Disease relevance of Octoxinol

• In contrast, OTC vaginal cleansing and contraceptive films containing octoxynol-9 or nonoxynol-9 (N-9) demonstrated similar levels of toxicity but distinct immunoinflammatory profiles [1].
• Triton-X-100-treated pilus suspensions prepared from Neisseria gonorrhoeae produced a single line of precipitate in immunodiffusion tests [2].
• Treatment of virions with 2% Triton-X 100 under alkaline conditions in the absence or presence of 2 M-KCl solubilized the two glycoproteins and a fraction of the 71 and 44 K polypeptides, but not the 73 and 47 K polypeptides [3].
• We found that ganglioside GM1, integrin subunits alpha2 and beta3, and the heat shock cognate protein 70 (hsc70), all of which have been implicated as rotavirus receptors, are associated with TX-100 and Lubrol WX detergent-resistant membranes (DRMs) [4].
• A cytochrome c (cyt. c) was solubilized with Triton-X-100 and co-purified with cytochrome c oxidase from membranes of chemotrophically grown cells of Rhodopseudomonas capsulata [5].

High impact information on Octoxinol

• Chilled platelets show an increase in the amount of myosin in the Triton-X insoluble residue or 'cytoskeleton' which is correlated in time both with phosphorylation of the myosin regulatory light chain and with the induced shape change [6].
• Many trophozoite-target interfaces were outlined with a ring of polymerized amoeba actin, revealed by rhodamine-phalloidin staining of glutaraldehyde-fixed and Triton-X 100-extracted cells [7].
• Subsequent analyses showed that the subpool of CD73 released by TX-100 at 4 degrees C was not truly solubilized, but rather represented TX-100-induced release of CD73-containing membrane fragments [8].
• During ATP depletion, total cellular Na+,K(+)-ATPase activity was unaltered, but the Triton-X-100-insoluble fraction (cytoskeleton associated) of Na+,K(+)-ATPase activity decreased (P less than 0.01), with a corresponding increase in the detergent-soluble fraction of Na+,K(+)-ATPase (P less than 0.01) [9].
• Confocal microscopy demonstrated that the TX-insoluble compartment is perinuclear and co-localizes with endoplasmic reticulum (ER) markers [10].

Chemical compound and disease context of Octoxinol

• Using recombinant vaccinia viruses that express Sendai virus HN, F, or M protein individually, we observed that each viral protein (F, HN, or M) was independently capable of acquiring TX-100 insolubility in the absence of other viral components [11].
• The immunogenicity of zwitterionic detergent-disrupted influenza virus vaccine preparations, intact virus vaccine and vaccine preparations obtained by treatment of the intact virus with Triton-X 100 or cetyl trimethyl ammonium bromide (CTAB) was studied in hamsters and mice [12].
• Salting out by dehydration in competition with octoxynol 9 for the available water was observed with sulfate and phosphate anions, sodium, potassium, and ammonium tribasications, and the nonelectrolyte sorbitol [13].
• Interactions of M1 protein with HA or NA, the influenza virus envelope glycoproteins, were investigated by TX-100 detergent treatment of membrane fractions and floatation in sucrose gradients [14].
• The effect of surfactants on the biodegradation of trifluralin and atrazine (by Streptomyces PS1/5) and coumaphos (by degrading consortia from a contaminated cattle dip) in liquid cultures and soil slurries was tested at different concentrations of a rhamnolipid mixture (Rh-mix) and Triton X-100 (TX-100) [15].

Biological context of Octoxinol

• Together, these data imply that CD20 can evoke apoptosis without the involvement of mitochondria and caspases and irrespective of redistribution into TX-100 insoluble membrane rafts [16].
• Using Triton X-100 (TX-100) as a representative HA, we found that the mtrCDE efflux pump operon could be induced to higher levels of expression when an HA-sensitive strain was exposed to sublethal concentrations of this non-ionic detergent and the structurally related spermicide, nonoxynol-9 [17].
• The highest percentage of solubilized binding sites (45%) was obtained by treating brain membranes with 1% Triton-X-100 and 0.2% digitonin in 0.5 M potassium phosphate containing 20% glycerol [18].
• Biochemical and morphological examination of the TX-100 solubility of junctional E-cadherin and gamma-catenin in control and HGF treated cells showed an increase in solubility of only E-cadherin during loss of cell polarity [19].
• In particular, insertional mutagenesis of loop II prevented the insertion of the mutant protein into the plasma membrane of COS-7 cells and rendered it insoluble in TX-100 [20].

Anatomical context of Octoxinol

• Cells lacking CD45 showed identical phosphorylation of Lck in GEM and TX-100-soluble membranes [21].
• Approximately 50% of complexes were titrated into the TX-100-insoluble fraction coincident with the arrival of the complexes at the plasma membrane and the assembly of alpha-catenin [22].
• Three different in vitro preparations were used to nucleate the polymerization of muscle G-actin: (a) MV core fragments containing "barbed" and "pointed" filament ends exposed by shear during isolation, (b) isolated, membrane-intact brush borders, and (c) brush borders demembranated with Triton-X 100 [23].
• Here we show that incubation of chicken embryo erythroid cells in a medium in which arginine has been substituted by its amino acid analogue, canavanine, results in the inhibition of the posttranslational assembly of vimentin into the TX-100-insoluble filaments [24].
• The targeting differences for GSLs in FRT and MDCK cells cannot be accounted for by a differential ability to form clusters because, in spite of major differences in the GSL composition, both cell lines assembled GSLs into TX-100-insoluble complexes with identical isopycnic densities [25].

Associations of Octoxinol with other chemical compounds

• We analyzed the assembly of cadherin/catenin complexes in the TX-100-soluble fraction by [35S]methionine pulse-chase labeling, followed by sucrose density gradient fractionation of proteins [22].
• We here show that insolubility of NADPH oxidase subunits in nonionic detergents TX-100, Brij-58, and Brij-98 is a consequence of inclusion into cholesterol-enriched membrane microdomains (lipid rafts) [26].
• To compare the membrane-associated Lck present in the GEM and TX-100-soluble fractions of Jurkat cells, Lck from each fraction was immunoblotted with antibody to phosphotyrosine [21].
• The alpha-spectrin nascent polypeptide chains are released quantitatively from the TX-100 cytoskeleton by treatment of lysed cells with puromycin, suggesting that they themselves are not associated with the cytoskeleton [27].
• Merlin resists solubilization by the detergent Triton X-100 (TX-100), a property commonly attributed to association with the cytoskeleton [28].

Gene context of Octoxinol

• Extraction of transfected SW13Vim(-) cells with Triton-X-100-containing buffers showed that the mutant GFAP was more resistant to solubilization at elevated KCl concentrations [29].
• In cell fractionation of homogenized fly heads without monovalent cations, all dynamin was in pellet fractions and was minimally susceptible to Triton-X extraction [30].
• The bulk of apical CD73 ( approximately 60%) was released from the cell surface by treatment with 1% Triton X-100 (TX-100) at 4 degrees C, but such release was not affected by pretreatment with ligand or by prior, antibody-mediated cross-linking of CD73 [8].
• Accordingly, NF2 patient mutations that encode merlins with enhanced TX-100 solubility have been explained previously in terms of loss of cytoskeletal attachment [28].
• Membraneous P2X4 and P2X6 receptors resisted extraction with Triton-X 100, whereas cytoplasmic P2X receptors were Triton-X 100 soluble [31].

Analytical, diagnostic and therapeutic context of Octoxinol

• Western blots revealed the 08L antigen to be a protein, of M(r) approximately 140,000, found in the Triton-X 100 insoluble pellet [32].
• Immunoprecipitation and subsequent SDS gel electrophoresis showed that the synthesis of canavanine-vimentin is not inhibited and that it accumulates in the TX-100-soluble compartment [24].
• Analysis of these two fractions by two-dimensional gel electrophoresis after a short pulse-labeling period reveals that alpha-spectrin nascent polypeptides are present predominantly in the TX-100-insoluble fraction [27].
• The organization of the cytoskeleton was examined by fluorescent microscopy and by transmission electron microscopy, using immunogold tagging after Triton-X-100 (TX-100) extraction of the macrophages [33].
• Incorporation of radioactive phosphate into histone was assessed by SDS and acid/urea/Triton-X-100 (AUT) gel electrophoresis and radioautography [34].

References