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Статті в журналах з теми "Proton sensing"

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Автор: Grafiati

Опубліковано: 6 вересня 2023

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1

Mashiko, Misaki, Aya Kurosawa, Yuki Tani, Takashi Tsuji, and Shigeki Takeda. "GPR31 and GPR151 are activated under acidic conditions." Journal of Biochemistry 166, no. 4 (May 23, 2019): 317–22. http://dx.doi.org/10.1093/jb/mvz042.

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Анотація:

Abstract Recent studies have revealed that not only proton-sensing channels, but also one family of G protein-coupled receptors (GPCRs) comprising OGR1, GPR4, G2A and TDAG8 are responsible for the sensing of extracellular protons, or pH. Here, we report that two other GPCRs, GPR31 and GPR151, were also activated in acidic condition. Elevated pH of assay mixtures resulted in a remarkable increase in [35S]GTPγS binding by GPR31–Giα and GPR151–Giα fusion proteins in a narrow range between pH 6 and 5. Our reporter gene assays with CHO cells expressing recombinant GPR31 or GPR151 also showed that activation was maximal at pH ∼5.8. Although these results from in vitro and cellular assays revealed slightly different pH sensitivities, all of our results indicated that GPR31 and GPR151 sensed extracellular protons equally well as other proton-sensing GPCRs.

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2

Sherwood, Thomas W., Erin N. Frey, and Candice C. Askwith. "Structure and activity of the acid-sensing ion channels." American Journal of Physiology-Cell Physiology 303, no. 7 (October 1, 2012): C699—C710. http://dx.doi.org/10.1152/ajpcell.00188.2012.

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Анотація:

The acid-sensing ion channels (ASICs) are a family of proton-sensing channels expressed throughout the nervous system. Their activity is linked to a variety of complex behaviors including fear, anxiety, pain, depression, learning, and memory. ASICs have also been implicated in neuronal degeneration accompanying ischemia and multiple sclerosis. As a whole, ASICs represent novel therapeutic targets for several clinically important disorders. An understanding of the correlation between ASIC structure and function will help to elucidate their mechanism of action and identify potential therapeutics that specifically target these ion channels. Despite the seemingly simple nature of proton binding, multiple studies have shown that proton-dependent gating of ASICs is quite complex, leading to activation and desensitization through distinct structural components. This review will focus on the structural aspects of ASIC gating in response to both protons and the newly discovered activators GMQ and MitTx. ASIC modulatory compounds and their action on proton-dependent gating will also be discussed. This review is dedicated to the memory of Dale Benos, who made a substantial contribution to our understanding of ASIC activity.

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3

Sakata, Souhei, Tatsuki Kurokawa, Morten H. H. Nørholm, Masahiro Takagi, Yoshifumi Okochi, Gunnar von Heijne, and Yasushi Okamura. "Functionality of the voltage-gated proton channel truncated in S4." Proceedings of the National Academy of Sciences 107, no. 5 (December 14, 2009): 2313–18. http://dx.doi.org/10.1073/pnas.0911868107.

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The voltage sensor domain (VSD) is the key module for voltage sensing in voltage-gated ion channels and voltage-sensing phosphatases. Structurally, both the VSD and the recently discovered voltage-gated proton channels (Hv channels) voltage sensor only protein (VSOP) and Hv1 contain four transmembrane segments. The fourth transmembrane segment (S4) of Hv channels contains three periodically aligned arginines (R1, R2, R3). It remains unknown where protons permeate or how voltage sensing is coupled to ion permeation in Hv channels. Here we report that Hv channels truncated just downstream of R2 in the S4 segment retain most channel properties. Two assays, site-directed cysteine-scanning using accessibility of maleimide-reagent as detected by Western blotting and insertion into dog pancreas microsomes, both showed that S4 inserts into the membrane, even if it is truncated between the R2 and R3 positions. These findings provide important clues to the molecular mechanism underlying voltage sensing and proton permeation in Hv channels.

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4

Wobig, Lea, Thérèse Wolfenstetter, Sylvia Fechner, Wolfgang Bönigk, Heinz G. Körschen, Jan F. Jikeli, Christian Trötschel, et al. "A family of hyperpolarization-activated channels selective for protons." Proceedings of the National Academy of Sciences 117, no. 24 (May 28, 2020): 13783–91. http://dx.doi.org/10.1073/pnas.2001214117.

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Proton (H+) channels are special: They select protons against other ions that are up to a millionfold more abundant. Only a few proton channels have been identified so far. Here, we identify a family of voltage-gated “pacemaker” channels, HCNL1, that are exquisitely selective for protons. HCNL1 activates during hyperpolarization and conducts protons into the cytosol. Surprisingly, protons permeate through the channel’s voltage-sensing domain, whereas the pore domain is nonfunctional. Key to proton permeation is a methionine residue that interrupts the series of regularly spaced arginine residues in the S4 voltage sensor. HCNL1 forms a tetramer and thus contains four proton pores. Unlike classic HCN channels, HCNL1 is not gated by cyclic nucleotides. The channel is present in zebrafish sperm and carries a proton inward current that acidifies the cytosol. Our results suggest that protons rather than cyclic nucleotides serve as cellular messengers in zebrafish sperm. Through small modifications in two key functional domains, HCNL1 evolutionarily adapted to a low-Na+freshwater environment to conserve sperm’s ability to depolarize.

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5

Carvacho, Ingrid, I. Scott Ramsey, and David E. Clapham. "Voltage and proton gradient sensing in Hv1 proton channels." Biophysical Journal 96, no. 3 (February 2009): 484a. http://dx.doi.org/10.1016/j.bpj.2008.12.2495.

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6

Osmakov, Dmitry I., Sergey G. Koshelev, Igor A. Ivanov, Yaroslav A. Andreev, and Sergey A. Kozlov. "Endogenous Neuropeptide Nocistatin Is a Direct Agonist of Acid-Sensing Ion Channels (ASIC1, ASIC2 and ASIC3)." Biomolecules 9, no. 9 (August 22, 2019): 401. http://dx.doi.org/10.3390/biom9090401.

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Анотація:

Acid-sensing ion channel (ASIC) channels belong to the family of ligand-gated ion channels known as acid-sensing (proton-gated) ion channels. Only a few activators of ASICs are known. These are exogenous and endogenous molecules that cause a persistent, slowly desensitized current, different from an acid-induced current. Here we describe a novel endogenous agonist of ASICs—peptide nocistatin produced by neuronal cells and neutrophils as a part of prepronociceptin precursor protein. The rat nocistatin evoked currents in X. laevis oocytes expressing rat ASIC1a, ASIC1b, ASIC2a, and ASIC3 that were very similar in kinetic parameters to the proton-gated response. Detailed characterization of nocistatin action on rASIC1a revealed a proton-like dose-dependence of activation, which was accompanied by a dose-dependent decrease in the sensitivity of the channel to the protons. The toxin mambalgin-2, antagonist of ASIC1a, inhibited nocistatin-induced current, therefore the close similarity of mechanisms for ASIC1a activation by peptide and protons could be suggested. Thus, nocistatin is the first endogenous direct agonist of ASICs. This data could give a key to understanding ASICs activation regulation in the nervous system and also could be used to develop new drugs to treat pathological processes associated with ASICs activation, such as neurodegeneration, inflammation, and pain.

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7

Sisignano, Marco, Michael J. M. Fischer, and Gerd Geisslinger. "Proton-Sensing GPCRs in Health and Disease." Cells 10, no. 8 (August 10, 2021): 2050. http://dx.doi.org/10.3390/cells10082050.

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Анотація:

The group of proton-sensing G-protein coupled receptors (GPCRs) consists of the four receptors GPR4, TDAG8 (GPR65), OGR1 (GPR68), and G2A (GPR132). These receptors are cellular sensors of acidification, a property that has been attributed to the presence of crucial histidine residues. However, the pH detection varies considerably among the group of proton-sensing GPCRs and ranges from pH of 5.5 to 7.8. While the proton-sensing GPCRs were initially considered to detect acidic cellular environments in the context of inflammation, recent observations have expanded our knowledge about their physiological and pathophysiological functions and many additional individual and unique features have been discovered that suggest a more differentiated role of these receptors in health and disease. It is known that all four receptors contribute to different aspects of tumor biology, cardiovascular physiology, and asthma. However, apart from their overlapping functions, they seem to have individual properties, and recent publications identify potential roles of individual GPCRs in mechanosensation, intestinal inflammation, oncoimmunological interactions, hematopoiesis, as well as inflammatory and neuropathic pain. Here, we put together the knowledge about the biological functions and structural features of the four proton-sensing GPCRs and discuss the biological role of each of the four receptors individually. We explore all currently known pharmacological modulators of the four receptors and highlight potential use. Finally, we point out knowledge gaps in the biological and pharmacological context of proton-sensing GPCRs that should be addressed by future studies.

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8

Ludwig, Marie-Gabrielle, Miroslava Vanek, Danilo Guerini, Jürg A. Gasser, Carol E. Jones, Uwe Junker, Hans Hofstetter, Romain M. Wolf, and Klaus Seuwen. "Proton-sensing G-protein-coupled receptors." Nature 425, no. 6953 (September 2003): 93–98. http://dx.doi.org/10.1038/nature01905.

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9

Shapira, Barak, Eran Avraham, and Doron Aurbach. "Proton-selective electrode for pH sensing." Electrochemistry Communications 73 (December 2016): 80–84. http://dx.doi.org/10.1016/j.elecom.2016.11.007.

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10

Randolph, Aaron L., Carlos A. Villalba-Galea, and I. Scott Ramsey. "Voltage Sensing in Hv1 Proton Channels." Biophysical Journal 104, no. 2 (January 2013): 207a. http://dx.doi.org/10.1016/j.bpj.2012.11.1173.

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11

Bisikalo, D. V., V. I. Shematovich, J. C. Gérard, M. Meurant, S. B. Mende, and H. U. Frey. "Remote sensing of the proton aurora characteristics from IMAGE-FUV." Annales Geophysicae 21, no. 11 (November 30, 2003): 2165–73. http://dx.doi.org/10.5194/angeo-21-2165-2003.

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Анотація:

Abstract. The combination of simultaneous global images of the north polar region obtained with the IMAGE-FUV imaging system makes it possible to globally map the properties of the electron and proton auroral precipitation. The SI12 imager, which observes the Doppler-shifted Lyman-a emission, provides a global snapshot of the proton aurora every 2 min. These images may be combined with those from the Wide-band Imaging Camera (WIC), to remotely characterize the proton precipitation in proton-dominated auroral structures frequently observed in the afternoon and pre-midnight sectors at the equatorial edge of the auroral oval. It is shown that both the proton energy flux and the mean energy determined by this method are in good agreement with coincident in situ measurement from low altitude satellites carrying proton detectors, when taking into account the different spatial resolution of the two types of observations. Four proton-dominated cases are illustrated in this study. They belong to two categories of proton auroral features: (i) hydrogen arcs known to occur in the evening sector equatorward of the electron oval and (ii) detached proton arcs observed with IMAGE-FUV in the afternoon sector following changes in orientation of the interplanetary magnetic field. They are characterized by a proton flux of 0.5–2 mWm-2 and a mean energy in the range 10–17 keV.Key words. Magnetospheric physics (auroral phenomena; energetic particles, precipitating; magnetopause, cusp, arid boundary layers)

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12

Osmakov, Dmitry I., Sergey G. Koshelev, Ekaterina N. Lyukmanova, Mikhail A. Shulepko, Yaroslav A. Andreev, Peter Illes, and Sergey A. Kozlov. "Multiple Modulation of Acid-Sensing Ion Channel 1a by the Alkaloid Daurisoline." Biomolecules 9, no. 8 (August 2, 2019): 336. http://dx.doi.org/10.3390/biom9080336.

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Анотація:

Acid-sensing ion channels (ASICs) are proton-gated sodium-selective channels that are expressed in the peripheral and central nervous systems. ASIC1a is one of the most intensively studied isoforms due to its importance and wide representation in organisms, but it is still largely unexplored as a target for therapy. In this study, we demonstrated response of the ASIC1a to acidification in the presence of the daurisoline (DAU) ligand. DAU alone did not activate the channel, but in combination with protons, it produced the second peak component of the ASIC1a current. This second peak differs from the sustained component (which is induced by RF-amide peptides), as the second (DAU-induced) peak is completely desensitized, with the same kinetics as the main peak. The co-application of DAU and mambalgin-2 indicated that their binding sites do not overlap. Additionally, we found an asymmetry in the pH activation curve of the channel, which was well-described by a mathematical model based on the multiplied probabilities of protons binding with a pool of high-cooperative sites and a single proton binding with a non-cooperative site. In this model, DAU targeted the pool of high-cooperative sites and, when applied with protons, acted as an inhibitor of ASIC1a activation. Moreover, DAU’s occupation of the same binding site most probably reverses the channel from steady-state desensitization in the pH 6.9–7.3 range. DAU features disclose new opportunities in studies of ASIC structure and function.

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13

Glitsch, Maike. "Protons and Ca2+: Ionic Allies in Tumor Progression?" Physiology 26, no. 4 (August 2011): 252–65. http://dx.doi.org/10.1152/physiol.00005.2011.

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Ion channels and G-protein-coupled receptors (GPCRs) play a fundamental role in cancer progression by influencing Ca2+influx and signaling pathways in transformed cells. Transformed cells thrive in a hostile environment that is characterized by extracellular acidosis that promotes the pathological phenotype. The pathway(s) by which extracellular protons achieve this remain unclear. Here, a role for proton-sensing ion channels and GPCRs as mediators of the effects of extracellular protons in cancer cells is discussed.

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14

Mercado, Francisco, Iván A. López, Dora Acuna, Rosario Vega, and Enrique Soto. "Acid-Sensing Ionic Channels in the Rat Vestibular Endorgans and Ganglia." Journal of Neurophysiology 96, no. 3 (September 2006): 1615–24. http://dx.doi.org/10.1152/jn.00378.2006.

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Acid-sensing ionic channels (ASICs) are members of the epithelial Na+ channel/degenerin (ENaC/DEG) superfamily. ASICs are widely distributed in the central and peripheral nervous system. They have been implicated in synaptic transmission, pain perception, and the mechanoreception in peripheral tissues. Our objective was to characterize proton-gated currents mediated by ASICs and to determine their immunolocation in the rat vestibular periphery. Voltage clamp of cultured afferent neurons from P7 to P10 rats showed a proton-gated current with rapid activation and complete desensitization, which was carried almost exclusively by sodium ions. The current response to protons (H+) has a pH0.5 of 6.2. This current was reversibly decreased by amiloride, gadolinium, lead, acetylsalicylic acid, and enhanced by FMRFamide and zinc, and negatively modulated by raising the extracellular calcium concentration. Functional expression of the current was correlated with smaller-capacitance neurons. Acidification of the extracellular pH generated action potentials in vestibular neurons, suggesting a functional role of ASICs in their excitability. Immunoreactivity to ASIC1a and ASIC2a subunits was found in small vestibular ganglion neurons and afferent fibers that run throughout the macula utricle and crista stroma. ASIC2b, ASIC3, and ASIC4 were expressed to a lesser degree in vestibular ganglion neurons. The ASIC1b subunit was not detected in the vestibular endorgans. No acid-pH–sensitive currents or ASIC immunoreactivity was found in hair cells. Our results indicate that proton-gated current is carried through ASICs and that ionic current activated by H+ contributes to shape the vestibular afferent neurons' response to its synaptic input.

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15

Vitali, Victoria, Cintia Jozefkowicz, Agustina Canessa Fortuna, Gabriela Soto, F. Luis González Flecha, and Karina Alleva. "Cooperativity in proton sensing by PIP aquaporins." FEBS Journal 286, no. 5 (December 3, 2018): 991–1002. http://dx.doi.org/10.1111/febs.14701.

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16

Traverso, Sonia, Giovanni Zifarelli, Rita Aiello, and Michael Pusch. "Proton Sensing of CLC-0 Mutant E166D." Journal of General Physiology 127, no. 1 (December 27, 2005): 51–66. http://dx.doi.org/10.1085/jgp.200509340.

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CLC Cl− channels are homodimers in which each subunit has a proper pore and a (fast) gate. An additional slow gate acts on both pores. A conserved glutamate (E166 in CLC-0) is a major determinant of gating in CLC-0 and is crucially involved in Cl−/H+ antiport of CLC-ec1, a CLC of known structure. We constructed tandem dimers with one wild-type (WT) and one mutant subunit (E166A or E166D) to show that these mutations of E166 specifically alter the fast gate of the pore to which they belong without effect on the fast gate of the neighboring pore. In addition both mutations activate the common slow gate. E166A pores have a large, voltage-independent open probability of the fast gate (popen), whereas popen of E166D pores is dramatically reduced. Similar to WT, popen of E166D was increased by lowering pHint. At negative voltages, E166D presents a persistent inward current that is blocked by p-chlorophenoxy-acetic acid (CPA) and increased at low pHext. The pHext dependence of the persistent current is analogous to a similar steady inward current in WT CLC-0. Surprisingly, however, the underlying unitary conductance of the persistent current in E166D is about an order of magnitude smaller than that of the transient deactivating inward Cl− current. Collectively, our data support the possibility that the mutated CLC-0 channel E166D can assume two distinct open states. Voltage-independent protonation of D166 from the outside favors a low conductance state, whereas protonation from the inside favors the high conductance state.

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17

DeCoursey, Thomas E. "Voltage and pH sensing by the voltage-gated proton channel, H V 1." Journal of The Royal Society Interface 15, no. 141 (April 2018): 20180108. http://dx.doi.org/10.1098/rsif.2018.0108.

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Анотація:

Voltage-gated proton channels are unique ion channels, membrane proteins that allow protons but no other ions to cross cell membranes. They are found in diverse species, from unicellular marine life to humans. In all cells, their function requires that they open and conduct current only under certain conditions, typically when the electrochemical gradient for protons is outwards. Consequently, these proteins behave like rectifiers, conducting protons out of cells. Their activity has electrical consequences and also changes the pH on both sides of the membrane. Here we summarize what is known about the way these proteins sense the membrane potential and the pH inside and outside the cell. Currently, it is hypothesized that membrane potential is sensed by permanently charged arginines (with very high p K a ) within the protein, which results in parts of the protein moving to produce a conduction pathway. The mechanism of pH sensing appears to involve titratable side chains of particular amino acids. For this purpose their p K a needs to be within the operational pH range. We propose a ‘counter-charge’ model for pH sensing in which electrostatic interactions within the protein are selectively disrupted by protonation of internally or externally accessible groups.

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18

Kariev, Alisher M., and Michael E. Green. "Protons in Gating the Kv1.2 Channel: A Calculated Set of Protonation States in Response to Polarization/Depolarization of the Channel, with the Complete Proposed Proton Path from Voltage Sensing Domain to Gate." Membranes 12, no. 7 (July 20, 2022): 718. http://dx.doi.org/10.3390/membranes12070718.

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We have in the past proposed that proton motion constitutes the gating current in the potassium channel Kv1.2 and is responsible for the gating mechanism. For this to happen, there must be a proton path between the voltage-sensing domain (VSD) and the channel gate, and here we present quantum calculations that lead to a specific pair of proton paths, defined at the molecular level, with well-defined water molecule linkages, and with hydrogen bonding between residues; there is also at least one interpath crossover, where protons can switch paths. Quantum calculations on the entire 563-atom system give the complete geometry, the energy, and atomic charges. Calculations show that three specific residues (in the pdb 3Lut numbering, H418, E327, R326), and the T1 intracellular moiety, all of which have been shown experimentally to be involved in gating, would necessarily be protonated or deprotonated in the path between the VSD and the gate. Hydroxyl reorientation of serine and threonine residues are shown to provide a means of adjusting proton directions of motion. In the deprotonated state for K312, a low energy state, our calculations come close to reproducing the X-ray structure. The demonstration of the existence of a double proton path between VSD and gate supports the proposed proton gating mechanism; when combined with our earlier demonstration of proton generation in the VSD, and comparison with other systems that are known to move protons, we are close to achieving the definition of a complete gating mechanism in molecular detail. The coupling of the paths to the VSD, and to the PVPV section that essentially forms the gate, can be easily seen from the results of the calculation. The gate itself remains for further computations.

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19

DeCoursey, Thomas E. "Voltage-Gated Proton Channels Find Their Dream Job Managing the Respiratory Burst in Phagocytes." Physiology 25, no. 1 (February 2010): 27–40. http://dx.doi.org/10.1152/physiol.00039.2009.

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Анотація:

The voltage-gated proton channel bears surprising resemblance to the voltage-sensing domain (S1–S4) of other voltage-gated ion channels but is a dimer with two conduction pathways. The proton channel seems designed for efficient proton extrusion from cells. In phagocytes, it facilitates the production of reactive oxygen species by NADPH oxidase.

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20

Wang, Ju-Qiang, Junko Kon, Chihiro Mogi, Masayuki Tobo, Alatangaole Damirin, Koichi Sato, Mayumi Komachi, et al. "TDAG8 Is a Proton-sensing and Psychosine-sensitive G-protein-coupled Receptor." Journal of Biological Chemistry 279, no. 44 (August 23, 2004): 45626–33. http://dx.doi.org/10.1074/jbc.m406966200.

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Анотація:

T cell death-associated gene 8 (TDAG8) has been reported to be a receptor for psychosine. Ovarian cancer G-protein-coupled receptor 1 (OGR1) and GPR4, G-protein-coupled receptors (GPCRs) closely related to TDAG8, however, have recently been identified as proton-sensing or extracellular pH-responsive GPCRs that stimulate inositol phosphate and cAMP production, respectively. In the present study, we examined whether TDAG8 senses extracellular pH change. In the several cell types that were transfected with TDAG8 cDNA, cAMP was markedly accumulated in response to neutral to acidic extracellular pH, with a peak response at approximately pH 7.0–6.5. The pH effect was inhibited by copper ions and was reduced or lost in cells expressing mutated TDAG8 in which histidine residues were changed to phenylalanine. In the membrane fractions prepared from TDAG8-transfected cells, guanosine 5′-O-(3-thiotriphosphate) binding activity and adenylyl cyclase activity were remarkably stimulated in response to neutral and acidic pH. The concentration-dependent effect of extracellular protons on cAMP accumulation was shifted to the right in the presence of psychosine. The inhibitory psychosine effect was also observed for pH-dependent actions in OGR1- and GPR4-expressing cells but not for prostaglandin E2- and sphingosine 1-phosphate-induced actions in any pH in native and sphingosine 1-phosphate receptor-expressing cells. Glucosylsphingosine and sphingosylphosphorylcholine similarly inhibited the pH-dependent action, although to a lesser extent. Psychosine-sensitive and pH-dependent cAMP accumulation was also observed in mouse thymocytes. We concluded that TDAG8 is one of the proton-sensing GPCRs coupling to adenylyl cyclase and psychosine, and its related lysosphingolipids behave as if they were antagonists against protein-sensing receptors, including TDAG8, GPR4, and OGR1.

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21

Christensen, Burgess N., Mikhail Kochukov, Terry A. McNearney, Giulio Taglialatela, and Karin N. Westlund. "Proton-sensing G protein-coupled receptor mobilizes calcium in human synovial cells." American Journal of Physiology-Cell Physiology 289, no. 3 (September 2005): C601—C608. http://dx.doi.org/10.1152/ajpcell.00039.2005.

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Анотація:

Lowered extracellular pH in a variety of tissues is associated with increased tissue destruction and initiation of inflammatory processes. Although the acid-sensing receptors described previously are ion channels, we describe a G protein-coupled proton-sensitive receptor that stimulates Ca2+ release from intracellular stores in a tumor-derived synoviocyte cell line (SW982) and in primary cultures of human synovial cells from patients with inflammatory arthropathies. We established a link between proton-dependent receptor activation and intracellular Ca2+ mobilization by demonstrating 1) dependence on the integrity of the intracellular Ca2+ store, 2) independence from extracellular Ca2+, and 3) proton-induced production of inositol phosphate and 4) by abolishing the effect with GTPase inhibitors. We propose that this G protein-coupled acid-sensing receptor linked to intracellular Ca2+ mobilization in synoviocytes can contribute to downstream inflammatory and cellular proliferative processes in synovial fibroblasts. The acid-sensing receptor has distinct characteristics as a metabotropic G protein-coupled receptor on human synoviocytes in this emerging new class of receptors.

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22

El Chemaly, Antoun, Yoshifumi Okochi, Mari Sasaki, Serge Arnaudeau, Yasushi Okamura, and Nicolas Demaurex. "VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification." Journal of Experimental Medicine 207, no. 1 (December 21, 2009): 129–39. http://dx.doi.org/10.1084/jem.20091837.

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Анотація:

Neutrophils kill microbes with reactive oxygen species generated by the NADPH oxidase, an enzyme which moves electrons across membranes. Voltage-gated proton channels (voltage-sensing domain only protein [VSOP]/Hv1) are required for high-level superoxide production by phagocytes, but the mechanism of this effect is not established. We show that neutrophils from VSOP/Hv1−/− mice lack proton currents but have normal electron currents, indicating that these cells have a fully functional oxidase that cannot conduct protons. VSOP/Hv1−/− neutrophils had a more acidic cytosol, were more depolarized, and produced less superoxide and hydrogen peroxide than neutrophils from wild-type mice. Hydrogen peroxide production was rescued by providing an artificial conductance with gramicidin. Loss of VSOP/Hv1 also aborted calcium responses to chemoattractants, increased neutrophil spreading, and decreased neutrophil migration. The migration defect was restored by the addition of a calcium ionophore. Our findings indicate that proton channels extrude the acid and compensate the charge generated by the oxidase, thereby sustaining calcium entry signals that control the adhesion and motility of neutrophils. Loss of proton channels thus aborts superoxide production and causes a severe signaling defect in neutrophils.

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23

Okasha, Rawda M. "Proton Sensing Color Changing Organoiron and Organic Macromolecules." Journal of Inorganic and Organometallic Polymers and Materials 25, no. 3 (February 17, 2015): 354–66. http://dx.doi.org/10.1007/s10904-015-0193-6.

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24

Zhu, X., E. Mose, S. Hogan, and N. Zimmermann. "Proton-sensing Receptor GPR65 Regulates Allergic Gastrointestinal Eosinophilia." Journal of Allergy and Clinical Immunology 129, no. 2 (February 2012): AB245. http://dx.doi.org/10.1016/j.jaci.2011.12.051.

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25

Knight, Harold K. "Auroral ionospheric E region parameters obtained from satellite- based far-ultraviolet and ground-based ionosonde observations – effects of proton precipitation." Annales Geophysicae 39, no. 1 (January 28, 2021): 105–18. http://dx.doi.org/10.5194/angeo-39-105-2021.

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Abstract. Coincident auroral far-ultraviolet (FUV) and ground-based ionosonde observations are compared for the purpose of determining whether auroral FUV remote sensing algorithms that assume pure electron precipitation are biased in the presence of proton precipitation. Auroral particle transport and optical emission models, such as the Boltzmann 3-Constituent (B3C) model, predict that maximum E region electron density (NmE) values derived from auroral Lyman–Birge–Hopfield (LBH) emissions, assuming electron precipitation, will be biased by up to ∼20 % (high) for pure proton aurora, while comparisons between LBH radiances and radiances derived from in situ particle flux observations (i.e., Knight et al., 2008, 2012) indicate that the bias associated with proton aurora should be much larger. Surprisingly, in the comparisons with ionosonde observations described here, no bias associated with proton aurora is found in FUV-derived auroral NmE, which means that auroral FUV remote sensing methods for NmE are more accurate in the presence of proton precipitation than was suggested in the aforementioned earlier works. Possible explanations for the discrepancy with the earlier results are discussed.

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26

Posson, David J., Ameer N. Thompson, Jason G. McCoy, and Crina M. Nimigean. "Molecular interactions involved in proton-dependent gating in KcsA potassium channels." Journal of General Physiology 142, no. 6 (November 11, 2013): 613–24. http://dx.doi.org/10.1085/jgp.201311057.

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The bacterial potassium channel KcsA is gated open by the binding of protons to amino acids on the intracellular side of the channel. We have identified, via channel mutagenesis and x-ray crystallography, two pH-sensing amino acids and a set of nearby residues involved in molecular interactions that influence gating. We found that the minimal mutation of one histidine (H25) and one glutamate (E118) near the cytoplasmic gate completely abolished pH-dependent gating. Mutation of nearby residues either alone or in pairs altered the channel’s response to pH. In addition, mutations of certain pairs of residues dramatically increased the energy barriers between the closed and open states. We proposed a Monod–Wyman–Changeux model for proton binding and pH-dependent gating in KcsA, where H25 is a “strong” sensor displaying a large shift in pKa between closed and open states, and E118 is a “weak” pH sensor. Modifying model parameters that are involved in either the intrinsic gating equilibrium or the pKa values of the pH-sensing residues was sufficient to capture the effects of all mutations.

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27

Phan, Thi Tuong Vy. "Gating Mechanism of Hv1 Studied by Molecular Dynamic Simulations." Materials Proceedings 4, no. 1 (November 11, 2020): 20. http://dx.doi.org/10.3390/iocn2020-07862.

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The voltage-gated proton channel (Hv1) plays the important role in proton extrusion, pH homeostasis, sperm motility, and cancer progression. The closed-state structure of Hv1 was recently revealed by X-ray crystallography. However, the opened-state structure has not been captured yet. To investigate the mechanism of proton transfer in Hv1, molecular dynamics (MD) simulations were performed with the closed-state structure of Hv1 under electric field and pH conditions. The residues arrangement on the closed-state structure revealed that the selectivity filter (Asp108) which is located in the hydrophobic layer (consists of two Phe residues 146 and 179) might prevent water penetration. In molecular dynamics simulations, we observed that the channel opened by moving 3 Arg up on the S4 helix and a continuous hydrogen-bonded chain of water molecules (a “water wire”) went through the channel when it opened. During simulations, the open channel allowed water molecules to pass through the channel but excluded other ions. This indicates the Hv1 channel is highly selective for protons. Our results clearly showed the Hv1 channel is voltage-and pH-gradient sensing.

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28

Singh, Harpreet, Vijay K. Tomer, Nityasagar Jena, Indu Bala, Nidhi Sharma, Devadutta Nepak, Abir De Sarkar, Kamalakannan Kailasam, and Santanu Kumar Pal. "A porous, crystalline truxene-based covalent organic framework and its application in humidity sensing." J. Mater. Chem. A 5, no. 41 (2017): 21820–27. http://dx.doi.org/10.1039/c7ta05043g.

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29

Malik, Ritu, Vijay K. Tomer, Vandna Chaudhary, Manjeet S. Dahiya, Anshu Sharma, S. P. Nehra, Surender Duhan, and Kamalakannan Kailasam. "An excellent humidity sensor based on In–SnO2 loaded mesoporous graphitic carbon nitride." Journal of Materials Chemistry A 5, no. 27 (2017): 14134–43. http://dx.doi.org/10.1039/c7ta02860a.

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30

John, Scott, Brian Kim, Riccardo Olcese, Joshua I. Goldhaber, and Michela Ottolia. "Proton Sensitivity of NCX: Modulation by Na, Ca and a Distinct Proton-Sensing Domain." Biophysical Journal 112, no. 3 (February 2017): 275a. http://dx.doi.org/10.1016/j.bpj.2016.11.1488.

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31

Takeshita, Kohei, Souhei Sakata, Eiki Yamashita, Yuichiro Fujiwara, Yasushi Okamura, and Atsushi Nakagawa. "X-ray crystal structure of voltage-gated proton channel." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1501. http://dx.doi.org/10.1107/s2053273314084988.

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The voltage-gated proton channel, Hv1 (VSOP) has a voltage-sensor domain (VSD) but lacks an authentic pore domain, and the VSD of Hv1 plays dual roles of voltage sensing and proton permeation. Hv1 is required for high-level superoxide production by phagocytes through its tight functional coupling with NADPH oxidase to eliminate pathogens. Hv1 is also expressed in human sperm and has been suggested to regulate motility through activating pH-sensitive calcium channels. The activities of Hv1 also have pathological implications, such as exacerbation of ischemic brain damage and progression of cancer. In this study, our crystal structure of mouse Hv1 (mHv1) showed a "closed umbrella" shape with a long helix consisting of the cytoplasmic coiled-coil and the voltage-sensing helix, S4, and featured a wide inner-accessible vestibule. We also found a Zn2+ion at the extracellular region of mHv1 protomer. The binding of Zn2+strongly suggested that the crystal structure of mHv1 represents the resting state, since Zn2+specifically inhibits activities of voltage-gated proton channels. Actually, two out of three arginines as sensor residues (R204 and R207) were located lower than the conserved phenylalanine, F146, on the S2 in a charge transfer center. This makes contrast with previous structures of other VSDs in the activated state where many positive residues of S4 were located upper than the conserved phenylalanine. Additionally, the crystal structure of mHv1 highlighted two hydrophobic barriers. Aspartic acid (D108), which is critical for proton selective permeation, was located facing intracellular vestibule below the inner hydrophobic barrier, thereby being accessible to water from the cytoplasm. Another hydrophobic layer of extracellular side probably ensures interruption of the proton pathway of mHv1 in resting state. These findings provide a novel platform for understanding the general principles of voltage sensing and proton permeation.

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32

Mazumdar, Prativa, Samir Maity, Milan Shyamal, Debasish Das, Gobinda Prasad Sahoo, and Ajay Misra. "Proton triggered emission and selective sensing of picric acid by the fluorescent aggregates of 6,7-dimethyl-2,3-bis-(2-pyridyl)-quinoxaline." Physical Chemistry Chemical Physics 18, no. 10 (2016): 7055–67. http://dx.doi.org/10.1039/c5cp05827a.

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33

Zhang, Yuwei, Qikun Sun, Zhongping Li, Yongfeng Zhi, He Li, Ziping Li, Hong Xia, and Xiaoming Liu. "Light-emitting conjugated microporous polymers based on an excited-state intramolecular proton transfer strategy and selective switch-off sensing of anions." Materials Chemistry Frontiers 4, no. 10 (2020): 3040–46. http://dx.doi.org/10.1039/d0qm00384k.

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34

Burgoyne, Edward D., Andrés F. Molina-Osorio, Reza Moshrefi, Rachel Shanahan, Gerard P. McGlacken, Talia Jane Stockmann, and Micheál D. Scanlon. "Detection of Pseudomonas aeruginosa quorum sensing molecules at an electrified liquid|liquid micro-interface through facilitated proton transfer." Analyst 145, no. 21 (2020): 7000–7008. http://dx.doi.org/10.1039/d0an01245a.

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35

Boonstra, Eger, Hiroaki Hatano, Yuji Miyahara, Satoshi Uchida, Tatsuro Goda, and Horacio Cabral. "A proton/macromolecule-sensing approach distinguishes changes in biological membrane permeability during polymer/lipid-based nucleic acid delivery." Journal of Materials Chemistry B 9, no. 21 (2021): 4298–302. http://dx.doi.org/10.1039/d1tb00645b.

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36

Villalba-Galea, Carlos A., Ludivine Frezza, Walter Sandtner, and Francisco Bezanilla. "Sensing charges of the Ciona intestinalis voltage-sensing phosphatase." Journal of General Physiology 142, no. 5 (October 14, 2013): 543–55. http://dx.doi.org/10.1085/jgp.201310993.

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Voltage control over enzymatic activity in voltage-sensitive phosphatases (VSPs) is conferred by a voltage-sensing domain (VSD) located in the N terminus. These VSDs are constituted by four putative transmembrane segments (S1 to S4) resembling those found in voltage-gated ion channels. The putative fourth segment (S4) of the VSD contains positive residues that likely function as voltage-sensing elements. To study in detail how these residues sense the plasma membrane potential, we have focused on five arginines in the S4 segment of the Ciona intestinalis VSP (Ci-VSP). After implementing a histidine scan, here we show that four arginine-to-histidine mutants, namely R223H to R232H, mediate voltage-dependent proton translocation across the membrane, indicating that these residues transit through the hydrophobic core of Ci-VSP as a function of the membrane potential. These observations indicate that the charges carried by these residues are sensing charges. Furthermore, our results also show that the electrical field in VSPs is focused in a narrow hydrophobic region that separates the extracellular and intracellular space and constitutes the energy barrier for charge crossing.

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37

Kottke, Tilman, Aihua Xie, Delmar S. Larsen, and Wouter D. Hoff. "Photoreceptors Take Charge: Emerging Principles for Light Sensing." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 291–313. http://dx.doi.org/10.1146/annurev-biophys-070317-033047.

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The first stage in biological signaling is based on changes in the functional state of a receptor protein triggered by interaction of the receptor with its ligand(s). The light-triggered nature of photoreceptors allows studies on the mechanism of such changes in receptor proteins using a wide range of biophysical methods and with superb time resolution. Here, we critically evaluate current understanding of proton and electron transfer in photosensory proteins and their involvement both in primary photochemistry and subsequent processes that lead to the formation of the signaling state. An insight emerging from multiple families of photoreceptors is that ultrafast primary photochemistry is followed by slower proton transfer steps that contribute to triggering large protein conformational changes during signaling state formation. We discuss themes and principles for light sensing shared by the six photoreceptor families: rhodopsins, phytochromes, photoactive yellow proteins, light-oxygen-voltage proteins, blue-light sensors using flavin, and cryptochromes.

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38

Stankovic, Srboljub, Radovan Ilic, Milos Davidovic, Milojko Kovacevic, and Dragomir Davidovic. "Influence of packaging configuration with kovar lid on RADFET response to proton irradiation." Nuclear Technology and Radiation Protection 23, no. 1 (2008): 37–40. http://dx.doi.org/10.2298/ntrp0801037s.

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Radiation sensing MOSFETs (RADFETs) have found numerous applications in space research, as well as in nuclear technology and research, and radiotherapy. Since proton irradiation is an essential part of the space radiation environment, it is important to know RADFET proton response precisely. In this work a numerical simulation of RADFET proton response is performed. To this end the proton transport Monte Carlo software SRNA-2K5, developed by one of the authors, has been adapted to obtain the energy deposited in the RADFET structure and dose distribution within the microscopic dimensions of the dosimeter sensitive volume. Our results show that RADFET response to proton irradiation depends significantly of packaging configurations with kovar lid.

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39

Ishikita, Hiroshi. "Proton-Binding Sites of Acid-Sensing Ion Channel 1." PLoS ONE 6, no. 2 (February 14, 2011): e16920. http://dx.doi.org/10.1371/journal.pone.0016920.

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40

Waldmann, Rainer, Guy Champigny, Frédéric Bassilana, Catherine Heurteaux, and Michel Lazdunski. "A proton-gated cation channel involved in acid-sensing." Nature 386, no. 6621 (March 1997): 173–77. http://dx.doi.org/10.1038/386173a0.

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41

Li, Haibin, Dongliang Jin, Qingchun Yu, and Hengyong Tu. "Optical humidity sensing, proton-conducting sol–gel glass monolith." Journal of Power Sources 196, no. 8 (April 2011): 3836–40. http://dx.doi.org/10.1016/j.jpowsour.2011.01.004.

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42

Bush, Diana L., and Garry A. Rechnitz. "Antibody sensing polymer membrane electrode using a proton carrier." Fresenius' Zeitschrift für analytische Chemie 323, no. 5 (January 1986): 491. http://dx.doi.org/10.1007/bf00470768.

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43

Tang, Xiling, Zhi Xu, Adam Trontz, Wenheng Jing, and Junhang Dong. "Proton-Conducting Nanocrystalline Ceramics for High-Temperature Hydrogen Sensing." Metallurgical and Materials Transactions E 1, no. 1 (January 25, 2014): 48–57. http://dx.doi.org/10.1007/s40553-014-0008-7.

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44

Ramaswamy, Swarna S., David M. MacLean, Alemayehu A. Gorfe, and Vasanthi Jayaraman. "Proton Mediated Conformational Changes in ACID Sensing Ion Channel1a." Biophysical Journal 106, no. 2 (January 2014): 152a. http://dx.doi.org/10.1016/j.bpj.2013.11.876.

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45

Polak, A. J., S. Petty-weeks, and A. J. Beuhler. "Applications of novel proton-conducting polymers to hydrogen sensing." Sensors and Actuators 9, no. 1 (February 1986): 1–7. http://dx.doi.org/10.1016/0250-6874(86)80001-4.

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46

Matsumura, Midori, Yusuke Daiko, and Masayuki Nogami. "Hydrogen-Sensor Prepared Using Proton-Conducting Glass Films." Solid State Phenomena 124-126 (June 2007): 627–30. http://dx.doi.org/10.4028/www.scientific.net/ssp.124-126.627.

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Solid-state potentiometric thin film hydrogen gas sensors were successfully fabricated using a sol-gel-derived high proton-conducting P2O5-SiO2 glass films. Manganese oxide thin film coated on an indium tin oxide (ITO)-coated glass substrate was used for reference electrode. The sensor exhibited high speed responsibility within 10 s and 120 s at 30 oC and -30oC, respectively, for 1 vol.% hydrogen gas. A linear relationship between the electromotive force (EMF) and the logarithmic hydrogen concentration of 0.1~1 vol.% was obtained in the temperature ranging from -30 to 30 oC. The sensing mechanism was also discussed to improve the sensitivity and sensing speed against low H2 concentration at low temperatures.

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47

Wu, Zhao-Feng, Zhi-Hua Fu, Ever Velasco, Kai Xing, Hao Wang, Guo-Dong Zou, Xiao-Ying Huang, and Jing Li. "A robust and multifunctional calcium coordination polymer as a selective fluorescent sensor for acetone and iron (+3) and as a tunable proton conductor." Journal of Materials Chemistry C 8, no. 47 (2020): 16784–89. http://dx.doi.org/10.1039/d0tc04371k.

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48

He, Xiaofei, Mark Wunderlich, Benjamin Mizukawa, James C. Mulloy, Saran Feng, Lauren Lawley, Caleb Hawkins, et al. "Proton Sensor GPR68 Is Essential to Maintain Myeloid Malignancies." Blood 132, Supplement 1 (November 29, 2018): 1353. http://dx.doi.org/10.1182/blood-2018-99-110399.

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Abstract Despite the improvement of chemotherapy and targeted therapy, drug resistance still remains a challenge for long term disease free survival in aggressive leukemia patients. Recently, enhanced glycolysis is observed in acute myeloid leukemia (AML), and in association with poor clinical outcomes and chemoresistance. The byproducts of glycolysis include lactate and protons (H+), which contribute to intracellular acidosis. The extrusion of protons further results in extracellular acidosis. A group of G protein-coupled receptors (GPCRs), including GPR4, GPR65 (TDAG8), GPR68 (OGR1) and GPR132 (G2A), have been demonstrated to respond to extracellular acidosis, resulting in activation of downstream signaling pathways that regulate pleotropic cellular processes. However, it remains unclear whether these proton-sensing GPCRs contribute to the etiology of AML. Here, we performed genomic examination of leukemia (via cBioPortal). Among 660 leukemia patients, only one patient exhibited deletion of GPR132. Other than this single case, we found no genetic mutations or cytogenetic abnormalities pertaining to proton-sensing GPCRs. Examination of transcripts of these proton-sensing GPCRs revealed that GPR68 was upregulated in both pediatric and adult AML. AML patients with higher levels of GPR68 were associated with shorter overall survival. To understand the function of GPR68 in AML, we knocked down GPR68 in AML cell lines with shRNA targeting GPR68 (shGPR68). GPR68 knockdown markedly induced apoptosis, and reduced colony formation and proliferation in AML cells. This result indicates that myeloid malignancies acquire a dependency on GPR68 function. In response to extracellular H+ or overexpression, GPR68 activates Ca2+ pathway. To determine the molecular mechanism by which GPR68 overexpression supports leukemia cell growth and survival, we examined the intracellular Ca2+ levels (i.e. [Ca2+]i) in primary AML samples. Compared with CD34+ normal hematopoietic cells, all primary AML specimens tested exhibited increased [Ca2+]i, consistent with GPR68 overexpression in AML cells. Meanwhile, shGPR68 reduced [Ca2+]i in all AML cell lines tested, indicating that overexpressed GPR68 activates the Ca2+ pathway in AML. Given that enhanced glycolysis leads to extracellular acidosis, we tested whether glycolysis-mediated local acidosis could also explain enhanced GPR68 activation in AML. Indeed, inhibition of glycolysis by 2-deoxyglucose (2-DG) reduced [Ca2+]i in most of the AML cell lines tested, indicating that glycolysis is likely responsible for enhanced GPR68 activation in AML as well. Next, we attempted to identify the Ca2+-dependent molecular mechanism that mediates the prosurvival effects due to GPR68 activation. We screened a series of pharmacological inhibitors for their efficacy in reducing cell growth and inducing apoptosis. Among the inhibitors tested, only a calcineurin (CaN) inhibitor, Cyclosporine, dramatically reduced cell growth and induced apoptosis in AML cells. This finding raises the possibility that GPR68 promotes AML cell survival through activating the Gq/11/Ca2+/CaN pathway. In summary, we find that the myeloid malignancies acquire a dependency on GPR68 signaling pathway, and inhibition of GPR68 might provide a novel therapeutic strategy for AML, especially in those developing chemoresistance. Disclosures No relevant conflicts of interest to declare.

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49

Wang, Chenghong, Xinlei Liu, Nilay Keser Demir, J. Paul Chen, and Kang Li. "Applications of water stable metal–organic frameworks." Chemical Society Reviews 45, no. 18 (2016): 5107–34. http://dx.doi.org/10.1039/c6cs00362a.

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50

Pozharskii, Alexander F., Valery A. Ozeryanskii, Vladimir Y. Mikshiev, Anatoly V. Chernyshev, Anatoly V. Metelitsa та Alexander S. Antonov. "Proton-induced fluorescence in modified quino[7,8-h]quinolines: dual sensing for protons and π-donors". Organic & Biomolecular Chemistry 17, № 35 (2019): 8221–33. http://dx.doi.org/10.1039/c9ob01391a.

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