Disease relevance of monensin

• Moreover, immunotoxin plus 0.1 microM liposomal monensin was fivefold more toxic for H-MESO-1 cells and 1000-fold and 2200-fold more toxic for human glioblastoma U373 and U87 cells, respectively, than immunotoxin plus 0.1 microM free monensin in buffer [1].
• Inhibition of [3H]leucine incorporation was used to evaluate the cytotoxic action of immunotoxin with or without monensin in vitro on the following human tumor cell lines: H-MESO-1 malignant mesothelioma, LS174T colorectal carcinoma, and U373, U87, and MG-1 glioblastomas [1].
• Monensin-treated influenza virus-infected MDCK cells also contain dilated cytoplasmic vesicles, but virus particles were not found in these structures, and numerous influenza virions were observed budding at the cell surface [2].
• In BHK21 cells, monensin also inhibits VSV production, but influenza virus is also sensitive to the ionophore [2].
• Monensin-resistant mouse Balb/3T3 cell mutant with aberrant penetration of vesicular stomatitis virus [3].

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

• These results indicate that influenza virus glycoprotein transport is not blocked by monensin treatment, whereas there is a block in transport of VSV G protein [2].
• The carboxylic ionophores monensin and nigericin, at concentrations higher than 10 and 6 muM, respectively, prevent the penetration of the Semliki Forest virus (SFV) genome into the cytosol of baby hamster kidney (BHK-21) cells and thereby inhibit viral replication [9].
• Processing of the structural proteins of human immunodeficiency virus type 1 in the presence of monensin and cerulenin [10].
• In this report we demonstrate that the lysosomotropic agent ammonium chloride and the carboxylic ionophore monensin substantially potentiate the cytotoxicity of anti-TAC-A on HUT 102 cells, a long-term cultured HTLV-I infected T-cell line [11].
• Relations between intracellular ions and energy metabolism: a study with monensin in synaptosomes, neurons, and C6 glioma cells [12].

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

• In the presence of monensin (an inhibitor of protein secretion), the cells secrete cholesterol, but little apolipoprotein E [20].
• Similar potentiation of the cytotoxicity of anti-CEA immunotoxins was produced by monensin and nigericin [21].
• (i) The cyclooxygenase inhibitor indomethacin partially removed the inhibition produced by deletion of serosal Na+ and almost completely impeded the inhibitions produced by either monensin or A23187 [22].
• In the absence of FMLP, a rise in pHi to 7.7-7.8 by exposure of cells to 30 mM NH4Cl, 10 microM monensin (a Na/H exchanging ionophore), or after a prepulse with 18% CO2 did not result in O2- generation [23].
• Ouabain and monensin caused nearly identical changes to IFN-gamma [24].

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

• In mice, liposomal monensin in combination with specific immunotoxin substantially prolonged survival, and three (21%) of 14 mice bearing H-MESO-1 xenografts treated with the liposomes showed no evidence of tumor at day 160 after treatment [1].
• The distribution of these proteins in control and inhibited (5 x 10(-7) M monensin) cells has been studied by immunofluorescence microscopy [30].
• Dissection of the Golgi complex. II. Density separation of specific Golgi functions in virally infected cells treated with monensin [31].
• Combined cell fractionation and autoradiographic studies of the pancreas show that the effect of monensin is exerted at the point of the exit of secretory protein from the Golgi apparatus [32].
• Quantitative analyses of 48 individual fast-transported protein species, after separation by two-dimensional gel electrophoresis, revealed that monensin depresses all proteins to a similar extent [33].

References