMed Web of Science ®Google Scholar
• Spencer J. P., Elbein A. D. Transfer of mannose from GDP-mannose to lipid-linked oligosaccharides by soluble mannosyl transferas. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 2524
   PubMed Web of Science ®Google Scholar
• Jensen J. W., Schutzbach J. S. The biosynthesis of oligosaccharide-lipids. Partial purification and characterization of mannosyl transferase I. J. Biol. Chem. 1981; 256: 12899
   PubMed Web of Science ®Google Scholar
• Chapman A., Fujimoto K., Kornfeld S. The primary glycosylation defect in class E Thy-1-negative mutant mouse lymphoma cells is an inability to synthesize dolichol-P-mannos. J. Biol. Chem. 1980; 255: 4441
   PubMed Web of Science ®Google Scholar
• Bannerjee D. K., Scher M. G., Waechter C. J. Amphomycin: Effect of the lipopeptide antibiotic on the glycosylation and extraction of dolichyl monophosphate in calf brain microsome. Biochemistry 1981; 20: 1561
   PubMed Web of Science ®Google Scholar
• Ericson J. G., Gafford J., Elbein A. D. In vivo and in vitro inhibition of lipid-linked saccharide and glycoprotein synthesis in plants by Amphomyci. Arch. Biochem., Biophys., 191, 598, 1089.
   Google Scholar
• Elbein A. D. The effect of tsuschimycin on the synthesis of lipid-linked saccharides in aort. Biochem. J. 1981; 193: 477
   PubMed Web of Science ®Google Scholar
• Stone K. J., Strominger J. L. Mechanism of action of bacitracin: Complexation with metal ion and C-55-isoprenyl pyrophosphat. Proc. Natl. Acad. Sci. U.S.A. 1971; 68: 3223
   PubMed Web of Science ®Google Scholar
• Stone K., Strominger J. L. Inhibition of sterol biosynthesis by bacitraci. Proc. Natl. Acad. Sci. U.S.A. 1972; 69: 1287
   PubMed Web of Science ®Google Scholar
• Schechter N., Momose K., Rudney H. The effect of bacitracin and Ca++ on the formation of polyprenylpyrophosphates and their incorporation into ubiquinone precursors in mammalian and bacterial system. Biochem. Biophys. Res. Commun. 1972; 48: 83
   Web of Science ®Google Scholar
• McKelvy T., LeBlanc P., Laudes C., Perrie S., Grimm-Jorgenson Y., Kordon C. The use of bacitracin as an inhibitor of the degradation of thyrotropin-releasing factor and leiteinzing hormone releasing facto. Biochem. Biophys. Res. Commun. 1976; 73: 507
   PubMed Web of Science ®Google Scholar
• Chen W. W., Lennarz W. J. Participation of a trisaccharide-lipid in glycosylation of oviduct membrane glycoprotein. J. Biol. Chem. 1976; 251: 7802
   PubMed Web of Science ®Google Scholar
• Hercovics A., Bugge B., Jeanloz R. W. Effect of bacitracin on the biosynthesis of dolichol derivatives in calf pancreas microsome. FEBS Lett. 1977; 82: 215
   PubMed Web of Science ®Google Scholar
• Reuvers F., Boer P., Styen-Parvé E. P. The effect of bacitracin on the formation of polyprenol derivatives in yeast membrane vesicle. Biochem. Biophys. Res. Commun. 1978; 82: 800
   PubMed Web of Science ®Google Scholar
• Spencer J. P., Kang M. S., Elbein A. D. Inhibition of lipid-linked saccharide synthesis by bacitraci. Arch. Biochem. Biophys. 1978; 190: 829
   PubMed Web of Science ®Google Scholar
• Ericson M. C., Gafford J., Elbein A. D. Bacitracin inhibits the synthesis of lipid-linked saccharides and glycoproteins in plant. Plant Physiol. 1978; 62: 373
   PubMed Web of Science ®Google Scholar
• Nishimura H., Mayama M., Komatsu Y., Kato H., Shimaoka N., Tanaka Y. Showdomycin, a new antibiotic from . Streptomyces sp., J. Antibiot. 1964; 17: 148
   PubMed Web of Science ®Google Scholar
• Roy-Burman S., Roy-Burman P., Visser D. W. Showdomycin, a new nucleoside antibioti. Cancer Res. 1968; 28: 1605
   PubMed Web of Science ®Google Scholar
• Kang M. S., Spencer J. P., Elbein A. D. The effect of showdomycin on glycolipid formation. Inhibition of glucosyl-phosphoryl-dolichol in aorta and stimulation of glucosylceramide in yeas. J. Biol. Chem. 1979; 254: 10037
   PubMed Web of Science ®Google Scholar
• Müller T., Bause E., Jaenicke L. Glycolipid formation in Volvox carteri t. Nagariensis. Effects of tunicamycin and showdomyci. FEBS Lett. 1981; 128: 208
   PubMed Web of Science ®Google Scholar
• Kean E. L. Effect of the inhibition of the formation of dolichol-phosphate-mannose on the biosynthesis of the N-acetylglucosaminylpyrophosphoryl polyprenols by the retin. Biochim. Biophys. Acta, in press.
   Google Scholar
• Rogers H. J., Perkins H. R., Ward J. B. Microbial Cell Walls and Membranes. Chapman and Hall, London 1980; 298
   Google Scholar
• Brown W. E., Seinerova V., Chan W. M., Laskin A. I., Linnet P., Strominger J. L. Inhibition of cell wall synthesis by the antibiotics diumycin and janiemyci. Ann. N. Y. Acad. Sci. 1974; 235: 399
   PubMed Web of Science ®Google Scholar
• Meyers E., Slusarchyk D. S., Bouchard J. L., Weisenborn F. L. Diumycins, new members of an antibiotic family having prolonged in vivo activit. J. Antibiot. 1969; 22: 490
   PubMed Web of Science ®Google Scholar
• Lugtenberg E. J. J., Hellings J. A., Van de Berg G. J. Inhibition of peptidoglycan synthesis by the antibiotic Diumycin . Antimicrobiol. Agents Chemother. 1972; 2: 485
   PubMed Web of Science ®Google Scholar
• Babczinski P. Inhibition of lipid-linked mannose and mannoprotein synthesis in yeast by diumycin in vitr. Eur. J. Biochem. 1980; 112: 53
   PubMedGoogle Scholar
• Villemez C. L., Carlo P. L. Properties of a soluble polyprenyl phosphate. UDP-GlcNAc-1-P transferas. J. Biol. Chem. 1980; 255: 8174
   PubMed Web of Science ®Google Scholar
• Turco S. Modification of oligosaccharide-lipid synthesis and protein glycosylation in glucose-deprived cell. Arch. Biochem. Biophys. 1980; 205: 330
   PubMed Web of Science ®Google Scholar
• Sefton B. M. Immediate glycosylation of Sinbis Virus membrane protei. Cell 1977; 10: 659
   PubMed Web of Science ®Google Scholar
• Datema R., Schwarz R. T. Effect of energy depletion on the glycosylation of a viral glycoprotei. J. Biol. Chem. 1981; 256: 11191
   PubMed Web of Science ®Google Scholar
• Colgate S. M., Dorling P. R., Huxtable C. R. A spectrophotometric investigation of swainsonine, an α-mannosidase inhibitor isolated fro. Swainsona canescens, Aust. J. Chem. 1979; 32: 2257
   Web of Science ®Google Scholar
• Dorling P. R., Huxtable C. R., Colegate S. M. Lysosomal storage in Swainsona spp. toxicosis. An induced mannosidosi. Neuropathol. Appl. Neurobiol. 1978; 4: 285
   PubMed Web of Science ®Google Scholar
• Dorling P. R., Huxtable C. R., Colegate S. M. Inhibition of lysosomal α-mannosidase by swainsonine, an indolizidine alkaloid isolated from Swainsona canescen. Biochem. J. 1980; 191: 649
   PubMed Web of Science ®Google Scholar
• Molyneux R. J., James J. P. Loco intoxication: indolizidine alkaloids of spotted locowee. (Astragalus lentiginosus), Science 1982; 216: 190
   Google Scholar
• Schneider M. J., Ungemach F. S., Harris T. M. (IS, 2R, 8R, 8αR)-1,2,8-trihydroxyoctahy-droindolizine (swainsonine) an α-mannosidase inhibitor from Rhizoctonia leguminicol. Tetrahedron, in press.
   Google Scholar
• Elbein A. D., Solf R., Dorling P. R., Vosbeck K. Swainsonine, an inhibitor of glycoprotein processin. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 7393
   PubMed Web of Science ®Google Scholar
• Tarentino A. L., Maley F. Purification and properties of an endo-β-N-acetyl-glucosaminidase fro. Streptomyces griseus, J. Biol. Chem. 1974; 249: 811
   PubMedGoogle Scholar
• Elbein A. D., Dorling P. R., Vosbeck K., Horisberger M. Swainsonine prevents the processing of the oligosaccharide chains of influenza virus hemagglutini. J. Biol. Chem. 1982; 257: 1573
   PubMed Web of Science ®Google Scholar
• Nakamura K., Compans R. D. Glycopeptide components of influenza viral glycoprotein. Virology 1978; 86: 432
   PubMed Web of Science ®Google Scholar
• Tulsiani D. P. R., Harris T. M., Touster O. Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase I. J. Biol. Chem. 1982; 257: 7936
   PubMed Web of Science ®Google Scholar
• Elbein A. D., Pan Y. T., Solf R., Vosbeck K. Effect of Swainsonine, an inhibitor of glycoprotein processing on cultured mammalian cell. J. Cell. Physiol. 1983; 115: 265
   PubMed Web of Science ®Google Scholar
• Hohenschutz L. D., Bell E. A., Jewess P. J., Leworthy D. P., Pryce R. J., Arnold E., Clardy J. Castanospermine, a 1,6,7,8-tetrahydroxyoctahydroindolizine alkaloid, from seeds o. Castanospermun australe, Phytochemistry 1981; 20: 811
   Web of Science ®Google Scholar
• Saul R., Chambers J. P., Molyneux R. J., Elbein A. D. Castanospermine, a tetrahydroxylated alkaloid that inhibits β-glucosidase and β-glucocerebrosidas. Arch. Biochem. Biophys. 1983; 221: 265
   Web of Science ®Google Scholar
• Pan Y. T., Hori H., Saul R., Sanford B. A., Molyneux R. J., Elbein A. D. Castanospermine inhibits the processing of the oligosaccharide portion of the influenza viral hemagglutini. Biochemistry 1983; 22: 3975
   PubMed Web of Science ®Google Scholar
• Inouye S., Tsuruoka T., Ito T., Nüda T. Structure and synthesis of Nojirimyci. Tetrahedron 1968; 24: 2125
   PubMed Web of Science ®Google Scholar
• Frommer W., Junge B., Müeller L., Schmidt D., Truscheit E. New enzyme inhibitors from microorganism. Planta Med. 1979; 35: 195
   PubMed Web of Science ®Google Scholar
• Schmidt D. D., Frommer W., Müeller L., Truscheit E. Glucosidase-inhibitoen aus Brazille. Naturwissenschaften 1979; 66: 584
   PubMed Web of Science ®Google Scholar
• Hanozet G., Pircher H., Vanni P., Oesch B., Semenza G. An example of enzyme hysteresis. The slow and tight interaction of some fully competitive inhibitors with small intestinal sucras. J. Biol. Chem. 1981; 256: 3703
   PubMed Web of Science ®Google Scholar
• Chambers J. P., Elbein A. D., Williams J. C. Nojirimycin — a potent inhibitor of purifieid lysosomal α-glucosidase from human live. Biochem. Biophys. Res. Commun. 1982; 107: 1490
   PubMed Web of Science ®Google Scholar
• Saunier B., Kilker R. D., Tkaez J. S., Quaroni A., Herscovics A. Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidase. J. Biol. Chem. 1982; 257: 14155
   PubMed Web of Science ®Google Scholar
• Legler G., Lotz W. Functionelle gruppen am activen Centrum liver α-glucosidase au. Saccharomycescerevesiae, Hoppe-Seyler's Z. Physiol. Chem. 1973; 354: 243
   PubMedGoogle Scholar
• Datema R., Romer P. A., Legler G., Schwarz R. T. Inhibition of formation of complex oligosaccharides by the glucosidase inhibitor bromocondurito. Proc. Natl. Acad. Sci. U.S.A., 79, 6787.
   Google Scholar
• Lucas J. J., Levin E. Increase in the lipid intermediate pathway of protein glycosylation during hen oviduct differentiatio. J. Biol. Chem. 1977; 252: 4330
   PubMed Web of Science ®Google Scholar
• Harford J. R., Waechter C. J., Earl F. L. Effect of exogenous dolichyl monophosphate on a developmental change in mannosylphosphoryldolichol biosynthesi. Biochem. Biophys. Res. Commun. 1977; 76: 1036
   PubMed Web of Science ®Google Scholar
• Grange P. K., Adair W. L., Jr. Studies on the biosynthesis of dolichyl-phosphate: Evidence for the in vitro formation of 2,3-dehydrodolichyl phosphat. Biochem. Biophys. Res. Commun. 1977; 79: 734
   PubMed Web of Science ®Google Scholar
• Mills J. J., Adamany A. M. Impairment of dolichyl saccharide synthesis and dolichol-mediated glycoprotein assembly in the aortic smooth muscle cell in culture by inhibitors of cholesterol biosynthesi. J. Biol Chem. 1978; 253: 5270
   PubMed Web of Science ®Google Scholar
• James M. J., Kandutsch A. A. Interrelationships between dolichol and sterol synthesis in mammalian cell culture. J. Biol. Chem. 1979; 254: 8442
   PubMed Web of Science ®Google Scholar
• Keller R. K., Adair W. L., Jr., Ness G. C. Studies on the regulation of glycoprotein biosynthesis. An investigation of the rate-limiting steps of dolichol-P biosynthesi. J. Biol. Chem. 1979; 254: 9966
   PubMed Web of Science ®Google Scholar
• Tavares I. A., Coolbear T., Hemming F. W. Increased hepatic dolichol and dolichyl-mediated glycosylation in rats fed cholestero. Arch. Biochem. Biophys. 1981; 207: 427
   PubMed Web of Science ®Google Scholar
• White D. A., Middleton B., Rawson S., Bradshaw R. O., Clegg R. J., Hemming F. W., Bell G. C. Regulation of dolichol and cholesterol biosynthesis in cholesterol-fed rabbit. Arch. Biochem. Biophys. 1981; 208: 30
   PubMed Web of Science ®Google Scholar
• Kandutsch A. A., Chen H. W., Heineger H. Biological activity of some oxygenated sterol. Science 1978; 201: 498
   PubMed Web of Science ®Google Scholar
• Endo A., Kuroda M., Tanzawa K. Completive inhibition of 3-hydroxy-3-methylglutaryl Co A reductase by ML-236Z and ML-236B fungal metabolites having hypocholesterolemic activit. FEBS Lett. 1976; 72: 323
   PubMed Web of Science ®Google Scholar
• Brown A. G., Smale T. C., King T. J., Hasenkamp R., Thompson R. H. Crystal and molecular structure of compactin, a new antifungal metabolite from Penicillium brevicompactu. J. Chem. Soc. Perkins Trans. I. 1976; 1165
   Google Scholar
• Goldstein J. L., Helgeson J. A. S., Brown M. S. Inhibition of cholesterol synthesis with compactin renders growth of cultured cells dependent on the low density lipoprotein recepto. J. Biol. Chem. 1979; 254: 5403
   PubMed Web of Science ®Google Scholar
• Carson D. P., Lennarz W. J. Inhibition of polyisoprenoid and glycoprotein biosynthesis causes abnormal embryonic developmen. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 5709
   PubMed Web of Science ®Google Scholar
• Pressman B. C. Biological applications of ionophore. Annu. Rev. Biochem. 1976; 45: 501
   PubMed Web of Science ®Google Scholar
• Tartakoff A. M., Vassalli P. Plasma cell immunoglobulin secretion. Arrest is accompanied by alterations of the Golgi comple. J. Exp. Med. 1977; 146: 1332
   PubMed Web of Science ®Google Scholar
• Uchida N., Smilowitz H., Tanzer M. L. Monovalent ionophores inhibit secretion of procollagen and fibronectin from cultured human fibroblast. Proc. Natl. Acad. Set., U.S.A. 1979; 76: 1868
   PubMed Web of Science ®Google Scholar
• Ledger P. W., Uchida N., Tanzer M. L. Immunocytochemical localization of procollagen and fibronectin in human fibroblasts: Effects of the monovalent ionophore, monensi. J. Cell. Biol. 1980; 87: 663
   PubMed Web of Science ®Google Scholar
• Srinivas R. V., Melsen L. R., Compans R. W. Effects of monensin on morphogenesis and infectivity of Friend murine leukemia viru. J. Virol. 1982; 42: 1067
   PubMed Web of Science ®Google Scholar
• Chaterjee S., Bradac J. A., Hunter E. Effect of monensin on Mason-Pfizer monkey virus glycoprotein synthesi. J. Virol. 1982; 44: 1003
   PubMed Web of Science ®Google Scholar
• Kaariainen L., Hashimoto K., Saraste J., Xertanen I., Penttinen K. Monensin and FCCP inhibit the intracellular transport of alphavirus membrane glycoprotein. J. Cell Biol. 1980; 87: 783
   PubMed Web of Science ®Google Scholar
• Johnson D. C., Schlesinger M. J. Vesicular stomatitis virus and Sindbis virus glycoprotein transport to the cell surface is inhibited by ionophore. Virology 1980; 103: 407
   PubMed Web of Science ®Google Scholar
• Schmitt J. W., Elbein A. D. Inhibition of protein synthesis also inhibits synthesis of lipid-linked oligosaccharide. J. Biol. Chem. 1979; 254: 12291
   PubMed Web of Science ®Google Scholar
• Hubbard S. C., Robbins P. W. Synthesis of N-linked oligosaccharides of glycoproteins. Assembly of the lipid-linked precursor oligosaccharide and its relation to protein synthesis in viv. J. Biol. Chem. 1980; 255: 11782
   PubMed Web of Science ®Google Scholar
• Reitman M. L., Trowbridge I. S., Kornfeld S. A lecin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoprotein-processing enzym. J. Biol. Chem. 1982; 257: 10357
   PubMed Web of Science ®Google Scholar
• Stanley P. Surface carbohydrate alterations of mutant mammalian cells selected for resistance to plant lectin. The Biochemistry of Glycoproteins and Proteoglycans, W. J. Lennarz. Plenum Press, New York 1980; 161
   Google Scholar