PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9516235-8 1998 The Na-H exchanger inhibitor amiloride (1 mM) reduced pHi 0.52 +/- 0.10 pH units. Amiloride 29-38 glucose-6-phosphate isomerase Oryctolagus cuniculus 54-57 9516235-9 1998 In the presence of DBI, the magnitude of pHi reduction caused by amiloride was significantly (P < 0.05) reduced to 0.26 +/- 0.09 pH units. Amiloride 65-74 glucose-6-phosphate isomerase Oryctolagus cuniculus 41-44 9516235-11 1998 DBI also reduced by approximately 40% the rate of pHi recovery in cells acidified by an ammonium chloride (20 mM) prepulse; a reduction in pHi recovery rate was also caused by ACTZ and amiloride. Amiloride 185-194 glucose-6-phosphate isomerase Oryctolagus cuniculus 139-142 7736498-8 1995 The increase in steady state pHi was blocked by inhibitors of Na+/H+ exchange, amiloride (1 mM) and EIPA (10 microM). Amiloride 79-88 glucose-6-phosphate isomerase Oryctolagus cuniculus 29-32 9374847-3 1997 In contrast, intracellular pH (pHi) recovery after removing luminal NH4+ was unaffected by bumetanide and Ba2+ but was sensitive to 1 mM luminal amiloride (71% inhibition). Amiloride 145-154 glucose-6-phosphate isomerase Oryctolagus cuniculus 31-34 7722419-4 1995 Osmotic cell shrinkage was accompanied by an amiloride-sensitive increase in baseline pHi. Amiloride 45-54 glucose-6-phosphate isomerase Oryctolagus cuniculus 86-89 8214100-6 1993 Both cell populations demonstrated similar rates of Na+/H+ exchange, as assessed by peritubular Na(+)-dependent, amiloride-sensitive pHi recovery from an intracellular acid load. Amiloride 113-122 glucose-6-phosphate isomerase Oryctolagus cuniculus 133-136 2003583-9 1991 In the absence of a demonstrable H+ conductance, it is concluded that amiloride-induced acidification and K(+)-induced pHi changes are via a carrier-mediated K(+)-H+ exchanger. Amiloride 70-79 glucose-6-phosphate isomerase Oryctolagus cuniculus 119-122 8381606-5 1993 However, bath amiloride significantly reduced the initial rate of pHi recovery after acidification (0.70 pH U/min in control vs. 0.39 pH U/min with amiloride). Amiloride 14-23 glucose-6-phosphate isomerase Oryctolagus cuniculus 66-69 1329529-8 1992 However, addition of 10(-4) M amiloride caused pHi to decrease to 7.29 +/- 0.18 (P less than 0.01). Amiloride 30-39 glucose-6-phosphate isomerase Oryctolagus cuniculus 47-50 1504097-11 1992 pHi recovery to the initial value was caused mainly by amiloride-sensitive Na+/H+ exchange and to a lesser extent by an amiloride-insensitive system, which was not studied in detail. Amiloride 55-64 glucose-6-phosphate isomerase Oryctolagus cuniculus 0-3 1504097-11 1992 pHi recovery to the initial value was caused mainly by amiloride-sensitive Na+/H+ exchange and to a lesser extent by an amiloride-insensitive system, which was not studied in detail. Amiloride 120-129 glucose-6-phosphate isomerase Oryctolagus cuniculus 0-3 1629906-6 1992 A similar pHi recovery was also stimulated by Li, Cs (both 72 mM), and Tl (10 mM), in the order Li greater than K greater than Cs greater than Tl (all in the presence of amiloride), and these alkalinizations were also blocked by 100 microM SCH28080. Amiloride 170-179 glucose-6-phosphate isomerase Oryctolagus cuniculus 10-13 1310223-7 1992 For a given pHi, amiloride-inhibitable proton efflux rates during pHi recovery from an acid load were identical in resting and stimulated cells, suggesting that neither the transport capacity not the pHi set point of the parietal cell Na(+)-H+ exchanger is altered by cAMP-dependent stimulation of acid formation. Amiloride 17-26 glucose-6-phosphate isomerase Oryctolagus cuniculus 12-15 1310223-7 1992 For a given pHi, amiloride-inhibitable proton efflux rates during pHi recovery from an acid load were identical in resting and stimulated cells, suggesting that neither the transport capacity not the pHi set point of the parietal cell Na(+)-H+ exchanger is altered by cAMP-dependent stimulation of acid formation. Amiloride 17-26 glucose-6-phosphate isomerase Oryctolagus cuniculus 66-69 1310223-7 1992 For a given pHi, amiloride-inhibitable proton efflux rates during pHi recovery from an acid load were identical in resting and stimulated cells, suggesting that neither the transport capacity not the pHi set point of the parietal cell Na(+)-H+ exchanger is altered by cAMP-dependent stimulation of acid formation. Amiloride 17-26 glucose-6-phosphate isomerase Oryctolagus cuniculus 66-69 2035650-6 1991 pHi of PC and IC significantly increased by bath Cl- removal in the absence of Na+ and decreased by bath Na+ removal in the absence of Cl- but with amiloride. Amiloride 148-157 glucose-6-phosphate isomerase Oryctolagus cuniculus 0-3 2168329-16 1990 These studies indicate that nucleated esophageal cells obtained from rabbits possess an amiloride-sensitive Na+,H+ antiport that functions to regulate basal pHi and responds to intracellular acidification. Amiloride 88-97 glucose-6-phosphate isomerase Oryctolagus cuniculus 157-160 1966525-3 1990 When cells were acidified by ammonium withdrawal, the initial pHi recovery rate was 0.33 +/- 0.02 pH unit/min; replacement of extracellular Na+ (130 mM) with N-methyl-D-glucamine+ reduced the pHi recovery rate to 0.08 +/- 0.02 pH unit/min, while addition of 0.1 mM amiloride in the presence of extracellular Na+ reduced the rate of pHi recovery to 0.02 +/- 0.02 pH unit/min. Amiloride 265-274 glucose-6-phosphate isomerase Oryctolagus cuniculus 62-65 1966525-3 1990 When cells were acidified by ammonium withdrawal, the initial pHi recovery rate was 0.33 +/- 0.02 pH unit/min; replacement of extracellular Na+ (130 mM) with N-methyl-D-glucamine+ reduced the pHi recovery rate to 0.08 +/- 0.02 pH unit/min, while addition of 0.1 mM amiloride in the presence of extracellular Na+ reduced the rate of pHi recovery to 0.02 +/- 0.02 pH unit/min. Amiloride 265-274 glucose-6-phosphate isomerase Oryctolagus cuniculus 192-195 1966525-3 1990 When cells were acidified by ammonium withdrawal, the initial pHi recovery rate was 0.33 +/- 0.02 pH unit/min; replacement of extracellular Na+ (130 mM) with N-methyl-D-glucamine+ reduced the pHi recovery rate to 0.08 +/- 0.02 pH unit/min, while addition of 0.1 mM amiloride in the presence of extracellular Na+ reduced the rate of pHi recovery to 0.02 +/- 0.02 pH unit/min. Amiloride 265-274 glucose-6-phosphate isomerase Oryctolagus cuniculus 192-195 2919659-9 1989 The recovery of pHi after the initial acidosis on stimulation with ACh could be blocked by 1 mM amiloride, suggesting that the recovery phase was mediated by Na+-H+ exchange. Amiloride 96-105 glucose-6-phosphate isomerase Oryctolagus cuniculus 16-19 2166273-6 1990 After the acid-loading procedure, cultured proximal cells recovered their pHi by means of the classic Na+/H+ antiporter, sensitive to amiloride and located in the apical membrane only. Amiloride 134-143 glucose-6-phosphate isomerase Oryctolagus cuniculus 74-77 2603961-6 1989 However, a slow pHi decrease was observed in response to bath Na+ removal when the bath fluid contained ACTZ and the luminal fluid contained 4 mM amiloride. Amiloride 146-155 glucose-6-phosphate isomerase Oryctolagus cuniculus 16-19 2476937-7 1989 Amiloride or Na-free solution (which should reverse the Na-H exchanger and cause cellular acidification) caused pHi to decrease 2.5 or 5 times, respectively, more slowly in stimulated PC compared with resting PC. Amiloride 0-9 glucose-6-phosphate isomerase Oryctolagus cuniculus 112-115 2782409-5 1989 In solutions containing 1 mM amiloride, which blocked Na-H exchange, pHi recovered only if Na and HCO3 were both present. Amiloride 29-38 glucose-6-phosphate isomerase Oryctolagus cuniculus 69-72 2782409-6 1989 This amiloride-resistant, Na- and HCO3-dependent pHi recovery was inhibited by 100 microM H2 4,4"-diisothiocyanostilbene-2,2"-disulfonic acid (reversibly) and occurred at equal rates in Cl-containing and Cl-free solutions. Amiloride 5-14 glucose-6-phosphate isomerase Oryctolagus cuniculus 49-52 2782409-7 1989 In NaCl solutions buffered with HCO3-CO2 and containing amiloride, after an acid load pHi recovers to pHi 7.0-7.1 solely through the activity of the Na-HCO3 cotransporter. Amiloride 56-65 glucose-6-phosphate isomerase Oryctolagus cuniculus 86-89 2782409-7 1989 In NaCl solutions buffered with HCO3-CO2 and containing amiloride, after an acid load pHi recovers to pHi 7.0-7.1 solely through the activity of the Na-HCO3 cotransporter. Amiloride 56-65 glucose-6-phosphate isomerase Oryctolagus cuniculus 102-105 2755773-6 1989 In the presence of 10(-3) mol/l amiloride, the response to acetylcholine was a rapid decrease in pHi to 7.02 +/- 0.02. Amiloride 32-41 glucose-6-phosphate isomerase Oryctolagus cuniculus 97-100 3225554-7 1988 Amiloride (1-2 mM) inhibited the pHi recovery that was elicited by returning 15 or 29 mM Na+ to lumen by only approximately 30%. Amiloride 0-9 glucose-6-phosphate isomerase Oryctolagus cuniculus 33-36 2854165-5 1988 In the presence of luminal amiloride (1 mM), the rate of decrease of pHi was significantly less, 0.73 +/- 0.18 pH/min. Amiloride 27-36 glucose-6-phosphate isomerase Oryctolagus cuniculus 69-72 2854165-6 1988 Steady-state pHi decreased 0.18 pH units following the addition of amiloride (1 mM) to the lumen (Na+ 140 mM lumen and bath). Amiloride 67-76 glucose-6-phosphate isomerase Oryctolagus cuniculus 13-16 2854165-8 1988 The rate of decrease of pHi was significantly less in the presence of 1 mM basolateral amiloride, 0.29 +/- 0.04 pH/min. Amiloride 87-96 glucose-6-phosphate isomerase Oryctolagus cuniculus 24-27 2854165-9 1988 Addition of 1 mM amiloride to the basolateral side (Na+ 140 mM lumen and bath) caused steady-state pHi to decrease significantly by 0.06 pH units. Amiloride 17-26 glucose-6-phosphate isomerase Oryctolagus cuniculus 99-102 2854165-12 1988 The rate of pHi recovery was inhibited 93% by 1 mM luminal amiloride. Amiloride 59-68 glucose-6-phosphate isomerase Oryctolagus cuniculus 12-15 2854165-14 1988 Addition of 1 mM basolateral amiloride inhibited the recovery of pHi by 97%. Amiloride 29-38 glucose-6-phosphate isomerase Oryctolagus cuniculus 65-68 2843231-7 1988 There was a dose-dependent inhibition of pHi recovery after NH4Cl prepulse by amiloride with an IC50 of about 15 microM. Amiloride 78-87 glucose-6-phosphate isomerase Oryctolagus cuniculus 41-44 2843231-8 1988 Amiloride in a concentration of 1 mM almost completely abolished pHi recovery. Amiloride 0-9 glucose-6-phosphate isomerase Oryctolagus cuniculus 65-68 3225554-8 1988 However, in the absence of external acetate (Ac-), 1 mM amiloride inhibited approximately 66% of the pHi recovery induced by the readdition of 29 mM Na+ to the lumen only. Amiloride 56-65 glucose-6-phosphate isomerase Oryctolagus cuniculus 101-104 2888787-5 1987 The decrease in pHi was inhibited 62% by 1 mM amiloride (lumen) and was unaffected by 50 microM 4,4"-diisothiocyanostilbene-2,2"-disulfonic acid (lumen) and Cl- removal (lumen, bath). Amiloride 46-55 glucose-6-phosphate isomerase Oryctolagus cuniculus 16-19 3037913-9 1987 It was also found that changing from NMG gluconate to Na gluconate Ringer caused pHi to increase from 7.1 to 7.3, and this alkalinization was blocked by 10(-3) M amiloride; changing from NMG gluconate to NMG Cl Ringer caused pHi to decrease to 6.7. Amiloride 162-171 glucose-6-phosphate isomerase Oryctolagus cuniculus 81-84 3037913-9 1987 It was also found that changing from NMG gluconate to Na gluconate Ringer caused pHi to increase from 7.1 to 7.3, and this alkalinization was blocked by 10(-3) M amiloride; changing from NMG gluconate to NMG Cl Ringer caused pHi to decrease to 6.7. Amiloride 162-171 glucose-6-phosphate isomerase Oryctolagus cuniculus 225-228 3030871-5 1987 This regulatory range of pHi (= 0.7 pH units) was abolished by sodium-free Ringer"s or addition of 10(-3) M amiloride and also by 10(-4) M ouabain. Amiloride 108-117 glucose-6-phosphate isomerase Oryctolagus cuniculus 25-28 3001217-12 1985 The basolateral Na-dependent pHi recovery was reversibly inhibited by amiloride. Amiloride 70-79 glucose-6-phosphate isomerase Oryctolagus cuniculus 29-32