About: Indolizidine is a(n) research topic. Over the lifetime, 1104 publication(s) have been published within this topic receiving 22885 citation(s).
31 Dec 1998-
Abstract: Preface. Acknowledgments. Introduction. Fatty acids. Acetylenic compounds in plants. Plant waxes. Polyketides. Benzoquinones. Naphthoquinones, and anthraquinones. Shikimic acid pathway. Phenylpropanoids. Coumarins. 2-pyrones, stilbenes, dihydrophenanthrenes, and xanthones. Flavonoids. Tannins. Non-protein amino acids. Peptides. Carbohydrates. Cyanogenic glycosides, and Cyanolipids. Glucosinolates. Introduction to terpenes. Monoterpenes. Iridoid monoterpenes. Sesquiterpenes. Diterpenes and sesterterpences. Triterpenes and steroids. Saponins and cardenolides. Limonoids, Quassinoids and related compounds. Tetraterpenes or cartenoids. Limonoids, quassinoids, and related compounds. Simple aimines, simple aromatic and pyridine alkaloids. Pyrrolidine, tropane, piperidine, and polyeketide alkaloids. Pyrrolizidine, quinolizidine and indolizidine alkaloids. Alkaloids derived from anthranilic acid. Isoquinoline and benzylisoquineoline alkaloids. Alkaloids derived from both tyrosine and phenylalanine. Indole alkaloids. Ergot and other indole alkaloids. Alkaloids of terpenoid orgin. Miscellaneous types of alkaloids.
09 Apr 1982-Science
Abstract: The indolizidine alkaloids swainsonine and swainsonine N-oxide have been isolated and identified as constituents of spotted locoweed. The inhibition of lysosomal α-mannosidase by these alkaloids su...
01 Nov 1980-Biochemical Journal
Abstract: An indolizidine alkaloid (swainsonine) was isolated from the plant Swainsona canescens. Swainsonine is a specific and potent inhibitor of alpha-mannosidase (EC 220.127.116.11) and when administered to animals produces a phenocopy of the genetically based lysosomal storage disease, mannosidosis. Evidence is presented to suggest that swainsonine is a reversible active site-directed inhibitor of lysosomal alpha-mannosidase.
Joseph P. Michael1•Institutions (1)
01 Jan 1994-Natural Product Reports
Abstract: Covering: July 2000 to June 2001. Previous review: Nat. Prod. Rep., 2001, 18, 520This review covers the isolation, structure determination, synthesis and biological activity of indolizidine and quinolizidine alkaloids from microbial, plant and animal sources. Included in the review are slaframine; hydroxylated indolizidines and their analogues; alkaloids from ants and amphibians; metabolites of the genera Prosopis, Streptomyces and Nuphar and the Lythraceae; phenanthroindolizidines and related alkaloids; lupin alkaloids; and alkaloids from sponges, tunicates and coccinellid beetles. The literature from July 2000 to June 2001 is reviewed, and 172 references are cited.
Abstract: Swainsonine, an indolizidine alkaloid, inhibits the processing of asparagine-linked glycoproteins in both cell-free extracts and animal cells in culture. Thus, in a liver particulate enzyme preparation, swainsonine at 0.1-1.0 microM inhibited the mannosidase that releases [3H]mannose from a high mannose glycopeptide but only slightly inhibited the release of glucose from a glucose-labeled glycopeptide. MDCK and Chinese hamster ovary cells in culture incorporate [2-3H]mannose and [6-3H]glucosamine into both high mannose and complex types of oligosaccharides. When these cells were incubated with swainsonine and then labeled with mannose or glucosamine, there was a dramatic decrease in the amount of label in the complex type of glycopeptide and a substantial increase in the radioactivity in the high mannose type. This change was monitored by the increase in radioactivity that became susceptible to digestion by endoglucosaminidase H with increasing concentrations of swainosine. The endoglucosaminidase H-released oligosaccharide(s) from swainsonine-treated cells was larger and more homogeneous than that from controls and eluted from Bio-Gel P-4 at the position of Man9GlcNAc. Several tissue culture cell lines were grown in the presence of swainsonine to determine its effect on cell surface glycoproteins. Cells grown in the alkaloid showed an increased capacity to bind Escherichia coli B886, a bacterium that binds to high mannose glycoproteins. These cells also showed an increasing binding of [3H]concanavalin A.