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Статті в журналах з теми "PH regulation"

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Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 25 травня 2024

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1

Boron, Walter F. "Regulation of intracellular pH." Advances in Physiology Education 28, no. 4 (December 2004): 160–79. http://dx.doi.org/10.1152/advan.00045.2004.

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The approach that most animal cells employ to regulate intracellular pH (pHi) is not too different conceptually from the way a sophisticated system might regulate the temperature of a house. Just as the heat capacity (C) of a house minimizes sudden temperature (T) shifts caused by acute cold and heat loads, the buffering power (β) of a cell minimizes sudden pHi shifts caused by acute acid and alkali loads. However, increasing C (or β) only minimizes T (or pHi) changes; it does not eliminate the changes, return T (or pHi) to normal, or shift steady-state T (or pHi). Whereas a house may have a furnace to raise T, a cell generally has more than one acid-extruding transporter (which exports acid and/or imports alkali) to raise pHi. Whereas an air conditioner lowers T, a cell generally has more than one acid-loading transporter to lower pHi. Just as a house might respond to graded decreases (or increases) in T by producing graded increases in heat (or cold) output, cells respond to graded decreases (or increases) in pHi with graded increases (or decreases) in acid-extrusion (or acid-loading) rate. Steady-state T (or pHi) can change only in response to a change in chronic cold (or acid) loading or chronic heat (or alkali) loading as produced, for example, by a change in environmental T (or pH) or a change in the kinetics of the furnace (or acid extrudes) or air conditioner (or acid loaders). Finally, just as a temperature-control system might benefit from environmental sensors that provide clues about cold and heat loading, at least some cells seem to have extracellular CO2 or extracellular HCO3− sensors that modulate acid-base transport.

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2

DUNN, JEFF F., and GILLIAN J. WALLEY. "Renal pH regulation in hypertension." Biochemical Society Transactions 19, no. 4 (November 1, 1991): 421S. http://dx.doi.org/10.1042/bst019421s.

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3

Hackam, David J., Sergio Grinstein, and Ori D. Rotstein. "INTRACELLULAR pH REGULATION IN LEUKOCYTES." Shock 5, no. 1 (January 1996): 17–21. http://dx.doi.org/10.1097/00024382-199601000-00005.

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4

Vaughan-Jones, Richard D., Kenneth W. Spitzer, and Pawel Swietach. "Intracellular pH regulation in heart." Journal of Molecular and Cellular Cardiology 46, no. 3 (March 2009): 318–31. http://dx.doi.org/10.1016/j.yjmcc.2008.10.024.

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5

Lacruz, Rodrigo S., Antonio Nanci, Ira Kurtz, J. Timothy Wright, and Michael L. Paine. "Regulation of pH During Amelogenesis." Calcified Tissue International 86, no. 2 (December 17, 2009): 91–103. http://dx.doi.org/10.1007/s00223-009-9326-7.

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6

Flintoft, Louisa. "pH regulation by histone acetylation." Nature Reviews Genetics 14, no. 1 (December 18, 2012): 7. http://dx.doi.org/10.1038/nrg3403.

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7

FELLE, HUBERT H. "pH Regulation in Anoxic Plants." Annals of Botany 96, no. 4 (July 15, 2005): 519–32. http://dx.doi.org/10.1093/aob/mci207.

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8

Dashper, S. G., and E. C. Reynolds. "pH Regulation by Streptococcus mutans." Journal of Dental Research 71, no. 5 (May 1992): 1159–65. http://dx.doi.org/10.1177/00220345920710050601.

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9

Chu, Shaoyou, Shin Tanaka, Jonathan D. Kaunitz, and Marshall H. Montrose. "Dynamic regulation of gastric surface pH by luminal pH." Journal of Clinical Investigation 103, no. 5 (March 1, 1999): 605–12. http://dx.doi.org/10.1172/jci5217.

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10

Dijkstra, J., J. L. Ellis, E. Kebreab, A. B. Strathe, S. López, J. France, and A. Bannink. "Ruminal pH regulation and nutritional consequences of low pH." Animal Feed Science and Technology 172, no. 1-2 (February 2012): 22–33. http://dx.doi.org/10.1016/j.anifeedsci.2011.12.005.

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11

Green, J., D. T. Yamaguchi, C. R. Kleeman, and S. Muallem. "Cytosolic pH regulation in osteoblasts. Regulation of anion exchange by intracellular pH and Ca2+ ions." Journal of General Physiology 95, no. 1 (January 1, 1990): 121–45. http://dx.doi.org/10.1085/jgp.95.1.121.

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Measurements of cytosolic pH (pHi) 36Cl fluxes and free cytosolic Ca2+ concentration ([Ca2+]i) were performed in the clonal osteosarcoma cell line UMR-106 to characterize the kinetic properties of Cl-/HCO3- (OH-) exchange and its regulation by pHi and [Ca2+]i. Suspending cells in Cl(-)-free medium resulted in rapid cytosolic alkalinization from pHi 7.05 to approximately 7.42. Subsequently, the cytosol acidified to pHi 7.31. Extracellular HCO3- increased the rate and extent of cytosolic alkalinization and prevented the secondary acidification. Suspending alkalinized and Cl(-)-depleted cells in Cl(-)-containing solutions resulted in cytosolic acidification. All these pHi changes were inhibited by 4',4',-diisothiocyano-2,2'-stilbene disulfonic acid (DIDS) and H2DIDS, and were not affected by manipulation of the membrane potential. The pattern of extracellular Cl- dependency of the exchange process suggests that Cl- ions interact with a single saturable external site and HCO3- (OH-) complete with Cl- for binding to this site. The dependencies of both net anion exchange and Cl- self-exchange fluxes on pHi did not follow simple saturation kinetics. These findings suggest that the anion exchanger is regulated by intracellular HCO3- (OH-). A rise in [Ca2+]i, whether induced by stimulation of protein kinase C-activated Ca2+ channels, Ca2+ ionophore, or depolarization of the plasma membrane, resulted in cytosolic acidification with subsequent recovery from acidification. The Ca2+-activated acidification required the presence of Cl- in the medium, could be blocked by DIDS, and H2DIDS and was independent of the membrane potential. The subsequent recovery from acidification was absolutely dependent on the initial acidification, required the presence of Na+ in the medium, and was blocked by amiloride. Activation of protein kinase C without a change in [Ca2+]i did not alter pHi. Likewise, in H2DIDS-treated cells and in the absence of Cl-, an increase in [Ca2+]i did not activate the Na+/H+ exchanger in UMR-106 cells. These findings indicate that an increase in [Ca2+]i was sufficient to activate the Cl-/HCO3- exchanger, which results in the acidification of the cytosol. The accumulated H+ in the cytosol activated the Na+/H+ exchanger. Kinetic analysis of the anion exchange showed that at saturating intracellular OH-, a [Ca2+]i increase did not modify the properties of the extracellular site. A rise in [Ca2+]i increased the apparent affinity for intracellular OH- (or HCO3-) of both net anion and Cl- self exchange. These results indicate that [Ca2+]i modifies the interaction of intracellular OH- (or HCO3-) with the proposed regulatory site of the anion exchanger in UMR-106 cells.

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12

Wilder, Logan M., Jonathan R. Thompson, and Richard M. Crooks. "Electrochemical pH regulation in droplet microfluidics." Lab on a Chip 22, no. 3 (2022): 632–40. http://dx.doi.org/10.1039/d1lc00952d.

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13

Almomani, Ensaf, Sumanpreet Kaur, R. Alexander, and Emmanuelle Cordat. "Intercalated Cells: More than pH Regulation." Diseases 2, no. 2 (April 8, 2014): 71–92. http://dx.doi.org/10.3390/diseases2020071.

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14

Felle, Hubert. "Short-term pH regulation in plants." Physiologia Plantarum 74, no. 3 (November 1988): 583–91. http://dx.doi.org/10.1111/j.1399-3054.1988.tb02022.x.

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15

Nordström, Tommy, Ori D. Rotstein, Robert Romanek, Satish Asotra, Johannes N. M. Heersche, Morris F. Manolson, Guy F. Brisseau, and Sergio Grinstein. "Regulation of Cytoplasmic pH in Osteoclasts." Journal of Biological Chemistry 270, no. 5 (February 3, 1995): 2203–12. http://dx.doi.org/10.1074/jbc.270.5.2203.

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16

Balgi, Aruna D., Graham H. Diering, Elizabeth Donohue, Karen K. Y. Lam, Bruno D. Fonseca, Carla Zimmerman, Masayuki Numata, and Michel Roberge. "Regulation of mTORC1 Signaling by pH." PLoS ONE 6, no. 6 (June 29, 2011): e21549. http://dx.doi.org/10.1371/journal.pone.0021549.

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17

Wang, Yuxin, and George R. Stark. "A new STAT3 function: pH regulation." Cell Research 28, no. 11 (October 10, 2018): 1045. http://dx.doi.org/10.1038/s41422-018-0098-3.

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18

Cheng, Li-Jing, and Hsueh-Chia Chang. "Microscale pH regulation by splitting water." Biomicrofluidics 5, no. 4 (December 2011): 046502. http://dx.doi.org/10.1063/1.3657928.

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19

Vlasova, I. I., J. Arnhold, A. N. Osipov, and O. M. Panasenko. "pH-dependent regulation of myeloperoxidase activity." Biochemistry (Moscow) 71, no. 6 (June 2006): 667–77. http://dx.doi.org/10.1134/s0006297906060113.

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20

Janis, Christine M., James G. Napoli, and Daniel E. Warren. "Palaeophysiology of pH regulation in tetrapods." Philosophical Transactions of the Royal Society B: Biological Sciences 375, no. 1793 (January 13, 2020): 20190131. http://dx.doi.org/10.1098/rstb.2019.0131.

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Анотація:

The involvement of mineralized tissues in acid–base homeostasis was likely important in the evolution of terrestrial vertebrates. Extant reptiles encounter hypercapnia when submerged in water, but early tetrapods may have experienced hypercapnia on land due to their inefficient mode of lung ventilation (likely buccal pumping, as in extant amphibians). Extant amphibians rely on cutaneous carbon dioxide elimination on land, but early tetrapods were considerably larger forms, with an unfavourable surface area to volume ratio for such activity, and evidence of a thick integument. Consequently, they would have been at risk of acidosis on land, while many of them retained internal gills and would not have had a problem eliminating carbon dioxide in water. In extant tetrapods, dermal bone can function to buffer the blood during acidosis by releasing calcium and magnesium carbonates. This review explores the possible mechanisms of acid–base regulation in tetrapod evolution, focusing on heavily armoured, basal tetrapods of the Permo-Carboniferous, especially the physiological challenges associated with the transition to air-breathing, body size and the adoption of active lifestyles. We also consider the possible functions of dermal armour in later tetrapods, such as Triassic archosaurs, inferring palaeophysiology from both fossil record evidence and phylogenetic patterns, and propose a new hypothesis relating the archosaurian origins of the four-chambered heart and high systemic blood pressures to the perfusion of the osteoderms. This article is part of the theme issue ‘Vertebrate palaeophysiology’.

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21

BONANNO, JOSEPH A. "Regulation of Corneal Epithelial Intracellular pH." Optometry and Vision Science 68, no. 9 (September 1991): 682–86. http://dx.doi.org/10.1097/00006324-199109000-00002.

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22

Ehrenfeld, J., I. Lacoste, and B. Harvey. "pH Regulation in frog skin epithelium." Comparative Biochemistry and Physiology Part A: Physiology 90, no. 4 (January 1988): 808. http://dx.doi.org/10.1016/0300-9629(88)90706-2.

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23

Aickin, C. C. "Intracellular pH Regulation by Vertebrate Muscle." Annual Review of Physiology 48, no. 1 (October 1986): 349–61. http://dx.doi.org/10.1146/annurev.ph.48.030186.002025.

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24

Boron, W. F. "Intracellular pH Regulation in Epithelial Cells." Annual Review of Physiology 48, no. 1 (October 1986): 377–88. http://dx.doi.org/10.1146/annurev.ph.48.030186.002113.

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25

JUEL, C. "Muscle pH regulation: role of training." Acta Physiologica Scandinavica 162, no. 3 (February 1998): 359–66. http://dx.doi.org/10.1046/j.1365-201x.1998.0305f.x.

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26

Vandenberg, J. I., N. D. Carter, H. W. Bethell, A. Nogradi, Y. Ridderstrale, J. C. Metcalfe, and A. A. Grace. "Carbonic anhydrase and cardiac pH regulation." American Journal of Physiology-Cell Physiology 271, no. 6 (December 1, 1996): C1838—C1846. http://dx.doi.org/10.1152/ajpcell.1996.271.6.c1838.

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Membrane-bound carbonic anhydrase (CA) has recently been identified in mammalian cardiac tissue. In this study, we have investigated the histochemical location and functional role of CA in the ferret heart. Heart sections stained by a modified Hansson's technique showed CA to be located on capillary endothelial membranes as well as on sarcolemmal membranes. In the Langendorff-perfused heart, washout of CO2 brought about by switching perfusion between 25 mM HCO3(-)-5% CO2-buffered solution and nominally HCO3(-)-CO2-free solution caused a transient rise in intracellular pH (pHi) measured by the chemical shift of 2-deoxy-D-glucose 6-phosphate with 31P nuclear magnetic resonance spectroscopy. The initial rate of change of pHi, measured over the first 60-75 s of CO2 efflux, was significantly reduced from 0.41 +/- 0.03 pH units/min (n = 9) in control hearts to 0.28 +/- 0.02 pH units/min (n = 5) in the presence of the membrane-permeable CA inhibitor 6-ethoxzolamide (P < 0.05 compared with control) and to 0.22 +/- 0.04 pH units/min (n = 5) in the presence of the membrane-impermeable CA inhibitor CL-11,366 (P < 0.01 compared with control). After reperfusion of the ischemic myocardium, both CA inhibitors caused a significant slowing of initial rate of change in pH (and initial rate of recovery of contractile function) compared with control hearts. These results suggest that CA, by facilitating the hydration-dehydration of CO2-H2CO3, alters the relative concentrations of CO2 inside and outside the cells, thus enhancing the rate of CO2 transfer from the intracellular to extracellular compartments, which contributes significantly to pHi recovery after reperfusion of the ischemic myocardium.

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27

Juel, C. "Regulation of Muscle pH after Activity." Clinical Science 87, s1 (January 1, 1994): 56–57. http://dx.doi.org/10.1042/cs087s056a.

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28

Knepper, M. A., M. B. Burg, J. Orloff, R. W. Berliner, and F. C. Rector. "Ammonium, urea, and systemic pH regulation." American Journal of Physiology-Renal Physiology 253, no. 1 (July 1, 1987): F199—F202. http://dx.doi.org/10.1152/ajprenal.1987.253.1.f199.

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29

Booth, I. R. "Regulation of cytoplasmic pH in bacteria." Microbiological Reviews 49, no. 4 (1985): 359–78. http://dx.doi.org/10.1128/mmbr.49.4.359-378.1985.

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30

Booth, I. R. "Regulation of cytoplasmic pH in bacteria." Microbiological Reviews 49, no. 4 (1985): 359–78. http://dx.doi.org/10.1128/mr.49.4.359-378.1985.

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31

Bevans, Carville G., and Andrew L. Harris. "Regulation of Connexin Channels by pH." Journal of Biological Chemistry 274, no. 6 (February 5, 1999): 3711–19. http://dx.doi.org/10.1074/jbc.274.6.3711.

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32

Ishida, Yoichi, Smita Nayak, Joseph A. Mindell, and Michael Grabe. "A model of lysosomal pH regulation." Journal of General Physiology 141, no. 6 (May 27, 2013): 705–20. http://dx.doi.org/10.1085/jgp.201210930.

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Lysosomes must maintain an acidic luminal pH to activate hydrolytic enzymes and degrade internalized macromolecules. Acidification requires the vacuolar-type H+-ATPase to pump protons into the lumen and a counterion flux to neutralize the membrane potential created by proton accumulation. Early experiments suggested that the counterion was chloride, and more recently a pathway consistent with the ClC-7 Cl–/H+ antiporter was identified. However, reports that the steady-state luminal pH is unaffected in ClC-7 knockout mice raise questions regarding the identity of the carrier and the counterion. Here, we measure the current–voltage characteristics of a mammalian ClC-7 antiporter, and we use its transport properties, together with other key ion regulating elements, to construct a mathematical model of lysosomal pH regulation. We show that results of in vitro lysosome experiments can only be explained by the presence of ClC-7, and that ClC-7 promotes greater acidification than Cl–, K+, or Na+ channels. Our models predict strikingly different lysosomal K+ dynamics depending on the major counterion pathways. However, given the lack of experimental data concerning acidification in vivo, the model cannot definitively rule out any given mechanism, but the model does provide concrete predictions for additional experiments that would clarify the identity of the counterion and its carrier.

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33

Yamashiro, Darrell J., and Frederick R. Maxfield. "Regulation of endocytic processes by pH." Trends in Pharmacological Sciences 9, no. 6 (June 1988): 190–93. http://dx.doi.org/10.1016/0165-6147(88)90078-8.

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34

Arst, Herbert N., and Miguel A. Peñalva. "Recognizing gene regulation by ambient pH." Fungal Genetics and Biology 40, no. 1 (October 2003): 1–3. http://dx.doi.org/10.1016/s1087-1845(03)00077-x.

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35

Kathagen, Nadine, and Peter Prehm. "Regulation of intracellular pH by glycosaminoglycans." Journal of Cellular Physiology 228, no. 10 (June 20, 2013): 2071–75. http://dx.doi.org/10.1002/jcp.24376.

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36

FitzHarris, Greg, and Jay M. Baltz. "Regulation of intracellular pH during oocyte growth and maturation in mammals." REPRODUCTION 138, no. 4 (October 2009): 619–27. http://dx.doi.org/10.1530/rep-09-0112.

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Regulation of intracellular pH (pHi) is a fundamental homeostatic process essential for the survival and proliferation of virtually all cell types. The mammalian preimplantation embryo, for example, possesses Na+/H+and HCO3−/Cl−exchangers that robustly regulate against acidosis and alkalosis respectively. Inhibition of these transporters prevents pH corrections and, perhaps unsurprisingly, leads to impaired embryogenesis. However, recent studies have revealed that the role and regulation of pHiis somewhat more complex in the case of the developing and maturing oocyte. Small meiotically incompetent growing oocytes are apparently incapable of regulating their own pHi, and instead rely upon the surrounding granulosa cells to correct ooplasmic pH, until such a time that the oocyte has developed the capacity to regulate its own pHi. Later, during meiotic maturation, pHi-regulating activities that were developed during growth are inactivated, apparently under the control of MAPK signalling, until the oocyte is successfully fertilized. Here, we will discuss pH homeostasis in early mammalian development, focussing on recent developments highlighting the unusual and unexpected scenario of pH regulation during oocyte growth and maturation.

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37

Grabe, Michael, and George Oster. "Regulation of Organelle Acidity." Journal of General Physiology 117, no. 4 (March 28, 2001): 329–44. http://dx.doi.org/10.1085/jgp.117.4.329.

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Intracellular organelles have characteristic pH ranges that are set and maintained by a balance between ion pumps, leaks, and internal ionic equilibria. Previously, a thermodynamic study by Rybak et al. (Rybak, S., F. Lanni, and R. Murphy. 1997. Biophys. J. 73:674–687) identified the key elements involved in pH regulation; however, recent experiments show that cellular compartments are not in thermodynamic equilibrium. We present here a nonequilibrium model of lumenal acidification based on the interplay of ion pumps and channels, the physical properties of the lumenal matrix, and the organelle geometry. The model successfully predicts experimentally measured steady-state and transient pH values and membrane potentials. We conclude that morphological differences among organelles are insufficient to explain the wide range of pHs present in the cell. Using sensitivity analysis, we quantified the influence of pH regulatory elements on the dynamics of acidification. We found that V-ATPase proton pump and proton leak densities are the two parameters that most strongly influence resting pH. Additionally, we modeled the pH response of the Golgi complex to varying external solutions, and our findings suggest that the membrane is permeable to more than one dominant counter ion. From this data, we determined a Golgi complex proton permeability of 8.1 × 10−6 cm/s. Furthermore, we analyzed the early-to-late transition in the endosomal pathway where Na,K-ATPases have been shown to limit acidification by an entire pH unit. Our model supports the role of the Na,K-ATPase in regulating endosomal pH by affecting the membrane potential. However, experimental data can only be reproduced by (1) positing the existence of a hypothetical voltage-gated chloride channel or (2) that newly formed vesicles have especially high potassium concentrations and small chloride conductance.

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38

Peral, MJ, ML Calonge, and AA Ilundain. "Intracellular pH regulation in chicken enterocytes: the importance of extracellular pH." Experimental Physiology 80, no. 6 (November 1, 1995): 1001–7. http://dx.doi.org/10.1113/expphysiol.1995.sp003897.

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39

PUTNAM, ROBERT W. "Down-Regulation of pH-Regulating Transport Systems in BC3H-1 Cells." Annals of the New York Academy of Sciences 574, no. 1 Bicarbonate, (December 1989): 354–69. http://dx.doi.org/10.1111/j.1749-6632.1989.tb25170.x.

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40

Boutilier, Robert G., and Ralph A. Ferguson. "Nucleated red cell function: metabolism and pH regulation." Canadian Journal of Zoology 67, no. 12 (December 1, 1989): 2986–93. http://dx.doi.org/10.1139/z89-421.

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The full extent and apportionment of aerobic and anaerobic contributions to energy transduction for membrane pumps associated with cellular pH regulation are very poorly understood. One way of approaching this problem at the cellular level is by using the nucleated erythrocyte as a model cell. Indeed, the aerobic and anaerobic capacity of salmonid erythrocytes and their β-adrenergic mediated pH regulation offers a model "pH regulating system" for examining cellular strategies of response to acute and (or) chronic changes in oxygen availability. Much of our work has focused on the balance between metabolic energy production and the maintenance of erythrocytic pH through primarily or secondarily active ionic exchange mechanisms at the cell membrane. Upon adrenergic stimulation, a rise in cyclic AMP activates the Na+–H+ exchanger, leading to cell alkalinization and an elevation of intracellular Na+. The increased Na+ evidently stimulates Na+,K+-ATPase activity and the increased ATP consumption is matched with aerobic energy production. The pHi that is subsequently established appears to be set by levels of poly anionic phosphates.

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41

Jensen, P. E. "Regulation of antigen presentation by acidic pH." Journal of Experimental Medicine 171, no. 5 (May 1, 1990): 1779–84. http://dx.doi.org/10.1084/jem.171.5.1779.

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The effect of pH on functional association of peptide antigens with APC membranes was investigated by using aldehyde-fixed B cells and class II-restricted T cell hybridomas to assess antigen/MHC complex formation. The results indicated that the rate and extent of functional peptide binding was markedly increased at pH 5.0 as compared with pH 7.3. The pH dependence of binding was preserved after pretreatment of fixed APC with pH 5.0 buffer, suggesting that pH had a direct effect on the interaction of peptide with the APC membrane. Similar results were obtained by using several peptides and I-Ad- and I-Ed-restricted T cells, indicating that pH may be of general importance in regulating the formation of functional antigen/class II MHC complexes.

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42

J. Reshkin, Stephan, Rosa A. Cardone, and Salvador Harguindey. "Na+-H+ Exchanger, pH Regulation and Cancer." Recent Patents on Anti-Cancer Drug Discovery 8, no. 1 (November 1, 2012): 85–99. http://dx.doi.org/10.2174/1574892811308010085.

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Kaunitz, Jonathan, and Yasutada Akiba. "Regulation of extracellular pH by purinergic signalling." Physiology News, Winter 2009 (January 1, 2010): 22–24. http://dx.doi.org/10.36866/pn.77.22.

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Clausen, Torben. "Potassium and Sodium Transport and pH Regulation." Canadian Journal of Physiology and Pharmacology 70, S1 (May 15, 1992): S219—S222. http://dx.doi.org/10.1139/y92-265.

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Анотація:

The excitatory and metabolic events in nervous tissue lead to localized increases in extracellular potassium (K+) and intracellular hydrogen (H+) and calcium (Ca2+) ion concentrations. Even more pronounced increases are seen under pathological conditions and may interfere with the maintenance of cellular function and structure. Most presentations on the second day focussed on these processes and the mechanisms for the clearance of K+, H+, and Ca2+ from intra- or extra-cellular compartments. The essential role of glial cells was a returning theme. Extracellular K+ is transported into cells by the Na–K pump and by two other processes, Na–K–Cl2 cotransport and spatial buffering, which both depend on the operation of the Na–K pump. The clearance of H+ from the cytoplasm and into the extracellular space is mediated by Na+ gradient dependent processes, Na+/H+ antiport, Cl−/HCO3− exchange, and Na+–HCO3− cotransport. Also the clearance of cytoplasmic Ca2+ is to a large extent mediated by a Na+ gradient dependent process, the Na+/Ca2+ antiport. There is a wide divergence between the rates of Na–K pump mediated K+ influx measured in various cultures of glial and neuronal cells. There is a considerable need for systematic comparison between the functional capacity and the concentration of Na–K pumps in cell cultures and intact nervous tissue. It has not yet been ascertained whether K+ transport as measured in cultured astrocytes is representative for K+ transport in the in situ functioning astrocyte. In astrocytes, glutamate was shown to elicit a rapid intercellular propagation of a rise in cytoplasmic Ca2+. In neurons, the elevation of cytoplasmic Ca2+ during exposure to hypoxia, ischemia, or excitatory amino acids was described and related to cell damage. Cytoplasmic Ca2+ may be cleared by Na+/Ca2+ antiport as well as by a Ca2+-activated ATPase in the plasma membrane. The total concentration of this enzyme has not been quantified, and little is known about its energy requirements.Key words: potassium, glial cells, Na–K pump, calcium, sodium.

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Simchowitz, L., and A. Roos. "Regulation of intracellular pH in human neutrophils." Journal of General Physiology 85, no. 3 (March 1, 1985): 443–70. http://dx.doi.org/10.1085/jgp.85.3.443.

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The intracellular pH (pHi) of isolated human peripheral blood neutrophils was measured from the fluorescence of 6-carboxyfluorescein (6-CF) and from the equilibrium distribution of [14C]5,5-dimethyloxazolidine -2,4-dione (DMO). At an extracellular pH (pHo) of 7.40 in nominally CO2-free medium, the steady state pHi using either indicator was approximately 7.25. When pHo was suddenly raised from 7.40 to 8.40 in the nominal absence of CO2, pHi slowly rose by approximately 0.35 during the subsequent hour. A change of similar magnitude in the opposite direction occurred when pHo was reduced to 6.40. Both changes were reversible. Intrinsic intracellular buffering power, determined by using graded pulses of CO2 or NH4Cl, was approximately 50 mM/pH over the pHi range of 6.8-7.9. The course of pHi obtained from the distribution of DMO was followed during and after imposition of intracellular acid and alkaline loads. Intracellular acidification was brought about either by exposing cells to 18% CO2 or by prepulsing with 30 mM NH4Cl, while pHo was maintained at 7.40. In both instances, pHi (6.80 and 6.45, respectively) recovered toward the control value at rates of 0.029 and 0.134 pH/min. These rates were reduced by approximately 90% either by 1 mM amiloride or by replacement of extracellular Na with N-methyl-D-glucamine. Recovery was not affected by 1 mM SITS or by 40 mM alpha-cyano-4-hydroxycinnamate (CHC), which inhibits anion exchange in neutrophils. Therefore, recovery from acid loading is probably due to an exchange of internal H for external Na. Intracellular alkalinization was achieved by exposing the cells to 30 mM NH4Cl or by prepulsing with 18% CO2, both at a constant pHo 7.40. In both instances, pHi, which was 7.65 and 7.76, respectively, recovered to the control value. The recovery rates (0.033 and 0.077 pH/min, respectively) were reduced by 80-90% either by 40 mM CHC or by replacement of extracellular Cl with p-aminohippurate (PAH). SITS, amiloride, and ouabain (0.1 mM) were ineffective.(ABSTRACT TRUNCATED AT 400 WORDS)

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46

Dale, B., Y. Menezo, J. Cohen, L. DiMatteo, and M. Wilding. "Intracellular pH regulation in the human oocyte." Human Reproduction 13, no. 4 (April 1, 1998): 964–70. http://dx.doi.org/10.1093/humrep/13.4.964.

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47

Phillips, K. P. "Intracellular pH regulation in human preimplantation embryos." Human Reproduction 15, no. 4 (April 1, 2000): 896–904. http://dx.doi.org/10.1093/humrep/15.4.896.

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Prasad, Hari, and Rajini Rao. "Histone deacetylase–mediated regulation of endolysosomal pH." Journal of Biological Chemistry 293, no. 18 (March 22, 2018): 6721–35. http://dx.doi.org/10.1074/jbc.ra118.002025.

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49

Shartau, Ryan B., Daniel W. Baker, Dane A. Crossley, and Colin J. Brauner. "Preferential intracellular pH regulation: hypotheses and perspectives." Journal of Experimental Biology 219, no. 15 (August 1, 2016): 2235–44. http://dx.doi.org/10.1242/jeb.126631.

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50

Mathieu, Yves, Jean Guern, Armen Kurkdjian, Pierre Manigault, Jeanne Manigault, Teresa Zielinska, Brigitte Gillet, Jean-Claude Beloeil, and Jean-Yves Lallemand. "Regulation of Vacuolar pH of Plant Cells." Plant Physiology 89, no. 1 (January 1, 1989): 19–26. http://dx.doi.org/10.1104/pp.89.1.19.

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