PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9516235-5 1998 ACTZ markedly inhibited the rapid pHi changes elicited by bicarbonate/CO2 removal and readdition but DBI was ineffective in this respect, consistent with the inability of DBI to enter the cell and inhibit cytoplasmic CA isozymes. Bicarbonates 58-69 glucose-6-phosphate isomerase Oryctolagus cuniculus 34-37 10652030-8 2000 An analysis of pHi responses to bath HCO3- reduction revealed that DA, SKF 38393 (a DA1 agonist), and adenosine 3",5"-cyclic monophosphate (cAMP) inhibited the basolateral Na+:HCO3- cotransporter in rabbit and Wistar-Kyoto rat (WKY), if its transport stoichiometry was converted to 3 HCO3-:1 Na+ by DMEM plus NE incubation. Bicarbonates 37-41 glucose-6-phosphate isomerase Oryctolagus cuniculus 15-18 10652030-8 2000 An analysis of pHi responses to bath HCO3- reduction revealed that DA, SKF 38393 (a DA1 agonist), and adenosine 3",5"-cyclic monophosphate (cAMP) inhibited the basolateral Na+:HCO3- cotransporter in rabbit and Wistar-Kyoto rat (WKY), if its transport stoichiometry was converted to 3 HCO3-:1 Na+ by DMEM plus NE incubation. Bicarbonates 176-180 glucose-6-phosphate isomerase Oryctolagus cuniculus 15-18 16916522-11 2006 When compared to HEPES-buffered solutions, HFH myocytes in CO2/HCO3--buffered solutions shortened 12+/-6.8% better than expected given the 0.16+/-0.02 units more acidic pHi"s at which they twitched. Bicarbonates 63-67 glucose-6-phosphate isomerase Oryctolagus cuniculus 169-172 12812914-3 2003 Intracellular pH (pHi), measured with the dye BCECF, fell by 0.54 +/- 0.08 (n = 14) when we added CO2/HCO3- to the lumen. Bicarbonates 102-106 glucose-6-phosphate isomerase Oryctolagus cuniculus 18-21 12812914-4 2003 In 14 tubules in which we added CO2/HCO3- to the bath, pHi fell by 0.55 +/- 0.11 in 9 with a high initial pHi, but rose by 0.28 +/- 0.07 in the other 5 with a low initial pHi. Bicarbonates 36-40 glucose-6-phosphate isomerase Oryctolagus cuniculus 55-58 12812914-4 2003 In 14 tubules in which we added CO2/HCO3- to the bath, pHi fell by 0.55 +/- 0.11 in 9 with a high initial pHi, but rose by 0.28 +/- 0.07 in the other 5 with a low initial pHi. Bicarbonates 36-40 glucose-6-phosphate isomerase Oryctolagus cuniculus 106-109 12812914-4 2003 In 14 tubules in which we added CO2/HCO3- to the bath, pHi fell by 0.55 +/- 0.11 in 9 with a high initial pHi, but rose by 0.28 +/- 0.07 in the other 5 with a low initial pHi. Bicarbonates 36-40 glucose-6-phosphate isomerase Oryctolagus cuniculus 106-109 9041246-4 1997 RESULTS: Cells exposed to low pHo in both bicarbonate-free and bicarbonate-containing buffers produced a decline in pHi to as low as 6.5, but this occurred without change in volume. Bicarbonates 42-53 glucose-6-phosphate isomerase Oryctolagus cuniculus 116-119 9041246-4 1997 RESULTS: Cells exposed to low pHo in both bicarbonate-free and bicarbonate-containing buffers produced a decline in pHi to as low as 6.5, but this occurred without change in volume. Bicarbonates 63-74 glucose-6-phosphate isomerase Oryctolagus cuniculus 116-119 8946002-5 1996 Consistent with the cotransporter stimulation, PMA decreased steady-state pHi in the presence of CO2/ HCO3-. Bicarbonates 102-106 glucose-6-phosphate isomerase Oryctolagus cuniculus 74-77 7631810-1 1995 Three different mechanisms interact to control the cytosolic pH (pHi) of alveolar macrophages (M phi), namely, plasmalemmal vacuolar-type H(+)-ATPase (V-ATPase), Na+/H+ exchange, and Na(+)-independent HCO3-/Cl- exchange. Bicarbonates 201-205 glucose-6-phosphate isomerase Oryctolagus cuniculus 65-68 7821379-6 1994 Replacement of 28 mM Hepes by 28 mM HCO3-/5% CO2 led to a 0.14 +/- 0.04 increase in pHi. Bicarbonates 36-40 glucose-6-phosphate isomerase Oryctolagus cuniculus 84-87 7864155-9 1995 Over a broad range of pHi values, total net acid extrusion was approximately four times higher in bilateral presence of CO2/HCO3- than in its absence. Bicarbonates 124-128 glucose-6-phosphate isomerase Oryctolagus cuniculus 22-25 7864155-11 1995 Initial rate of luminal Na(+)-dependent net acid extrusion in presence of CO2/HCO3- was approximately 229 microM/s (pHi 6.92), approximately 1.8 times higher than the flux of approximately 127 microM/s (P < 0.005) obtained in absence of CO2/HCO3- (pHi 6.66). Bicarbonates 78-82 glucose-6-phosphate isomerase Oryctolagus cuniculus 116-119 7864155-12 1995 CO2/HCO3- alkali-shifted the flux vs. pHi relationship by 0.3-0.4 pH units. Bicarbonates 4-8 glucose-6-phosphate isomerase Oryctolagus cuniculus 38-41 7864155-15 1995 Also, Na(+)-independent net acid extrusion rate was approximately two to three times higher in presence than in absence of CO2/HCO3- at comparable pHi. Bicarbonates 127-131 glucose-6-phosphate isomerase Oryctolagus cuniculus 147-150 7864155-17 1995 Stimulation of luminal Na+/H+ exchange and Na(+)-independent acid extrusion appears to be the major, if not the entire, explanation for the higher steady-state pHi caused by bilateral addition of CO2/HCO3-. Bicarbonates 200-204 glucose-6-phosphate isomerase Oryctolagus cuniculus 160-163 7864156-11 1995 On the other hand, basolateral CO2/HCO3- increased the pHi recovery rate to an even greater extent than had bilateral CO2/HCO3-. Bicarbonates 35-39 glucose-6-phosphate isomerase Oryctolagus cuniculus 55-58 7864156-14 1995 On the other hand, adding CO2/HCO3- to only the bath substantially increased the rate of Na(+)-independent pHi recovery, which generally was greater than that observed with bilateral CO2/HCO3-. Bicarbonates 30-34 glucose-6-phosphate isomerase Oryctolagus cuniculus 107-110 7707229-16 1994 The pHi range for allosteric activation found in this study would suggest that for both the ileum and the parietal cell anion exchanger, but especially for the latter, a potentiating effect of the allosteric activation and the HCO3- availability occurs within the physiological pHi range and can cause dramatic increases in maximal anion exchange rates with increasing pHi. Bicarbonates 227-231 glucose-6-phosphate isomerase Oryctolagus cuniculus 4-7 7707229-16 1994 The pHi range for allosteric activation found in this study would suggest that for both the ileum and the parietal cell anion exchanger, but especially for the latter, a potentiating effect of the allosteric activation and the HCO3- availability occurs within the physiological pHi range and can cause dramatic increases in maximal anion exchange rates with increasing pHi. Bicarbonates 227-231 glucose-6-phosphate isomerase Oryctolagus cuniculus 278-281 7707229-16 1994 The pHi range for allosteric activation found in this study would suggest that for both the ileum and the parietal cell anion exchanger, but especially for the latter, a potentiating effect of the allosteric activation and the HCO3- availability occurs within the physiological pHi range and can cause dramatic increases in maximal anion exchange rates with increasing pHi. Bicarbonates 227-231 glucose-6-phosphate isomerase Oryctolagus cuniculus 278-281 8203522-1 1994 In many cell types, the regulation of intracellular pH (pHi) is different in the presence vs. absence of HCO3-. Bicarbonates 105-109 glucose-6-phosphate isomerase Oryctolagus cuniculus 56-59 8203522-3 1994 In Cl(-)-depleted parietal cells, the dependence of maximal proton efflux rate on pHi showed a strong inverse correlation but was identical in the presence and absence of HCO3-. Bicarbonates 171-175 glucose-6-phosphate isomerase Oryctolagus cuniculus 82-85 8203522-6 1994 In Cl(-)-containing cells, there was also some Na(+)-independent, extracellular HCO(3-)- and intracellular Cl(-)-dependent, DIDS-inhibitable pHi recovery from an acid load, most likely due to intracellular Cl(-)-extracellular HCO3- exchange. Bicarbonates 226-230 glucose-6-phosphate isomerase Oryctolagus cuniculus 141-144 8203522-7 1994 Recovery from an alkaline load was primarily mediated by anion exchange, and the dependence of maximal anion exchange rates on pHi was very different in the absence and presence of HCO3-. Bicarbonates 181-185 glucose-6-phosphate isomerase Oryctolagus cuniculus 127-130 8203522-9 1994 In the presence of HCO3-, however, there was an S-shaped dependence of maximal flux rates on pHi, with a steep increase in flux rates between 6.8 and 7.5. Bicarbonates 19-23 glucose-6-phosphate isomerase Oryctolagus cuniculus 93-96 8419242-4 1993 Cells in HEPES switched to CO2/HCO3- buffer rapidly acidified to pHi of 7, then alkalinized to a new steady-state pHi. Bicarbonates 31-35 glucose-6-phosphate isomerase Oryctolagus cuniculus 65-68 8133244-10 1993 Basolateral CO2/HCO3- elicited the usual pHi increase even when all solutes were replaced, short or long-term (> 45 min), by N-methyl-D-glucammonium/glucuronate (NMDG+/Glr-). Bicarbonates 16-20 glucose-6-phosphate isomerase Oryctolagus cuniculus 41-44 8133244-12 1993 Although the sustained pHi increase elicited by basolateral CO2/HCO3- could be due to a basolateral HCO3- uptake mechanism, net reabsorption of HCO3- by the S3 segment, as well as our ACZ data, suggest instead that basolateral CO2/HCO3- elicits the sustained pHi increase either by inhibiting an acid-loading process or stimulating acid extrusion across the luminal membrane (e.g., via an H+ pump). Bicarbonates 64-68 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 8133244-12 1993 Although the sustained pHi increase elicited by basolateral CO2/HCO3- could be due to a basolateral HCO3- uptake mechanism, net reabsorption of HCO3- by the S3 segment, as well as our ACZ data, suggest instead that basolateral CO2/HCO3- elicits the sustained pHi increase either by inhibiting an acid-loading process or stimulating acid extrusion across the luminal membrane (e.g., via an H+ pump). Bicarbonates 64-68 glucose-6-phosphate isomerase Oryctolagus cuniculus 259-262 8133244-12 1993 Although the sustained pHi increase elicited by basolateral CO2/HCO3- could be due to a basolateral HCO3- uptake mechanism, net reabsorption of HCO3- by the S3 segment, as well as our ACZ data, suggest instead that basolateral CO2/HCO3- elicits the sustained pHi increase either by inhibiting an acid-loading process or stimulating acid extrusion across the luminal membrane (e.g., via an H+ pump). Bicarbonates 100-104 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 8133244-12 1993 Although the sustained pHi increase elicited by basolateral CO2/HCO3- could be due to a basolateral HCO3- uptake mechanism, net reabsorption of HCO3- by the S3 segment, as well as our ACZ data, suggest instead that basolateral CO2/HCO3- elicits the sustained pHi increase either by inhibiting an acid-loading process or stimulating acid extrusion across the luminal membrane (e.g., via an H+ pump). Bicarbonates 100-104 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 8133244-12 1993 Although the sustained pHi increase elicited by basolateral CO2/HCO3- could be due to a basolateral HCO3- uptake mechanism, net reabsorption of HCO3- by the S3 segment, as well as our ACZ data, suggest instead that basolateral CO2/HCO3- elicits the sustained pHi increase either by inhibiting an acid-loading process or stimulating acid extrusion across the luminal membrane (e.g., via an H+ pump). Bicarbonates 100-104 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 8500555-10 1993 Replacement of 28 mM Hepes by 28 mM HCO3-/5% CO2 led to a 0.13 pHi increase in the PE and a decrease of 0.27 U in the NPE. Bicarbonates 36-40 glucose-6-phosphate isomerase Oryctolagus cuniculus 63-66 8384246-7 1993 4,4"-Diisothiocyanatostilbene-2,2"-disulfonic acid (DIDS), an inhibitor of Cl-/HCO3- antiports, blocked recovery of pHi in a dose-related fashion in the presence of bicarbonate, but not in the presence of HEPES. Bicarbonates 79-83 glucose-6-phosphate isomerase Oryctolagus cuniculus 116-119 8384246-7 1993 4,4"-Diisothiocyanatostilbene-2,2"-disulfonic acid (DIDS), an inhibitor of Cl-/HCO3- antiports, blocked recovery of pHi in a dose-related fashion in the presence of bicarbonate, but not in the presence of HEPES. Bicarbonates 165-176 glucose-6-phosphate isomerase Oryctolagus cuniculus 116-119 8133244-3 1993 However, with acetate absent bilaterally, this causing steady-state pHi to be substantially lower (approximately 6.9), bilaterally switching to CO2/HCO3- caused a transient pHi fall (due to the influx of CO2), followed by a sustained rise to a level approximately 0.18 higher than the initial one. Bicarbonates 148-152 glucose-6-phosphate isomerase Oryctolagus cuniculus 173-176 8133244-5 1993 Switching to CO2/HCO3- only in the lumen caused a sustained pHi fall of approximately 0.15, whereas switching to CO2/HCO3- only in the bath caused a transient fall followed by a sustained pHi increase to approximately 0.26 above the initial value. Bicarbonates 17-21 glucose-6-phosphate isomerase Oryctolagus cuniculus 60-63 8214100-7 1993 In contrast, Na(+)-independent, HCO3(-)-independent pHi recovery from an acid load was present in both cell populations but had two to three times greater activity in a minority cell population. Bicarbonates 32-36 glucose-6-phosphate isomerase Oryctolagus cuniculus 52-55 8419242-4 1993 Cells in HEPES switched to CO2/HCO3- buffer rapidly acidified to pHi of 7, then alkalinized to a new steady-state pHi. Bicarbonates 31-35 glucose-6-phosphate isomerase Oryctolagus cuniculus 114-117 8419242-6 1993 Cells in a CO2/HCO3- buffer rapidly alkalinized to pH 8.2 when switched to HEPES, then acidified to a new steady-state pHi. Bicarbonates 15-19 glucose-6-phosphate isomerase Oryctolagus cuniculus 119-122 1329529-9 1992 When cells were acidified (pHi 6.3-7.0) using a NH4Cl (20 mM) pulse technique, pHi was rapidly restored toward neutrality in the presence of a HCO3(-)-free external Na+ concentration ([Na+]o)-containing solution (pH units/min = 0.26 +/- 0.12; n = 8). Bicarbonates 143-147 glucose-6-phosphate isomerase Oryctolagus cuniculus 79-82 1628400-4 1992 In normal perfusion with CO2/HCO3(-)-buffered blood at PCO2 of 35 mm Hg, pHi was 7.03 +/- 0.03. Bicarbonates 29-33 glucose-6-phosphate isomerase Oryctolagus cuniculus 73-76 1323499-2 1992 pHi was measured in single basal and mature squamous cells after loading with the fluorescent probe 2",7"-bis(carboxyethyl)-5(and -6)carboxyfluorescein at 25 degrees C in a nominally bicarbonate-free HEPES buffer. Bicarbonates 183-194 glucose-6-phosphate isomerase Oryctolagus cuniculus 0-3 1628400-11 1992 If the muscles were perfused with CO2/HCO3(-)-buffered perfusate in the absence of red blood cells, the changes of pHo and pHi were significantly larger (pHo, 6.00 versus 6.64; pHi, 6.46 versus 6.93 at 14 minutes) during ischemia. Bicarbonates 38-45 glucose-6-phosphate isomerase Oryctolagus cuniculus 123-126 1628400-11 1992 If the muscles were perfused with CO2/HCO3(-)-buffered perfusate in the absence of red blood cells, the changes of pHo and pHi were significantly larger (pHo, 6.00 versus 6.64; pHi, 6.46 versus 6.93 at 14 minutes) during ischemia. Bicarbonates 38-45 glucose-6-phosphate isomerase Oryctolagus cuniculus 177-180 1321841-6 1992 Basolateral membrane Cl-/HCO3- exchange activity assayed as the pHi response to basolateral Cl- addition was increased 73% in DOCA tubules versus controls, and decreased 44% in ADX tubules versus controls. Bicarbonates 25-29 glucose-6-phosphate isomerase Oryctolagus cuniculus 64-67 2166273-8 1990 Moreover, at physiological initial pHi values, chloride removal from the apical solution caused the pHi to increase in the presence of bicarbonate. Bicarbonates 135-146 glucose-6-phosphate isomerase Oryctolagus cuniculus 100-103 2035650-7 1991 4,4"-Diisothiocyanostilbene-2,2"-disulfonic acid (DIDS) inhibited these pHi responses to a reduction of bath HCO3-, Cl-, or Na+, and an alkali loading. Bicarbonates 109-113 glucose-6-phosphate isomerase Oryctolagus cuniculus 72-75 2127311-3 1990 In control solutions containing 25 mmol/l HCO3 pHi increased initially by 5.0 +/- 0.3 x 10(-3) unit/s but after perfusion with CO2/HCO3(-)-free solutions pHi of the same cells increased only by 1.3 +/- 0.2 x 10(-3) unit/s in response to Cl- substitution. Bicarbonates 42-46 glucose-6-phosphate isomerase Oryctolagus cuniculus 47-50 1314849-6 1992 DOCA, but not acidosis, increased (approximately 40%) initial pHi response to bath HCO3- or Cl- reduction in Na(+)-free condition. Bicarbonates 83-87 glucose-6-phosphate isomerase Oryctolagus cuniculus 62-65 1647688-6 1991 Luminal Na-H exchange was assayed by monitoring changes in pHi (dpHi/dt) in response to luminal Na+ removal in HCO3- free condition. Bicarbonates 111-115 glucose-6-phosphate isomerase Oryctolagus cuniculus 59-62 2022727-5 1991 Decreased PCO2 results in increased pHi associated with activation of Cl-/HCO3- exchange and partial recovery of pHi. Bicarbonates 74-78 glucose-6-phosphate isomerase Oryctolagus cuniculus 36-39 1645273-4 1991 In CO2/HCO3- Ringer"s, npe pHi = 7.09 +/- 0.11. Bicarbonates 7-11 glucose-6-phosphate isomerase Oryctolagus cuniculus 27-30 1645273-5 1991 Replacement of CO2/HCO3- by Hepes increased pHi by 0.22 +/- 0.02, indicating alkali secretory activity under the bicarbonate-rich conditions. Bicarbonates 19-23 glucose-6-phosphate isomerase Oryctolagus cuniculus 44-47 1645273-5 1991 Replacement of CO2/HCO3- by Hepes increased pHi by 0.22 +/- 0.02, indicating alkali secretory activity under the bicarbonate-rich conditions. Bicarbonates 113-124 glucose-6-phosphate isomerase Oryctolagus cuniculus 44-47 1645273-10 1991 In Cl(-)-free media pHi reached 7.8-8.0, a condition under which intracellular [HCO3-] is at least twice as high as its extracellular value. Bicarbonates 80-85 glucose-6-phosphate isomerase Oryctolagus cuniculus 20-23 2153152-6 1990 In the beta-intercalated cells, luminal Cl- removal blocked changes in pHi in response to changes in luminal HCO3- or peritubular Cl-, providing direct evidence for a luminal Cl-/HCO3- exchanger. Bicarbonates 109-113 glucose-6-phosphate isomerase Oryctolagus cuniculus 71-74 2336349-3 1990 From the response of pHi and [Cl-]i to changes in bath Cl- or HCO3- concentrations a Cl-/HCO3- exchanger was identified in the basolateral cell membrane. Bicarbonates 62-66 glucose-6-phosphate isomerase Oryctolagus cuniculus 21-24 2336349-3 1990 From the response of pHi and [Cl-]i to changes in bath Cl- or HCO3- concentrations a Cl-/HCO3- exchanger was identified in the basolateral cell membrane. Bicarbonates 89-93 glucose-6-phosphate isomerase Oryctolagus cuniculus 21-24 2155541-1 1990 We studied the role of basolateral HCO3- transport in the regulation of intracellular pH (pHi) in the isolated perfused S3 segment of the rabbit proximal tubule. Bicarbonates 35-39 glucose-6-phosphate isomerase Oryctolagus cuniculus 90-93 2155541-4 1990 pHi fell by approximately 0.17 when luminal [HCO3-] was lowered to 5 mM at fixed PCO2 (i.e., reducing pH to 6.8) but by approximately 0.42 when [HCO3-] in the bath (i.e., basolateral solution) was lowered to 5 mM. Bicarbonates 45-49 glucose-6-phosphate isomerase Oryctolagus cuniculus 0-3 2155541-4 1990 pHi fell by approximately 0.17 when luminal [HCO3-] was lowered to 5 mM at fixed PCO2 (i.e., reducing pH to 6.8) but by approximately 0.42 when [HCO3-] in the bath (i.e., basolateral solution) was lowered to 5 mM. Bicarbonates 145-149 glucose-6-phosphate isomerase Oryctolagus cuniculus 0-3 2155541-5 1990 The pHi decrease elicited by reducing bath [HCO3-] was substantially reduced by removal of Cl- or Na+, suggesting that components of basolateral HCO3- transport are Cl- and/or Na+ dependent. Bicarbonates 44-48 glucose-6-phosphate isomerase Oryctolagus cuniculus 4-7 2155541-5 1990 The pHi decrease elicited by reducing bath [HCO3-] was substantially reduced by removal of Cl- or Na+, suggesting that components of basolateral HCO3- transport are Cl- and/or Na+ dependent. Bicarbonates 145-149 glucose-6-phosphate isomerase Oryctolagus cuniculus 4-7 2155541-8 1990 Although the initial rate of this pHi increase was not reduced by removing Na+ bilaterally, it was substantially lowered by the nominal removal of HCO3- from bath and lumen or by the addition of 0.1 mM 4,4"-diisothiocyanostilbene-2,2"-disulfonate (DIDS) to the bath. Bicarbonates 147-151 glucose-6-phosphate isomerase Oryctolagus cuniculus 34-37 2155541-12 1990 Although the bilateral removal of Cl- had no effect on these rates, the nominal removal of HCO3- or the presence of DIDS substantially slowed the pHi changes. Bicarbonates 91-95 glucose-6-phosphate isomerase Oryctolagus cuniculus 146-149 2153152-6 1990 In the beta-intercalated cells, luminal Cl- removal blocked changes in pHi in response to changes in luminal HCO3- or peritubular Cl-, providing direct evidence for a luminal Cl-/HCO3- exchanger. Bicarbonates 179-183 glucose-6-phosphate isomerase Oryctolagus cuniculus 71-74 2782409-1 1989 Na- and HCO3-coupled recovery of intracellular pH (pHi) after acid loading was demonstrated in rabbit parietal cells. Bicarbonates 8-12 glucose-6-phosphate isomerase Oryctolagus cuniculus 51-54 2603961-4 1989 Bath HCO3- reduction decreased intracellular pH (pHi), and this pHi decrease was attenuated by ACTZ. Bicarbonates 5-9 glucose-6-phosphate isomerase Oryctolagus cuniculus 49-52 2603961-4 1989 Bath HCO3- reduction decreased intracellular pH (pHi), and this pHi decrease was attenuated by ACTZ. Bicarbonates 5-9 glucose-6-phosphate isomerase Oryctolagus cuniculus 64-67 2782409-5 1989 In solutions containing 1 mM amiloride, which blocked Na-H exchange, pHi recovered only if Na and HCO3 were both present. Bicarbonates 98-102 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. Bicarbonates 34-38 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. Bicarbonates 32-36 glucose-6-phosphate isomerase Oryctolagus cuniculus 86-89 2755773-2 1989 In the unstimulated gland perfused with HCO3-/CO2-buffered Ringer"s solution, pHi was 7.27 +/- 0.01. Bicarbonates 40-44 glucose-6-phosphate isomerase Oryctolagus cuniculus 78-81 2502023-8 1989 However, during such a pHi-shift experiment, metabolically derived CO2 produces a concomitant change in intracellular HCO3- concentration [( HCO3-]i). Bicarbonates 118-123 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 2502023-8 1989 However, during such a pHi-shift experiment, metabolically derived CO2 produces a concomitant change in intracellular HCO3- concentration [( HCO3-]i). Bicarbonates 118-122 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 2502023-10 1989 With this increase in [HCO3-]i at constant pHi, KCl increased by 51 +/- 10 nm/s. Bicarbonates 23-27 glucose-6-phosphate isomerase Oryctolagus cuniculus 43-46 2755773-8 1989 In the unstimulated gland, DIDS and the HCO3- -free perfusate caused decreases in pHi to 7.12 +/- 0.02 and 7.04 +/- 0.01 respectively. Bicarbonates 40-44 glucose-6-phosphate isomerase Oryctolagus cuniculus 82-85 2825539-4 1987 The intracellular pH (pHi) was measured in a bicarbonate-free medium [extracellular pH (pHe) = 7.30], using the fluorescent dye 2,7-biscarboxyethyl-5(6)-carboxyfluorescein (BCECF). Bicarbonates 45-56 glucose-6-phosphate isomerase Oryctolagus cuniculus 22-25 2843231-2 1988 Steady-state pHi in nominally bicarbonate free Ringer"s solution averaged 6.87 +/- 0.02 (mean +/- S.E., n = 53). Bicarbonates 30-41 glucose-6-phosphate isomerase Oryctolagus cuniculus 13-16 2919659-8 1989 However, Cl- -HCO3- exchange did appear to be present because replacement of Cl- caused a large DIDS-sensitive alkalinization of pHi, presumably caused by HCO3- uptake in exchange for Cl-. Bicarbonates 14-18 glucose-6-phosphate isomerase Oryctolagus cuniculus 129-132 2919659-8 1989 However, Cl- -HCO3- exchange did appear to be present because replacement of Cl- caused a large DIDS-sensitive alkalinization of pHi, presumably caused by HCO3- uptake in exchange for Cl-. Bicarbonates 155-159 glucose-6-phosphate isomerase Oryctolagus cuniculus 129-132 2455669-3 1988 Average pHi for the cells of Necturus and rabbit was approximately 7.1 in a HEPES-buffered, HCO3-free Ringer"s solution. Bicarbonates 92-96 glucose-6-phosphate isomerase Oryctolagus cuniculus 8-11 2455669-4 1988 Average pHi in Necturus cells in CO2/HCO3-buffered Ringer"s solution was approximately 7.0. Bicarbonates 37-41 glucose-6-phosphate isomerase Oryctolagus cuniculus 8-11 2450891-6 1988 The reduction rates of pHi induced by a peritubular bicarbonate reduction or sodium removal were attenuated by 20% by withdrawal of ambient chloride. Bicarbonates 52-63 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 2888787-3 1987 Steady state pHi in S3 tubules in nominally HCO3(-)-free solutions was 7.08 +/- 0.03. Bicarbonates 44-48 glucose-6-phosphate isomerase Oryctolagus cuniculus 13-16 3030871-9 1987 The data suggest that Na/H exchange is primarily responsible for the regulation of pHi over a wide range of pHo, although the specific pHi and the range of regulation are affected by the activity of the Cl/OH (HCO3) exchanger; the movement of protons or hydroxyl ions, or both, across gland cell membranes appears to be mediated under most circumstances by these two exchangers. Bicarbonates 210-214 glucose-6-phosphate isomerase Oryctolagus cuniculus 83-86 3037913-5 1987 The increase of pHi occurred equally rapidly in nominally CO2-HCO3-free solutions and in solutions containing 5% CO2 and 25 mM HCO3. Bicarbonates 62-66 glucose-6-phosphate isomerase Oryctolagus cuniculus 16-19 3037913-5 1987 The increase of pHi occurred equally rapidly in nominally CO2-HCO3-free solutions and in solutions containing 5% CO2 and 25 mM HCO3. Bicarbonates 127-131 glucose-6-phosphate isomerase Oryctolagus cuniculus 16-19 3030871-9 1987 The data suggest that Na/H exchange is primarily responsible for the regulation of pHi over a wide range of pHo, although the specific pHi and the range of regulation are affected by the activity of the Cl/OH (HCO3) exchanger; the movement of protons or hydroxyl ions, or both, across gland cell membranes appears to be mediated under most circumstances by these two exchangers. Bicarbonates 210-214 glucose-6-phosphate isomerase Oryctolagus cuniculus 135-138 3812695-2 1987 Lowering bath HCO3- from 25 to 5 mM at constant PCO2 depolarized basolateral membrane potential (Vbl), and reduced pHi. Bicarbonates 14-18 glucose-6-phosphate isomerase Oryctolagus cuniculus 115-118 3812695-8 1987 Total replacement of bath Cl- with isethionate depolarized Vbl gradually and increased pHi slightly, implying the existence of a Cl(-)-related HCO3- exit mechanism. Bicarbonates 143-147 glucose-6-phosphate isomerase Oryctolagus cuniculus 87-90 3812695-9 1987 The rate of decrease in pHi induced by lowering bath HCO3- was slightly reduced (20%) by the absence of bath Cl-. Bicarbonates 53-57 glucose-6-phosphate isomerase Oryctolagus cuniculus 24-27 6414249-2 1983 Most determinations of pHi in vivo have been performed by using indirect methods, e.g. CO2/HCO3 or DMO techniques, since no suitable direct method for reliable in vivo measurements have been available. Bicarbonates 91-95 glucose-6-phosphate isomerase Oryctolagus cuniculus 23-26 4037093-2 1985 The pHi of the rabbit proximal straight tubule perfused in vitro with a solution containing 25 mM HCO3- was 7.22 +/- 0.03. Bicarbonates 98-103 glucose-6-phosphate isomerase Oryctolagus cuniculus 4-7 2871045-8 1986 The MCD cell pHi response to abrupt removal of CO2/HCO3 included an initial alkalinization due to rapid CO2 efflux, followed by an acidification due to HCO3 efflux and a gradual recovery to the resting pHi of 7.24 +/- 0.06 partly due to the action of a plasma membrane H+-ATPase. Bicarbonates 51-55 glucose-6-phosphate isomerase Oryctolagus cuniculus 13-16 2871045-8 1986 The MCD cell pHi response to abrupt removal of CO2/HCO3 included an initial alkalinization due to rapid CO2 efflux, followed by an acidification due to HCO3 efflux and a gradual recovery to the resting pHi of 7.24 +/- 0.06 partly due to the action of a plasma membrane H+-ATPase. Bicarbonates 51-55 glucose-6-phosphate isomerase Oryctolagus cuniculus 202-205 2871045-8 1986 The MCD cell pHi response to abrupt removal of CO2/HCO3 included an initial alkalinization due to rapid CO2 efflux, followed by an acidification due to HCO3 efflux and a gradual recovery to the resting pHi of 7.24 +/- 0.06 partly due to the action of a plasma membrane H+-ATPase. Bicarbonates 152-156 glucose-6-phosphate isomerase Oryctolagus cuniculus 13-16 2871045-13 1986 The final pHi recovery required intracellular ATP, which indicated that Cl/HCO3 and H+-ATPase activities are present in the same cells in these suspensions. Bicarbonates 75-79 glucose-6-phosphate isomerase Oryctolagus cuniculus 10-13 3989871-3 1985 In 20 mM HEPES buffered solution, steady state pHi is close to that in control CO2/HCO-3 (25 mM HCO-3, 5% CO2) solution. Bicarbonates 83-88 glucose-6-phosphate isomerase Oryctolagus cuniculus 47-50