The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

monensin     4-[2-[5-ethyl-5-[5-[6- hydroxy-6...

Synonyms: monensin A, AGN-PC-00GH0Z, NSC-343257, AKOS015842889, FT-0601610, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of monensin


Psychiatry related information on monensin

  • Clinical signs of monensin toxicosis, including lethargy and recumbency, appeared on day 2 in the calves given the Se-E pretreatment, compared with the onset on day 1 in the saline solution-pretreated calves [4].
  • Interaction between bunk management and monensin concentration on finishing performance, feeding behavior, and ruminal metabolism during an acidosis challenge with feedlot cattle [5].

High impact information on monensin

  • Both EGF-Rs internalized rapidly, but kinase-negative receptor was surface down-regulated only with monensin or at 20 degrees C. Furthermore, EGF internalized by mutant receptor alone was, in significant proportion, returned to the cell surface undegraded [6].
  • When the intracellular transit of 3H-labeled (pro)-insulin polypeptides is perturbed by monensin in the pancreatic B-cell, proinsulin conversion is impaired and the radioactive peptides accumulate in a clathrin-coated membrane compartment related to the Golgi apparatus [7].
  • The coated compartment, which is dilated by monensin, comprises Golgi cisternae with condensing secretory material and newly formed secretory granules; under monensin block, the noncoated (storage) secretory granules do not become significantly labeled [7].
  • A clathrin-coated, Golgi-related compartment of the insulin secreting cell accumulates proinsulin in the presence of monensin [7].
  • The addition of O-linked oligosaccharides did not occur in cells treated with the ionophore monensin or in a ricin-resistant cell line defective in the processing of N-linked oligosaccharides [8].

Chemical compound and disease context of monensin


Biological context of monensin

  • Treatment with monensin caused accumulation in the cell of a form of G1 with partial sensitivity toward endo H, suggesting that monensin may act to inhibit the glycosylation process directly [13].
  • Rearrangement of cytoplasm, fusion of membranous organelles with the plasma membrane and growth of pseudopodia, all characteristic of in vivo spermiogenesis, occur within five minutes after exposure to monensin at concentrations of 0.1-1.0 micronM [14].
  • C6-NBD-ceramide was used to observe the morphology of the Golgi apparatus in living cells in the presence or absence of monensin or Colcemid, and during mitosis [15].
  • Analyzing the degree of receptor association of intracellular ligand revealed that monensin prevents the dissociation of the receptor-ligand complex that normally occurs subsequent to endocytosis [16].
  • In contrast, monensin only slightly delays the transport of newly synthesized beta-glucuronidase to lysosomes and causes no significant alteration in the extent of oligosaccharide phosphorylation, a process that appears to occur in the early (cis) Golgi complex [17].

Anatomical context of monensin

  • Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts [18].
  • The receptors that left the surface were trapped intracellularly within perinuclear vacuoles, as visualized by indirect immunofluorescence with the use of LDL, monensin caused about 50% of the receptors to be trapped intracellularly within 15 min [18].
  • Monensin-activated spermatozoa have normal morphology and normal amoeboid motility [14].
  • Vesicle fusion, pseudopod extension and amoeboid motility are induced in nematode spermatids by the ionophore monensin [14].
  • However, it has recently been reported that monensin-treated human embryonal fibroblasts attached and spread onto glass substrata to the same extent as untreated cells, although at later stages they fail to develop focal adhesion sites [19].

Associations of monensin with other chemical compounds


Gene context of monensin

  • In fact, when the cells were incubated in the presence of monensin during the adhesion assay, they still adhered but spreading did not occur, focal adhesions disappeared and BSP, OPN, and FN were accumulated in intracellular granules [25].
  • As assessed by monensin treatment and cell surface biotinylation, the internalization rate of PEST sequence-deleted ABCA1 (ABCA1-dPEST) was markedly decreased compared with wild-type ABCA1 (ABCA1-wt) [26].
  • NCX1 immunoreactivity was detectable in HEK293 as well as in TRPC3-overexpressing HEK293 cells, and reduction of extracellular Na(+) after Na(+) loading with monensin resulted in significant rises in intracellular free Ca(2+) (Ca(2+)(i)) of HEK293 cells [27].
  • Signaling does not occur in the presence of brefeldin A; instead, STAT1 is activated when protein secretion is blocked with monensin, suggesting that the hypochondroplasia receptor signals at the exit from the ER [28].
  • The focal clustering of beta 1 was impaired by monensin treatment, indicating that endogenous FN secretion was required to drive beta 1 into focal contacts [29].

Analytical, diagnostic and therapeutic context of monensin


  1. Potentiation of antitumor immunotoxins by liposomal monensin. Griffin, T., Rybak, M.E., Recht, L., Singh, M., Salimi, A., Raso, V. J. Natl. Cancer Inst. (1993) [Pubmed]
  2. Differential effect of monensin on enveloped viruses that form at distinct plasma membrane domains. Alonso, F.V., Compans, R.W. J. Cell Biol. (1981) [Pubmed]
  3. Monensin-resistant mouse Balb/3T3 cell mutant with aberrant penetration of vesicular stomatitis virus. Ono, M., Mifune, K., Yoshimura, A., Ohnishi, S., Kuwano, M. J. Cell Biol. (1985) [Pubmed]
  4. Effect of pretreatment with selenium-vitamin E on monensin toxicosis in cattle. Van Vleet, J.F., Amstutz, H.E., Rebar, A.H. Am. J. Vet. Res. (1985) [Pubmed]
  5. Interaction between bunk management and monensin concentration on finishing performance, feeding behavior, and ruminal metabolism during an acidosis challenge with feedlot cattle. Erickson, G.E., Milton, C.T., Fanning, K.C., Cooper, R.J., Swingle, R.S., Parrott, J.C., Vogel, G., Klopfenstein, T.J. J. Anim. Sci. (2003) [Pubmed]
  6. Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body. Felder, S., Miller, K., Moehren, G., Ullrich, A., Schlessinger, J., Hopkins, C.R. Cell (1990) [Pubmed]
  7. A clathrin-coated, Golgi-related compartment of the insulin secreting cell accumulates proinsulin in the presence of monensin. Orci, L., Halban, P., Amherdt, M., Ravazzola, M., Vassalli, J.D., Perrelet, A. Cell (1984) [Pubmed]
  8. O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. Johnson, D.C., Spear, P.G. Cell (1983) [Pubmed]
  9. Monensin inhibits Semliki Forest virus penetration into culture cells. Marsh, M., Wellsteed, J., Kern, H., Harms, E., Helenius, A. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  10. Processing of the structural proteins of human immunodeficiency virus type 1 in the presence of monensin and cerulenin. Pal, R., Gallo, R.C., Sarngadharan, M.G. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  11. Selective killing of human T-lymphotropic virus-I infected leukemic T-cells by monoclonal anti-interleukin 2 receptor antibody-ricin A chain conjugates: potentiation by ammonium chloride and monensin. Krönke, M., Schlick, E., Waldmann, T.A., Vitetta, E.S., Greene, W.C. Cancer Res. (1986) [Pubmed]
  12. Relations between intracellular ions and energy metabolism: a study with monensin in synaptosomes, neurons, and C6 glioma cells. Erecińska, M., Dagani, F., Nelson, D., Deas, J., Silver, I.A. J. Neurosci. (1991) [Pubmed]
  13. A membrane glycoprotein that accumulates intracellularly: cellular processing of the large glycoprotein of LaCrosse virus. Madoff, D.H., Lenard, J. Cell (1982) [Pubmed]
  14. Vesicle fusion, pseudopod extension and amoeboid motility are induced in nematode spermatids by the ionophore monensin. Nelson, G.A., Ward, S. Cell (1980) [Pubmed]
  15. A vital stain for the Golgi apparatus. Lipsky, N.G., Pagano, R.E. Science (1985) [Pubmed]
  16. Monensin inhibits intracellular dissociation of asialoglycoproteins from their receptor. Harford, J., Wolkoff, A.W., Ashwell, G., Klausner, R.D. J. Cell Biol. (1983) [Pubmed]
  17. Targeting of beta-glucuronidase to lysosomes in mannose 6-phosphate receptor-deficient MOPC 315 cells. Gabel, C.A., Kornfeld, S. J. Cell Biol. (1984) [Pubmed]
  18. Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts. Basu, S.K., Goldstein, J.L., Anderson, R.G., Brown, M.S. Cell (1981) [Pubmed]
  19. Monensin inhibits initial spreading of cultured human fibroblasts. Pizzey, J.A., Bennett, F.A., Jones, G.E. Nature (1983) [Pubmed]
  20. Independent pathways for secretion of cholesterol and apolipoprotein E by macrophages. Basu, S.K., Goldstein, J.L., Brown, M.S. Science (1983) [Pubmed]
  21. Enhancement of the cytotoxic effect of anti-carcinoembryonic antigen immunotoxins by adenovirus and carboxylic ionophores. Griffin, T.W., Childs, L.R., FitzGerald, D.J., Levin, L.V. J. Natl. Cancer Inst. (1987) [Pubmed]
  22. Roles of Ca2+ and Na+ on the modulation of antidiuretic hormone action on urea permeability in toad urinary bladder. Hardy, M.A., Ware, H.M. J. Clin. Invest. (1985) [Pubmed]
  23. Intracellular pH modulates the generation of superoxide radicals by human neutrophils. Simchowitz, L. J. Clin. Invest. (1985) [Pubmed]
  24. Inhibition of Na+,K+-ATPase by interferon gamma down-regulates intestinal epithelial transport and barrier function. Sugi, K., Musch, M.W., Field, M., Chang, E.B. Gastroenterology (2001) [Pubmed]
  25. Osteocalcin induces chemotaxis, secretion of matrix proteins, and calcium-mediated intracellular signaling in human osteoclast-like cells. Chenu, C., Colucci, S., Grano, M., Zigrino, P., Barattolo, R., Zambonin, G., Baldini, N., Vergnaud, P., Delmas, P.D., Zallone, A.Z. J. Cell Biol. (1994) [Pubmed]
  26. A PEST deletion mutant of ABCA1 shows impaired internalization and defective cholesterol efflux from late endosomes. Chen, W., Wang, N., Tall, A.R. J. Biol. Chem. (2005) [Pubmed]
  27. Ca(2+) signaling by TRPC3 involves Na(+) entry and local coupling to the Na(+)/Ca(2+) exchanger. Rosker, C., Graziani, A., Lukas, M., Eder, P., Zhu, M.X., Romanin, C., Groschner, K. J. Biol. Chem. (2004) [Pubmed]
  28. The kinase activity of fibroblast growth factor receptor 3 with activation loop mutations affects receptor trafficking and signaling. Lievens, P.M., Mutinelli, C., Baynes, D., Liboi, E. J. Biol. Chem. (2004) [Pubmed]
  29. Adhesion properties and integrin expression of cultured human osteoclast-like cells. Grano, M., Zigrino, P., Colucci, S., Zambonin, G., Trusolino, L., Serra, M., Baldini, N., Teti, A., Marchisio, P.C., Zallone, A.Z. Exp. Cell Res. (1994) [Pubmed]
  30. Immunocytochemical localization of procollagen and fibronectin in human fibroblasts: effects of the monovalent ionophore, monensin. Ledger, P.W., Uchida, N., Tanzer, M.L. J. Cell Biol. (1980) [Pubmed]
  31. Dissection of the Golgi complex. II. Density separation of specific Golgi functions in virally infected cells treated with monensin. Quinn, P., Griffiths, G., Warren, G. J. Cell Biol. (1983) [Pubmed]
  32. Comparative studies of intracellular transport of secretory proteins. Tartakoff, A., Vassalli, P., Détraz, M. J. Cell Biol. (1978) [Pubmed]
  33. Evidence that all newly synthesized proteins destined for fast axonal transport pass through the Golgi apparatus. Hammerschlag, R., Stone, G.C., Bolen, F.A., Lindsey, J.D., Ellisman, M.H. J. Cell Biol. (1982) [Pubmed]
WikiGenes - Universities