Detail of "51023-76-8"

Reference

Anion transport inhibitors: effects on water and sodium transport in the toad urinary bladder

Anion transport inhibitors: effects on water and sodium transport in the toad urinary bladder. Brem, Andrew S.; Eich, Elizabeth; Pearl, Mirilee; Taylor, Ann (Med. Coll., Cornell Univ., New York, NY 10021, USA). Am. J. Physiol., 248(4, Pt. 2), F594-F601 (English) 1985. CODEN: AJPHAP. ISSN: 0002-9513. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Acidification of the medium bathing the serosal surface of the toad urinary bladder impaired the water permeability response to vasopressin [11000-17-2]. The magnitude of the hydrosmotic response to a maximal concn. of either vasopressin or the cyclic nucleotide analog 8-(p-chlorophenylthio)-cAMP (ClPhS-cAMP) [41941-66-6] was progressively reduced when serosal bath pH was decreased from 8.5 to 6.5. The disulfonic stilbenes SITS [51023-76-8] and DIDS [53005-05-3] and the diuretic furosemide [54-31-9], agents known to interfere with anion transport and with the regulation of intracellular pH in other tissues, inhibited the water flow response to vasopressin and ClPhS-cAMP in a pH-dependent manner when added to the serosal bathing medium. Inhibition of the hydrosmotic response to 10-5 M ClPhS-cAMP was estd. to be half-maximal at 1.5 ′ 10-4 M SITS, 2 ′ 10-5 M DIDS, and 1 ′ 10-5 M furosemide. The degree of inhibition induced by the anion transport inhibitors varied inversely with the concn. of exogenous cyclic nucleotide. SITS, DIDS, and furosemide had no effect on either basal or vasopressin-stimulated short-circuit current at serosal pH 8.5; all 3 agents inhibited basal short-circuit at pH 7.1 but had no effect on the natriferic response to vasopressin. Evidently, changes in intracellular H+ and(or) anion concn. can selectively inhibit the increase in water permeability elicited by vasopressin at a step(s) distal to the generation of cAMP.

Entry of diphtheria toxin linked to concanavalin A into primate and murine cells

Entry of diphtheria toxin linked to concanavalin A into primate and murine cells. Guillemot, Jean Claude; Sundan, Anders; Olsnes, Sjur; Sandvig, Kirsten (Norsk Hydro's Inst. Cancer Res., Oslo, Norway). J. Cell. Physiol., 122(2), 193-9 (English) 1985. CODEN: JCLLAX. ISSN: 0021-9541. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Diphtheria toxin linked by a disulfide bridge to concanavalin A was highly toxic to HeLa S3 and Vero cells, as well as to murine L cells. The cells could be protected with a-Me mannoside [27939-30-6], indicating that the conjugate binds mainly through its concanavalin A moiety. Treatment of Vero cells with phospholipase C [9001-86-9], TPA [16561-29-8], and vanadate, which strongly reduce the ability of the cells to bind free diphtheria toxin, had little protective effect against the conjugate, whereas SITS [51023-76-8], which inhibits diphtheria toxin binding, as well as the subsequent entry, protected Vero cells, but not L cells. Both types of cells are protected against the conjugate by NH4Cl and monensin [17090-79-8], indicating that an acidified compartment is necessary for entry into the cytosol. Exposure of cells, bound with surface conjugate, to low pH induced entry of the toxin into Vero cells, but not into L cells. Phospholipase C, TPA, and vanadate did not protect L cells against the conjugate. Thus, toxin in the conjugate enters L cells by a route which involves low pH, but which is not identical to that in Vero cells.