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Chemical Compound Review

Polymannose     (2S,3S,4R,5R)-2,3,4,5,6- pentahydroxyhexanal

Synonyms: D-Mannose;, Poly(mannose), QSPL 159, AG-F-03190, AG-F-18436, ...
 
 
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Disease relevance of D-mannose

 

High impact information on D-mannose

  • Results of glycosidase digestions and lectin cytochemistry experiments suggest that many of the axonally transported glycoprotein carbohydrates are polymannose and/or hybrid N-linked oligosaccharides [5].
  • Endoglycosidase H (endo H) digestion prior to lectin cytochemistry characterized a large population of the axonally transported Con A binding sites as polymannose and/or hybrid N-linked oligosaccharides (endo H-susceptible) [5].
  • The enzyme, behaving as a lectin binding polymannose glycans of varied structures, would belong together with its enzymatically inactive homologue Htm1p/Mnl1p/EDEM, to a transport chain responsible for delivering irreparably misfolded glycoproteins to proteasomes [6].
  • In hepatocellular carcinoma HepG2 cells, free polymannose-type oligosaccharides appearing in the cytosol during the biosynthesis and quality control of glycoproteins are rapidly translocated into lysosomes by an as yet poorly defined process (Saint-Pol, A., Bauvy, C., Codogno, P., and Moore, S. E. H. (1997) J. Cell Biol. 136, 45-59) [7].
  • Cytosol-to-lysosome transport of free polymannose-type oligosaccharides. Kinetic and specificity studies using rat liver lysosomes [7].
 

Biological context of D-mannose

  • The large molecular size of N-glycosylated lysozyme with a polymannose chain was predominantly expressed in the yeast carrying the lysozyme expression plasmid in 9-fold greater secretion compared with the wild type [8].
  • These data suggest that the extensive glycosylation of yeast APase, which contains eight polymannose substituents, is not essential for secretion and expression of enzymatic activity of the transfected gene product [9].
  • Of the receptor sites for concanavalin A, 60-70% were subject to hydrolysis by endoglycosidase H indicating that the lectin reacts primarily with polymannose asparagine linked oligosaccharides [10].
 

Anatomical context of D-mannose

  • Release of glucose-containing polymannose oligosaccharides during glycoprotein biosynthesis. Studies with thyroid microsomal enzymes and slices [11].
  • To gain an understanding of why the polymannose-type oligosaccharide chain of bovine pancreatic ribonuclease B is not processed to a complex-type chain in vivo, the processing of this glycoprotein was studied in two cell-free systems [12].
  • Our investigations indicated that a peptide:N-glycanase (PNGase) is present in ER membranes that has the capacity to release from radiolabelled glycopeptides glucosylated as well as non-glucosylated polymannose oligosaccharides terminating at their reducing end in a di-N-acetylchitobiose sequence (OS-GlcNAc2) [13].
  • Oligosaccharides of the polymannose-type are also exported from the endoplasmic reticulum of mammalian cells to the cytosol in an ATP-dependent fashion [14].
  • Mannan, a polymannose carbohydrate isolated from the cell wall of yeast, is an appropriate and effective protein carrier for eliciting a cellular (T1-type) or humoral (T2-type) immune response depending on the mode of conjugation (oxidized or reduced) [15].
 

Associations of D-mannose with other chemical compounds

  • Since Man9GlcNAc was almost completely absent and the Man8GlcNAc isomer was shown to be identical with that formed by the in vitro action of endomannosidase on glucosylated polymannose oligosaccharides, we concluded that this enzyme was actively functioning in the intact cells and could provide a pathway for circumventing the glucosidase blockade [16].
 

Gene context of D-mannose

  • The Saccharomyces cerevisiae OCH1 gene encodes an alpha-1,6-mannosyltransferase that initiates the polymannose outer chain elongation of N-linked glycans [17].
  • Mucins (MUC1) have attracted interest as potential targets for immunotherapy of cancers of breast, pancreas, ovary and others, and we have demonstrated that mannan, a polymannose carbohydrate is an effective carrier for MUC1 in eliciting a cellular immune response [18].
  • Structural studies on N-linked oligosaccharides from gms1 mutant cells showed that the number of alpha-1,2-linked galactose residues wes markedly reduced, and unsubstituted alpha-1,6-linked polymannose outer chains were attached to the core oligosaccharides [19].
  • We conclude that the reversible preadsorption to the O8 and O9 polymannose antigens increases the rate of infection via the cellular receptor protein encoded by the fhuA (formerly tonA) gene [20].
  • Although optimal binding occurred with Glc1Man9GlcNAc, substantial interaction with calreticulin was retained after sequential trimming of the polymannose portion down to the Glc1Man5GlcNAc stage [21].
 

Analytical, diagnostic and therapeutic context of D-mannose

  • In contrast to strain X2180, invertase from the mnn9 mutant, which makes mannoprotein lacking the outer portion of the polymannose chains, shows only two major bands on isoelectric focusing [22].
  • The results of peptide mapping also supported the conclusion that the 160- to 170-kDa glycoproteins from the four echinoids are structurally homologous glycoproteins containing N-linked polymannose chains [23].

References

  1. Transfer of free polymannose-type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HepG2 cells. Saint-Pol, A., Bauvy, C., Codogno, P., Moore, S.E. J. Cell Biol. (1997) [Pubmed]
  2. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. Clarke, B.R., Cuthbertson, L., Whitfield, C. J. Biol. Chem. (2004) [Pubmed]
  3. Release of polymannose oligosaccharides from vesicular stomatitis virus G protein during endoplasmic reticulum-associated degradation. Spiro, M.J., Spiro, R.G. Glycobiology (2001) [Pubmed]
  4. Complement system is involved in anaphylactoid reaction induced by lipopolysaccharides in muramyldipeptide-treated mice. Kawabata, Y., Yang, T.S., Yokochi, T.T., Matsushita, M., Fujita, T., Shibazaki, M., Noikura, T., Endo, T.Y., Takada, H. Shock (2000) [Pubmed]
  5. Analysis of the carbohydrate composition of axonally transported glycoconjugates in sciatic nerve. Hart, C.E., Wood, J.G. J. Neurosci. (1986) [Pubmed]
  6. Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradation. Movsichoff, F., Castro, O.A., Parodi, A.J. Mol. Biol. Cell (2005) [Pubmed]
  7. Cytosol-to-lysosome transport of free polymannose-type oligosaccharides. Kinetic and specificity studies using rat liver lysosomes. Saint-Pol, A., Codogno, P., Moore, S.E. J. Biol. Chem. (1999) [Pubmed]
  8. Hyperglycosylation of hen egg white lysozyme in yeast. Nakamura, S., Takasaki, H., Kobayashi, K., Kato, A. J. Biol. Chem. (1993) [Pubmed]
  9. Expression, glycosylation and secretion of yeast acid phosphatase in hamster BHK cells. Reljic, R., Barbaric, S., Ries, B., Buxton, R., Hughes, R.C. Glycoconj. J. (1992) [Pubmed]
  10. Subcellular distribution and partial characterization of the three major classes of concanavalin A receptors associated with rat brain synaptic junctions. Gurd, J.W. Can. J. Biochem. (1980) [Pubmed]
  11. Release of glucose-containing polymannose oligosaccharides during glycoprotein biosynthesis. Studies with thyroid microsomal enzymes and slices. Anumula, K.R., Spiro, R.G. J. Biol. Chem. (1983) [Pubmed]
  12. Control of asparagine-linked oligosaccharide chain processing: studies on bovine pancreatic ribonuclease B. An in vitro system for the processing of exogenous glycoproteins. Williams, D.B., Lennarz, W.J. J. Biol. Chem. (1984) [Pubmed]
  13. Demonstration of a peptide:N-glycosidase in the endoplasmic reticulum of rat liver. Weng, S., Spiro, R.G. Biochem. J. (1997) [Pubmed]
  14. Glycopeptide export from mammalian microsomes is independent of calcium and is distinct from oligosaccharide export. Ali, B.R., Field, M.C. Glycobiology (2000) [Pubmed]
  15. Breast cancer immunotherapy: current status and future prospects. Apostolopoulos, V., McKenzie, I.F., Pietersz, G.A. Immunol. Cell Biol. (1996) [Pubmed]
  16. Demonstration that Golgi endo-alpha-D-mannosidase provides a glucosidase-independent pathway for the formation of complex N-linked oligosaccharides of glycoproteins. Moore, S.E., Spiro, R.G. J. Biol. Chem. (1990) [Pubmed]
  17. Cdc4 is involved in the transcriptional control of OCH1, a gene encoding alpha-1,6-mannosyltransferase in Saccharomyces cerevisiae. Cui, Z., Horecka, J., Jigami, Y. Yeast (2002) [Pubmed]
  18. MUC1 and breast cancer. Apostolopoulos, V., Pietersz, G.A., McKenzie, I.F. Curr. Opin. Mol. Ther. (1999) [Pubmed]
  19. Isolation and characterization of a glycosylation mutant from Schizosaccharomyces pombe. Takegawa, K., Tanaka, N., Tabuchi, M., Iwahara, S. Biosci. Biotechnol. Biochem. (1996) [Pubmed]
  20. Polymannose O-antigens of Escherichia coli, the binding sites for the reversible adsorption of bacteriophage T5+ via the L-shaped tail fibers. Heller, K., Braun, V. J. Virol. (1982) [Pubmed]
  21. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. Spiro, R.G., Zhu, Q., Bhoyroo, V., Söling, H.D. J. Biol. Chem. (1996) [Pubmed]
  22. Yeast invertase polymorphism is correlated with variable states of oligosaccharide chain phosphorylation. Frevert, J., Ballou, C.E. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  23. Structure of a major yolk glycoprotein and its processing pathway by limited proteolysis are conserved in echinoids. Scott, L.B., Lennarz, W.J. Dev. Biol. (1989) [Pubmed]
 
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