Drugs online research references
Am J Physiol. 1989 Jul;257(1 Pt 1):G65-72.
Active transport of taurine in rabbit jejunal brush-border membrane vesicles.
Miyamoto Y, Tiruppathi C, Ganapathy V, Leibach FH.
Department of Cell and Molecular Biology, Medical College of Georgia, Augusta 30912-2100.
The characteristics of taurine uptake in rabbit jejunal brush-border membrane vesicles were investigated. Taurine was transiently accumulated inside the vesicles against a concentration gradient when an inwardly directed NaCl gradient was imposed across the membrane. Uptake of taurine showed an absolute requirement for both Na+ and Cl-. The NaCl gradient-dependent taurine uptake was stimulated by a valinomycin-induced, inside-negative, K+-diffusion potential, suggesting that the uptake process was electrogenic. The uptake system exclusively interacted with beta-amino acids of small size, but had no affinity for alpha-amino acids. Kinetic analysis revealed that the system exhibited high affinity for taurine (Kt = 14.4 +/- 0.5 microM). Taurine uptake was greatly influenced by extravesicular concentrations of Na+ and Cl-. The Cl- stoichiometry was found to be one. In the presence of Cl-, taurine uptake was sigmoidally related to Na+ concentration, and the Na+ stoichiometry was calculated to be three. Thus three Na+ and one Cl- were involved per transport of one taurine molecule. The uptake process was not affected by other transport inhibitors such as amiloride, harmaline, furosemide, and 4,4'-diisothiocyanostilbene-2,2'-disulfonate.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2750911&dopt=Abstract
J Biol Chem. 1988 Jan 15;263(2):945-51.
Protein I, a translocatable ion channel from Neisseria gonorrhoeae, selectively inhibits exocytosis from human neutrophils without inhibiting O2- generation.
Haines KA, Yeh L, Blake MS, Cristello P, Korchak H, Weissmann G.
Department of Medicine, New York University Medical Center, New York 10016.
Protein I, the major outer membrane protein of Neisseria gonorrhoeae, is a voltage-dependent anion channel which can translocate from the gonococcus into human cells. Since granule exocytosis from neutrophils is regulated by ion fluxes, we examined the effect of protein I on neutrophil activation. Pretreatment with protein I (250 nM) impaired degranulation from neutrophils: beta-glucuronidase release decreased to 27 +/- 6% S.E. of cells treated with N-f-Met-Leu-Phe (fMLP, 0.1 microM) and to 13 +/- 4% of cells treated with leukotriene B4 (LTB4, 0.1 microM); lysozyme release decreased to 52 +/- 17% of fMLP-treated cells and 22 +/- 9% of LTB4-treated cells. Morphometric analysis was consistent: control neutrophils increased their surface membrane after fMLP (43.3 +/- 5.6 microns relative perimeter versus 71.4 +/- 3.7 microns) while protein I-treated neutrophils did not (29.4 +/- 2 (S.E.) microns relative perimeter versus 34 +/- 4 microns). Enzyme release after exposure to phorbol myristate acetate was not affected (lysozyme: 86 +/- 27% of control). Cell/cell aggregation in response to fMLP was inhibited by treatment with protein I. However, generation of O2 was not affected. Protein I altered the surface membrane potential (Oxonol V): protein I evoked a transient membrane hyperpolarization which was not inhibited by furosemide. After exposure to fMLP, protein I-treated neutrophils underwent a furosemide-sensitive hyperpolarization rather than the usual depolarization. Protein I did not alter increments in [Ca]i (Fura-2) stimulated by fMLP (460 +/- 99 nM (S.E.) versus 377 +/- 44 nM) nor decrements in [pH]i (7.22 +/- 0.04 S.E. versus 7.22 +/- 0.02, bis-(carboxy-ethyl)carboxyfluorescein). The results suggest that degranulation and O2 generation have separate ionic requirements and that protein I interrupts the activation sequence proximal to activation of protein kinase C.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2826469&dopt=Abstract
Am J Physiol. 1984 Nov;247(5 Pt 2):F753-9.
Absence of Cl-OH exchange and NaCl cotransport in rabbit renal microvillus membrane vesicles.
Seifter JL, Knickelbein R, Aronson PS.
Cl-transport was studied in microvillus membrane vesicles isolated from the rabbit renal cortex. Inwardly directed K+ gradients in the presence of the K+ ionophore valinomycin (Val) enhanced 10 mM 36Cl uptake 2.5-fold, confirming a Cl- conductive pathway. An inwardly directed H+ gradient (pHin 7.5, pHout 6.0) stimulated 10 mM Cl- uptake 1.5-fold compared with pHin = pHout = 6.0. However, this H+ gradient stimulation of Cl- uptake appeared secondary to the H+ diffusion potential rather than to Cl-OH exchange, as it was abolished by Val and K+in = K+out. Additional evidence against Cl- transport via anion exchange was the failure of an inwardly directed Cl- gradient to generate an inside-acid pH gradient as monitored by quenching of acridine orange fluorescence. Cl- influx was the same in the presence of inwardly directed gradients of Na+, K+, Cs+, Li+, and Rb+, arguing against NaCl cotransport. Finally, conductive Cl- transport was reduced by the inhibitors furosemide, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid and 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid. These data indicate the presence of an inhibitor-sensitive, conductive mode of Cl- transport but fail to demonstrate significant pathways for Cl- OH exchange or NaCl cotransport in rabbit renal microvillus membrane vesicles.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6093589&dopt=Abstract
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