Disposition Kinetics and Bioavailability of the Glucosidase Inhibitor N-Benzyl-1-deoxynojirimycin After Various Routes of Administration in Mice

References

• Bivin W. S., Crawford M. P., Brewer N. R. Morphophysiology. The Laboratory Rat, H. J. Baker, J. R. Lindsey, S. H. Weisbroth. Academic Press, New York 1979; 73–103
   Google Scholar
• Bollen M., Stalmans W. The antiglycogenolytic action of 1-deoxyno-jirimycin results from a specific inhibition of the α-1,6-glucosidase activity of the debranching enzyme. Eur. J. Biochem 1989; 181: 775–780
   PubMedGoogle Scholar
• Böshagen H., Junge B., Kinast G., Schüller M., Stoltefuss J., Paessens A. Synthesis of Benzyldeoxynojirimycin. Patent EP 315, 1989, p. 17, Bayer A. G., Germany
   Google Scholar
• Elbein A. D. Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem 1987; 56: 497–534
   PubMed Web of Science ®Google Scholar
• Faber E. D. Pharmacokinetics of Glycosidase Inhibitors. Thesis, Rijksuniversiteit Groningen. 1993; 118–121
   Google Scholar
• Faber E. D., Oosting R., Neefjes J. J., Ploegh H. L., Meijer D. K. F. Distribution and elimination of the glycosidase inhibitors 1-deoxyman-nojirimycin and N-methyl-1-deoxynojirimycin in the rat in vivo. Pharm. Res 1992; 9: 1442–1450
   PubMed Web of Science ®Google Scholar
• Fischer P., Collin M., Karlsson G. B., James W., Butters T. D., Davis S. J., Gordon S., Dwek R. A., Piatt F. M. The alpha-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4-binding. J. Virol 1995; 69: 5791–5797
   Web of Science ®Google Scholar
• Fuhrmann U., Bause E., Ploegh H. L. Inhibitors of oligosaccharide processing. Biochim. Biophys. Acta 1985; 825: 95–110
   PubMed Web of Science ®Google Scholar
• Gruters R. A., Neefjes J. J., Tersmette M., De Goede R. E. Y., Tulp A., Huisman H. G., Miedema F., Ploegh H. L. Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase. Nature 1987; 330: 74–77
   PubMed Web of Science ®Google Scholar
• Hackbarth H., Hackbarth D. Genetic analysis of renal function in mice. 1. Glomerular filtration rate and its correlation with body and kidney weight. Lab. Anim 1981; 15: 267–272
   PubMedGoogle Scholar
• Kuranda M. J., Aronson N. N., Jr. Receptor-mediated endocytosis and lysosomal degradation of asialoglycoproteins by the liver. Lysosomes: Their Role in Protein Breakdown, H. Glaumann, F. J. Ballard. Academic Press, London 1987; 241–282
   Google Scholar
• Lee S. M., Bustamante S., Flores C., Bezerra J., Goda T., Koldovsky O. Chronic effects of an α-glucosidase inhibitor (BAY o 1248) on intestinal disaccharidase activity in normal and diabetic mice. J. Pharmacol. Exp. Ther 1987; 240: 132–137
   PubMed Web of Science ®Google Scholar
• Lembcke B., Fölsch U. R., Creutzfeldt W. Effect of 1-desoxyno-jirimycin derivatives on small intestinal disaccharidase activities and on active transport in vitro. Digestion 1985b; 31: 120–127
   PubMed Web of Science ®Google Scholar
• Lembcke B., Fölsch U. R., Gatzemeier W., Ebert R., Siegel E., Creutzfeldt W. Inhibition of glycemic and hormonal responses after repetitive sucrose and starch loads by different doses of the α-glucosidase inhibitor miglitol (BAY m 1099) in man. Pharmacology 1991a; 43: 318–328
   PubMed Web of Science ®Google Scholar
• Lembcke B., Fölsch U. R., Gatzemeier W., Lücke B., Ebert R., Siegel E., Creutzfeldt W. Inhibition of sucrose- and starch-induced glycaemic and hormonal responses by the α-glucosidase inhibitor emigli-tate (BAY o 1248) in healthy volunteers. Eur. J. Clin. Pharmacol 1991b; 41: 561–567
   PubMed Web of Science ®Google Scholar
• Lembcke B., Folsch U. R., Rumpf K. W., Creutzfeldt W. α-Glucosidase inhibition by deoxynojirimycin derivatives. Diabetes Res. Clin. Pract 1985a; 1: S334–S335, Abstract
   Google Scholar
• Madara J. L. Loosening tight junctions: Lessons from the intestine. J. Clin. Invest 1989; 83: 1089–1094
   PubMed Web of Science ®Google Scholar
• Proost J. H. Application of a numerical deconvolution technique in the assessment of bioavailability. J. Pharm. Sci 1985; 74: 1135–1136
   PubMed Web of Science ®Google Scholar
• Puls W., Krause H. P., Müller L., Schutt H., Sitt R., Thomas G. Inhibitors of the rate of carbohydrate and lipid absorption by the intestine. Int. J. Obes 1984; 8: 181–190
   PubMed Web of Science ®Google Scholar
• Rhinehart B. L., Begovic M. E., Robinson K. M. Quantitative relationship of lysosomal glycogen accumulation to lysosomal α-glucosidase inhibition in castanospermine treated rats. Biochem. Pharmacol 1991; 41: 223–228
   PubMed Web of Science ®Google Scholar
• Roerig D. L., Kotrly K. J., Dawson C. A., Ahlf S. B., Gualtieri J. F., Kampine J. P. First-pass uptake of verapamil, diazepam, and thiopental in the human lung. Anesth. Analg 1989; 69: 461–466
   PubMed Web of Science ®Google Scholar
• Romero P. A., Saunier B., Herscovics A. Comparison between 1-deoxynojirimycin and N-methyl-1-deoxynojirimycin as inhibitors of oligosaccharide processing in intestinal epithelial cells. Biochem. J 1985; 226: 733–740
   PubMed Web of Science ®Google Scholar
• Schmidt D. D., Frommer W., Müller L., Truscheit E. Glucosidase-Inhibitoren aus Bazillen. Naturwissenschaften 1979; 66: 584–585
   PubMed Web of Science ®Google Scholar
• Schnack C., Röggla G., Luger A., Schernthaner G. Effects of the α-glucosidase inhibitor 1-desoxynojirimycin (BAY m 1099) on postprandial blood glucose, serum insulin and C-peptide levels in type II diabetic patients. Eur. J. Clin. Pharmacol 1986; 30: 417–419
   PubMed Web of Science ®Google Scholar
• Steinke W. Intestinal absorption mechanism of the glucosidase inhibitor BAY m 1099. Naunyn Schmiedebergs Arch. Pharmacol 1986; 332(Suppl)R41, Abstract
   Google Scholar
• Tan A., Van den Broek L., Van Boeckel C., Ploegh H., Bolscher J. Chemical modification of the glucosidase inhibitor 1-deoxynojirimycin: Structure-activity relationships. J. Biol. Chem 1991; 266: 14504–14510
   PubMed Web of Science ®Google Scholar
• Taylor R. H., Barker H. M., Bowey E. A., Canfield J. E. Intestinal monosaccharide transport is unimpaired by deoxynojirimycin-derived glycosidase inhibitors. Clin. Sci 1984; 67: 63P, Abstract
   Web of Science ®Google Scholar
• Trown P. W., Reardan D. T., Carroll S. F., Stoudemire J. B., Kawahata R. T. Improved pharmacokinetics and tumor localization of immunotoxins constructed with the Mr 30,000 form of ricin A chain. Cancer Res 1991; 51: 4219–4225
   PubMed Web of Science ®Google Scholar
• Van den Broek L. A. G. M., Vermaas D. J., Heskamp B. M., Van Boeckel C. A. A., Tan M. C. A. A., Bolscher J. G. M., Ploegh H. L., Van Kemenade F. J., De Goede R. E. Y., Miedema F. Chemical modification of azasugars, inhibitors of N-glycoprotein-processing glycosidases and of HIV-I infection. Review and structure-activity relationships. Reel. Trav. Chim. Pays-Bas 1993; 112: 82–94
   Google Scholar
• Varki A. Biological roles of oligosaccharides: All of the theories are correct. Glycobiology 1993; 3: 97–130
   PubMed Web of Science ®Google Scholar