{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,19]],"date-time":"2026-02-19T03:58:15Z","timestamp":1771473495950,"version":"3.50.1"},"reference-count":19,"publisher":"American Physiological Society","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[2004,4]]},"abstract":"<jats:p> Here we describe the effect of colistin on the barrier function of the mammalian urinary bladder epithelium. Addition of colistin to the mucosal solution of the rabbit urinary bladder epithelium (urothelium) resulted in an increase in the transepithelial conductance. The magnitude of the increase in transepithelial conductance was dependent on the membrane voltage, concentration of colistin, and presence of divalent cations in the bath solution. The initial site of action of colistin was at the apical membrane. Colistin increased the membrane conductance only when the apical membrane potential was cell interior negative. The more negative the membrane potential, the larger the conductance increase. The concentration dependence of the conductance increase saturated, suggesting a membrane binding site. Divalent cations decreased the magnitude of the conductance increase. This divalent cation action occurred at two sites: one in competition with colistin for a membrane binding site, and the other by rapidly blocking the induced conductance. At short exposure times, the increase in conductance was reversed by either removing colistin from the bath or changing the voltage so that the apical membrane was cell interior positive. At long exposure times, the increase was only partially reversible by voltage or removal from the bath. This finding suggests that at long exposure times, there is a toxic effect of colistin on the urothelium. <\/jats:p>","DOI":"10.1152\/ajpcell.00437.2003","type":"journal-article","created":{"date-parts":[[2004,3,4]],"date-time":"2004-03-04T18:07:45Z","timestamp":1078423665000},"page":"C913-C922","source":"Crossref","is-referenced-by-count":45,"title":["Colistin interactions with the mammalian urothelium"],"prefix":"10.1152","volume":"286","author":[{"given":"Jamie R.","family":"Lewis","sequence":"first","affiliation":[{"name":"Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-0641"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Simon A.","family":"Lewis","sequence":"additional","affiliation":[{"name":"Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-0641"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","reference":[{"key":"REF1","doi-asserted-by":"crossref","unstructured":"Berg JR, Spilker CM, and Lewis SA. Effects of polymyxin B on mammalian urinary bladder. J Membr Biol 154: 119\u2013130, 1996.","DOI":"10.1007\/s002329900137"},{"key":"REF2","doi-asserted-by":"crossref","unstructured":"Berg JR, Spilker CM, and Lewis SA. Modulation of polymyxin B effects on mammalian urinary bladder. Am J Physiol Renal Physiol 275: F204\u2013F215, 1998.","DOI":"10.1152\/ajprenal.1998.275.2.F204"},{"key":"REF3","doi-asserted-by":"crossref","unstructured":"Chihara S, Tobita T, Yahara M, Ito A, and Koyoma Y. Enzymatic degradation of colistin isolation and identification of \u03b1-N-acyl \u03b1,\u03b3-diaminobutyric acid and colistin nonapeptide. Agric Biol Chem 37: 2455\u20132463, 1973.","DOI":"10.1271\/bbb1961.37.2455"},{"key":"REF4","doi-asserted-by":"crossref","unstructured":"Conway SP, Pond MN, Watson A, Etherington C, Robey HL, and Goldman MH. Intravenous colistin sulphomethate in acute respiratory exacerbations in adult patients with cystic fibrosis. Thorax 52: 987\u2013993, 1997.","DOI":"10.1136\/thx.52.11.987"},{"key":"REF5","doi-asserted-by":"crossref","unstructured":"Eickhoff TC and Finland M. Polymyxin B and Colistin. Am J Med Sci 249: 172\u2013174, 1965.","DOI":"10.1097\/00000441-196502000-00005"},{"key":"REF6","doi-asserted-by":"crossref","unstructured":"Hausmann W and Craig LC. Polymyxin B fractionation, molecular weight determination, amino acid and fatty acid composition. J Am Chem Soc 76: 4802\u20134896, 1954.","DOI":"10.1021\/ja01648a039"},{"key":"REF7","doi-asserted-by":"crossref","unstructured":"Lewis SA, Eaton DC, Clausen C, and Diamond J. Nystatin as a probe for investigating the electrical properties of a tight epithelium. J Gen Physiol 70: 427\u2013440, 1977.","DOI":"10.1085\/jgp.70.4.427"},{"key":"REF8","unstructured":"Lewis SA and Wills NK. Applications and interpretations of ion-specific microelectrodes in tight epithelia. In: The Application of Ion-Selective Microelectrodes, edited by Zeuthen T. Amsterdam, The Netherlands: Elsevier Science, 1981, p. 3\u201325."},{"key":"REF9","doi-asserted-by":"crossref","unstructured":"Lewis SA, Wills NK, and Eaton DC. Basolateral membrane potential of a tight epithelium: ionic diffusion and electrogenic pumps. J Membr Biol 41: 117\u2013148, 1978.","DOI":"10.1007\/BF01972629"},{"key":"REF10","doi-asserted-by":"crossref","unstructured":"Nord NM and Hoeprich PD. Polymyxin B and Colistin. N Engl J Med 270: 1030\u20131035, 1964.","DOI":"10.1056\/NEJM196405142702002"},{"key":"REF11","doi-asserted-by":"crossref","unstructured":"Pristovsek P and Kidric J. Solution structure of polymyxins B and E and effect of binding to lipopolysaccharide: an NMR and molecular modeling study. J Med Chem 42: 4604\u20134613, 1999.","DOI":"10.1021\/jm991031b"},{"key":"REF12","doi-asserted-by":"crossref","unstructured":"Storm DR, Rosenthal KS, and Swanson PE. Polymyxin and related peptide antibiotics. Annu Rev Biochem 46: 723\u2013763, 1977.","DOI":"10.1146\/annurev.bi.46.070177.003451"},{"key":"REF13","doi-asserted-by":"crossref","unstructured":"Tsubery H, Ofek I, Cohen S, Eisenstein M, and Fridkin M. Modulation of the hydrophobic domain of polymyxin B nonapeptide: effect on outer-membrane permeabilization and lipopolysaccharide neutralization. Mol Pharmacol 62: 1036\u20131042, 2002.","DOI":"10.1124\/mol.62.5.1036"},{"key":"REF14","doi-asserted-by":"crossref","unstructured":"Tsubery H, Ofek I, Cohen S, and Fridkin M. Structure-function studies of polymyxin B nonapeptide: implications to sensitization of gram negative bacteria. J Med Chem 43: 3085\u20133092, 2000.","DOI":"10.1021\/jm0000057"},{"key":"REF15","doi-asserted-by":"crossref","unstructured":"Tzan CJ, Berg JR, and Lewis SA. Effect of protamine sulfate on the permeability properties of the mammalian urinary bladder. J Membr Biol 133: 227\u2013242, 1993.","DOI":"10.1007\/BF00232022"},{"key":"REF16","doi-asserted-by":"crossref","unstructured":"Tzan CJ, Berg JR, and Lewis SA. Modification of epithelial permeability by cationic polypeptides. Am J Physiol Cell Physiol 265: C1637\u2013C1647, 1993.","DOI":"10.1152\/ajpcell.1993.265.6.C1637"},{"key":"REF17","doi-asserted-by":"crossref","unstructured":"Vaara M. Agents that increase the permeability of the outer membrane. Microbiol Rev 56: 395\u2013411, 1992.","DOI":"10.1128\/mr.56.3.395-411.1992"},{"key":"REF18","doi-asserted-by":"crossref","unstructured":"Viljanen P, Matsunaga H, Kimura Y, and Vaara M. The outer membrane permeability-increasing action of deacylpolymyxins. J Antibiot (Tokyo) 44: 517\u2013523, 1991.","DOI":"10.7164\/antibiotics.44.517"},{"key":"REF19","doi-asserted-by":"crossref","unstructured":"Yonath J and Civan MM. Determination of the driving force of the Na+ pump in toad bladder by means of vasopressin. J Membr Biol 5: 366\u2013385, 1971.","DOI":"10.1007\/BF01957352"}],"container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.00437.2003","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T18:46:15Z","timestamp":1718649975000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.00437.2003"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,4]]},"references-count":19,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2004,4]]}},"alternative-id":["10.1152\/ajpcell.00437.2003"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.00437.2003","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[2004,4]]}}}