The Role of Ion-Transporting Proteins in Human Disease
Funding
Conflicts of Interest
References
- Levring, J.; Terry, D.S.; Kilic, Z.; Fitzgerald, G.; Blanchard, S.C.; Chen, J. CFTR function, pathology and pharmacology at single-molecule resolution. Nature 2023, 616, 606–614. [Google Scholar] [CrossRef]
- Oka, Y.; Butnaru, M.; von Buchholtz, L.; Ryba, N.J.; Zuker, C.S. High salt recruits aversive taste pathways. Nature 2013, 494, 472–475. [Google Scholar] [CrossRef]
- Tang, T.; Jian, B.; Liu, Z. Transmembrane protein 175, a lysosomal ion channel related to Parkinson’s disease. Biomolecules 2023, 13, 802. [Google Scholar] [CrossRef]
- Kato, H.E.; Inoue, K.; Abe-Yoshizumi, R.; Kato, Y.; Ono, H.; Konno, M.; Hososhima, S.; Ishizuka, T.; Hoque, M.R.; Kunitomo, H.; et al. Structural basis for Na+ transport mechanism by a light-driven Na+ pump. Nature 2015, 521, 48–53. [Google Scholar] [CrossRef]
- Bernardazzi, C.; Sheikh, I.A.; Xu, H.; Ghishan, F.K. The physiological function and potential role of the ubiquitous Na+/H+ exchanger Isoform 8 (NHE8): An overview Data. Int. J. Mol. Sci. 2022, 23, 10857. [Google Scholar] [CrossRef]
- Riordan, J.R.; Rommens, J.M.; Kerem, B.; Alon, N.; Rozmahel, R.; Grzelczak, Z.; Zielenski, J.; Lok, S.; Plavsic, N.; Chou, J.L.; et al. Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA. Science 1989, 245, 1066–1073. [Google Scholar] [CrossRef]
- Welsh, M.J.; Smith, A.E. Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 1993, 73, 1251–1254. [Google Scholar] [CrossRef]
- Cabrini, G.; Rimessi, A.; Borgatti, M.; Pinton, P.; Gambari, R. Overview of CF lung pathophysiology. Curr. Opin. Pharmacol. 2022, 64, 102214. [Google Scholar] [CrossRef]
- Putman, M.S.; Norris, A.W.; Hull, R.L.; Rickels, M.R.; Sussel, L.; Blackman, S.M.; Chan, C.L.; Ode, K.L.; Daley, T.; Stecenko, A.A.; et al. Cystic fibrosis-related diabetes workshop: Research priorities spanning disease pathophysiology, diagnosis, and outcomes. Diabetes 2023, 72, 677–689. [Google Scholar] [CrossRef]
- Costaguta, G.; Patey, N.; Álvarez, F. Cystic fibrosis liver disease in children—A review of our current understanding. Arch. Argent Pediatr. 2023, 121, e202202905. [Google Scholar]
- Raymond, C.M.; Gaul, S.P.; Han, S.; Huang, G.; Dong, J. Variability of clinical presentation in patients heterozygous for the F508del cystic fibrosis variant: A series of three cases and a review of the literature. Cureus 2023, 15, e40185. [Google Scholar] [CrossRef] [PubMed]
- Mall, M.A.; Mayer-Hamblett, N.; Rowe, S.M. Cystic fibrosis: Emergence of highly effective targeted therapeutics and potential clinical implications. Am. J. Respir. Crit. Care Med. 2020, 201, 1193–1208. [Google Scholar] [CrossRef] [PubMed]
- Koivula, F.N.; McClenaghan, N.H.; Harper, A.G.; Kelly, C. Islet-intrinsic effects of CFTR mutation. Diabetologia 2016, 59, 1350–1355. [Google Scholar] [CrossRef]
- Ong, T.; Ramsey, B.W. Cystic Fibrosis: A review. JAMA 2023, 329, 1859–1871. [Google Scholar] [CrossRef] [PubMed]
- Fontes, G.; Ghislain, J.; Benterki, I.; Zarrouki, B.; Trudel, D.; Berthiaume, Y.; Poitout, V. The ΔF508 mutation in the cystic fibrosis transmembrane conductance regulator is associated with progressive insulin resistance and decreased functional beta-cell mass in mice. Diabetes 2015, 64, 4112–4122. [Google Scholar] [CrossRef] [PubMed]
- Marunaka, Y. The mechanistic links between insulin and cystic fibrosis transmembrane conductance regulator (CFTR) Cl− channel. Int. J. Mol. Sci. 2017, 18, 1767. [Google Scholar] [CrossRef]
- Veit, G.; Avramescu, R.G.; Chiang, A.N.; Houck, S.A.; Cai, Z.; Peters, K.W.; Hong, J.S.; Pollard, H.B.; Guggino, W.B.; Balch, W.E.; et al. From CFTR biology toward combinatorial pharmacotherapy: Expanded classification of cystic fibrosis mutations. Mol. Biol. Cell 2016, 27, 424–433. [Google Scholar] [CrossRef]
- Ramsey, B.W.; Davies, J.; McElvaney, N.G.; Tullis, E.; Bell, S.C.; Dřevínek, P.; Griese, M.; McKone, E.F.; Wainwright, C.E.; Konstan, M.W.; et al. A CFTR potentiator in patients with cystic fibrosis and the G551D mutation. N. Engl. J. Med. 2011, 365, 1663–1672. [Google Scholar] [CrossRef]
- Sinha, M.; Zabini, D.; Guntur, D.; Nagaraj, C.; Enyedi, P.; Olschewski, H.; Kuebler, W.M.; Olschewski, A. Chloride channels in the lung: Challenges and perspectives for viral infections, pulmonary arterial hypertension, and cystic fibrosis. Pharmacol. Ther. 2022, 237, 108249. [Google Scholar] [CrossRef]
- Okada, Y.; Okada, T.; Sato-Numata, K.; Islam, M.R.; Ando-Akatsuka, Y.; Numata, T.; Kubo, M.; Shimizu, T.; Kurbannazarova, R.S.; Marunaka, Y.; et al. Cell volume-activated and volume-correlated anion channels in mammalian cells: Their biophysical, molecular, and pharmacological properties. Pharmacol. Rev. 2019, 71, 49–88. [Google Scholar] [CrossRef]
- Marunaka, Y. Physiological roles of chloride ions in bodily and cellular functions. J. Physiol. Sci. 2023, 73, 31. [Google Scholar] [CrossRef] [PubMed]
- Shekarabi, M.; Zhang, J.; Khanna, A.R.; Ellison, D.H.; Delpire, E.; Kahle, K.T. WNK kinase signaling in ion homeostasis and human disease. Cell Metab. 2017, 25, 285–299. [Google Scholar] [CrossRef] [PubMed]
- Köchl, R.; Thelen, F.; Vanes, L.; Brazão, T.F.; Fountain, K.; Xie, J.; Huang, C.L.; Lyck, R.; Stein, J.V.; Tybulewicz, V.L. WNK1 kinase balances T cell adhesion versus migration in vivo. Nat. Immunol. 2016, 17, 1075–1083. [Google Scholar] [CrossRef] [PubMed]
- Garzon-Muvdi, T.; Schiapparelli, P.; ap Rhys, C.; Guerrero-Cazares, H.; Smith, C.; Kim, D.H.; Kone, L.; Farber, H.; Lee, D.Y.; An, S.S.; et al. Regulation of brain tumor dispersal by NKCC1 through a novel role in focal adhesion regulation. PLoS Biol. 2012, 10, e1001320. [Google Scholar] [CrossRef]
- Haas, B.R.; Cuddapah, V.A.; Watkins, S.; Rohn, K.J.; Dy, T.E.; Sontheimer, H. With-No-Lysine Kinase 3 (WNK3) stimulates glioma invasion by regulating cell volume. Am. J. Physiol. Cell Physiol. 2011, 301, C1150–C1160. [Google Scholar] [CrossRef]
- Schwab, A.; Fabian, A.; Hanley, P.J.; Stock, C. Role of ion channels and transporters in cell migration. Physiol. Rev. 2012, 92, 1865–1913. [Google Scholar] [CrossRef] [PubMed]
- Carmona, B.; Marinho, H.S.; Matos, C.L.; Nolasco, S.; Soares, H. Tubulin post-translational modifications: The elusive roles of acetylation. Biology 2023, 12, 561. [Google Scholar] [CrossRef]
- Chen, Y.; Yu, X.; Yan, Z.; Zhang, S.; Zhang, J.; Guo, W. Role of epithelial sodium channel-related inflammation in human diseases. Front. Immunol. 2023, 14, 1178410. [Google Scholar] [CrossRef]
- Canessa, C.M.; Horisberger, J.D.; Rossier, B.C. Epithelial sodium channel related to proteins involved in neurodegeneration. Nature 1993, 361, 467–470. [Google Scholar] [CrossRef]
- Canessa, C.M.; Schild, L.; Buell, G.; Thorens, B.; Gautschi, I.; Horisberger, J.D.; Rossier, B.C. Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits. Nature 1994, 367, 463–467. [Google Scholar] [CrossRef]
- Baconguis, I.; Bohlen, C.J.; Goehring, A.; Julius, D.; Gouaux, E. X-ray structure of acid-sensing ion channel 1-snake toxin complex reveals open state of a Na+-selective channel. Cell 2014, 156, 717–729. [Google Scholar] [CrossRef]
- Kleyman, T.R.; Kashlan, O.B.; Hughey, R.P. Epithelial Na+ channel Rregulation by extracellular and intracellular factors. Annu. Rev. Physiol. 2018, 80, 263–281. [Google Scholar] [CrossRef]
- Zhang, L.; Wang, X.; Chen, J.; Kleyman, T.R.; Sheng, S. Accessibility of ENaC extracellular domain central core residues. J. Biol. Chem. 2022, 298, 101860. [Google Scholar] [CrossRef]
- Staub, O.; Gautschi, I.; Ishikawa, T.; Breitschopf, K.; Ciechanover, A.; Schild, L.; Rotin, D. Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination. EMBO J. 1997, 16, 6325–6336. [Google Scholar] [CrossRef]
- Shimkets, R.A.; Warnock, D.G.; Bositis, C.M.; Nelson-Williams, C.; Hansson, J.H.; Schambelan, M.; Gill, J.R., Jr.; Ulick, S.; Milora, R.V.; Findling, J.W.; et al. Liddle’s syndrome: Heritable human hypertension caused by mutations in the beta subunit of the epithelial sodium channel. Cell 1994, 79, 407–414. [Google Scholar] [CrossRef]
- Pradervand, S.; Barker, P.M.; Wang, Q.; Ernst, S.A.; Beermann, F.; Grubb, B.R.; Burnier, M.; Schmidt, A.; Bindels, R.J.; Gatzy, J.T.; et al. Salt restriction induces pseudohypoaldosteronism type 1 in mice expressing low levels of the beta-subunit of the amiloride-sensitive epithelial sodium channel. Proc. Natl. Acad. Sci. USA 1999, 96, 1732–1737. [Google Scholar] [CrossRef] [PubMed]
- Hansson, J.H.; Nelson-Williams, C.; Suzuki, H.; Schild, L.; Shimkets, R.; Lu, Y.; Canessa, C.; Iwasaki, T.; Rossier, B.; Lifton, R.P. Hypertension caused by a truncated epithelial sodium channel gamma subunit: Genetic heterogeneity of Liddle syndrome. Nat. Genet. 1995, 11, 76–82. [Google Scholar] [CrossRef] [PubMed]
- Hansson, J.H.; Schild, L.; Lu, Y.; Wilson, T.A.; Gautschi, I.; Shimkets, R.; Nelson-Williams, C.; Rossier, B.C.; Lifton, R.P. A de novo missense mutation of the beta subunit of the epithelial sodium channel causes hypertension and Liddle syndrome, identifying a proline-rich segment critical for regulation of channel activity. Proc. Natl. Acad. Sci. USA 1995, 92, 11495–11499. [Google Scholar] [CrossRef] [PubMed]
- Tamura, H.; Schild, L.; Enomoto, N.; Matsui, N.; Marumo, F.; Rossier, B.C. Liddle disease caused by a missense mutation of beta subunit of the epithelial sodium channel gene. J. Clin. Investig. 1996, 97, 1780–1784. [Google Scholar] [CrossRef] [PubMed]
- Staub, O.; Dho, S.; Henry, P.; Correa, J.; Ishikawa, T.; McGlade, J.; Rotin, D. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle’s syndrome. EMBO J. 1996, 15, 2371–2380. [Google Scholar] [CrossRef] [PubMed]
- Tabibzadeh, N.; Crambert, G. Mechanistic insights into the primary and secondary alterations of renal ion and water transport in the distal nephron. J. Intern. Med. 2023, 293, 4–22. [Google Scholar] [CrossRef]
- Taruno, A.; Gordon, M.D. Molecular and cellular mechanisms of salt taste. Annu. Rev. Physiol. 2023, 85, 25–45. [Google Scholar] [CrossRef]
- Marunaka, Y. Roles of interstitial fluid pH and weak organic acids in development and amelioration of insulin resistance. Biochem. Soc. Trans. 2021, 49, 715–726. [Google Scholar] [CrossRef]
- Pillai, S.R.; Damaghi, M.; Marunaka, Y.; Spugnini, E.P.; Fais, S.; Gillies, R.J. Causes, consequences, and therapy of tumors acidosis. Cancer Metastasis Rev. 2019, 38, 205–222. [Google Scholar] [CrossRef]
- Gillies, R.J.; Pilot, C.; Marunaka, Y.; Fais, S. Targeting acidity in cancer and diabetes. Biochim. Biophys. Acta. Rev. Cancer 2019, 1871, 273–280. [Google Scholar] [CrossRef]
- Fais, S.; Marunaka, Y. The acidic microenvironment: Is it a phenotype of all cancers? A focus on multiple myeloma and some analogies with diabetes mellitus. Cancers 2020, 12, 3226. [Google Scholar] [CrossRef] [PubMed]
- Puppulin, L.; Hosogi, S.; Sun, H.; Matsuo, K.; Inui, T.; Kumamoto, Y.; Suzaki, T.; Tanaka, H.; Marunaka, Y. Bioconjugation strategy for cell surface labelling with gold nanostructures designed for highly localized pH measurement. Nat. Commun. 2018, 9, 5278. [Google Scholar] [CrossRef] [PubMed]
- Marunaka, Y. Molecular mechanisms of obesity-induced development of insulin resistance and promotion of amyloid-β accumulation: Dietary therapy using weak organic acids via improvement of lowered interstitial fluid pH. Biomolecules 2023, 13, 779. [Google Scholar] [CrossRef] [PubMed]
- Kamariah, N.; Ragunathan, P.; Shin, J.; Saw, W.G.; Wong, C.F.; Dick, T.; Grüber, G. Unique structural and mechanistic properties of mycobacterial F-ATP synthases: Implications for drug design. Prog. Biophys. Mol. Biol. 2020, 152, 64–73. [Google Scholar] [CrossRef]
- Patel, H.; Kerndt, C.C.; Bhardwaj, A. Physiology, Respiratory Quotient. In StatPearls; StatPearls Publishing LLC: Treasure Island, FL, USA, 2020. [Google Scholar]
- Pessin, J.E.; Bell, G.I. Mammalian facilitative glucose transporter family: Structure and molecular regulation. Annu. Rev. Physiol. 1992, 54, 911–930. [Google Scholar] [CrossRef]
- Diaz-Vegas, A.; Sanchez-Aguilera, P.; Krycer, J.R.; Morales, P.E.; Monsalves-Alvarez, M.; Cifuentes, M.; Rothermel, B.A.; Lavandero, S. Is mitochondrial dysfunction a common root of noncommunicable chronic diseases? Endocr. Rev. 2020, 41, 491–517. [Google Scholar] [CrossRef]
- Michailidis, M.; Moraitou, D.; Tata, D.A.; Kalinderi, K.; Papamitsou, T.; Papaliagkas, V. Alzheimer’s disease as type 3 Diabetes: Common pathophysiological mechanisms between Alzheimer’s disease and type 2 diabetes. Int. J. Mol. Sci. 2022, 23, 2687. [Google Scholar] [CrossRef]
- Mthembu, S.X.H.; Mazibuko-Mbeje, S.E.; Ziqubu, K.; Nyawo, T.A.; Obonye, N.; Nyambuya, T.M.; Nkambule, B.B.; Silvestri, S.; Tiano, L.; Muller, C.J.F.; et al. Impact of physical exercise and caloric restriction in patients with type 2 diabetes: Skeletal muscle insulin resistance and mitochondrial dysfunction as ideal therapeutic targets. Life Sci. 2022, 297, 120467. [Google Scholar] [CrossRef]
- Shane, M.A.; Nofziger, C.; Blazer-Yost, B.L. Hormonal regulation of the epithelial Na+ channel: From amphibians to mammals. Gen. Comp. Endocrinol. 2006, 147, 85–92. [Google Scholar] [CrossRef]
- Lynn, J.; Park, M.; Ogunwale, C.; Acquaah-Mensah, G.K. A tale of two diseases: Exploring mechanisms linking diabetes mellitus with Alzheimer’s disease. J. Alzheimers Dis. 2022, 85, 485–501. [Google Scholar] [CrossRef] [PubMed]
- Potenza, M.A.; Sgarra, L.; Desantis, V.; Nacci, C.; Montagnani, M. Diabetes and Alzheimer’s disease: Might mitochondrial dysfunction help deciphering the common path? Antioxidants 2021, 10, 1257. [Google Scholar] [CrossRef] [PubMed]
- Paul, S.; Saha, D.; Bk, B. Mitochondrial dysfunction and mitophagy closely cooperate in neurological deficits associated with Alzheimer’s disease and type 2 diabetes. Mol. Neurobiol. 2021, 58, 3677–3691. [Google Scholar] [CrossRef] [PubMed]
- Woo, C.Y.; Jang, J.E.; Lee, S.E.; Koh, E.H.; Lee, K.U. Mitochondrial dysfunction in adipocytes as a primary cause of adipose tissue inflammation. Diabetes Metab. J. 2019, 43, 247–256. [Google Scholar] [CrossRef] [PubMed]
- Takano, C.; Ogawa, E.; Hayakawa, S. Insulin resistance in mitochondrial diabetes. Biomolecules 2023, 13, 126. [Google Scholar] [CrossRef] [PubMed]
- Petrenko, A.G.; Zozulya, S.A.; Deyev, I.E.; Eladari, D. Insulin receptor-related receptor as an extracellular pH sensor involved in the regulation of acid-base balance. Biochim. Biophys. Acta 2013, 1834, 2170–2175. [Google Scholar] [CrossRef]
- Hayata, H.; Miyazaki, H.; Niisato, N.; Yokoyama, N.; Marunaka, Y. Lowered extracellular pH is involved in the pathogenesis of skeletal muscle insulin resistance. Biochem. Biophys. Res. Commun. 2014, 445, 170–174. [Google Scholar] [CrossRef]
- Hampel, H.; Vassar, R.; De Strooper, B.; Hardy, J.; Willem, M.; Singh, N.; Zhou, J.; Yan, R.; Vanmechelen, E.; De Vos, A.; et al. The β-secretase BACE1 in Alzheimer’s disease. Biol. Psychiatry 2021, 89, 745–756. [Google Scholar] [CrossRef]
- Ju, Y.; Tam, K.Y. Pathological mechanisms and therapeutic strategies for Alzheimer’s disease. Neural Regen. Res. 2022, 17, 543–549. [Google Scholar]
- Kamble, S.; Barale, S.; Dhanavade, M.; Sonawane, K. Structural significance of neprylysin from Streptococcus suis GZ1 in the degradation of Aβ peptides, a causative agent in Alzheimer’s disease. Comput. Biol. Med. 2021, 136, 104691. [Google Scholar] [CrossRef]
- Kim, N.; Lee, H.J. Redox-active metal ions and amyloid-degrading enzymes in Alzheimer’s disease. Int. J. Mol. Sci. 2021, 22, 7697. [Google Scholar] [CrossRef]
- Bell, S.M.; Barnes, K.; De Marco, M.; Shaw, P.J.; Ferraiuolo, L.; Blackburn, D.J.; Venneri, A.; Mortiboys, H. Mitochondrial dysfunction in Alzheimer’s disease: A biomarker of the future? Biomedicines 2021, 9, 63. [Google Scholar] [CrossRef] [PubMed]
- Roda, A.R.; Serra-Mir, G.; Montoliu-Gaya, L.; Tiessler, L.; Villegas, S. Amyloid-beta peptide and tau protein crosstalk in Alzheimer’s disease. Neural Regen. Res. 2022, 17, 1666–1674. [Google Scholar] [PubMed]
- Cheng, L.; Li, W.; Chen, Y.; Lin, Y.; Wang, B.; Guo, Q.; Miao, Y. Plasma Aβ as a biomarker for predicting Aβ-PET status in Alzheimer’s disease: A systematic review with meta-analysis. J. Neurol. Neurosurg. Psychiatry 2022, 93, 513–520. [Google Scholar] [CrossRef] [PubMed]
- Kumar, N.; Kumar, V.; Anand, P.; Kumar, V.; Ranjan Dwivedi, A.; Kumar, V. Advancements in the development of multi-target directed ligands for the treatment of Alzheimer’s disease. Bioorg. Med. Chem. 2022, 61, 116742. [Google Scholar] [CrossRef] [PubMed]
- Peng, X.; Fan, R.; Xie, L.; Shi, X.; Dong, K.; Zhang, S.; Tao, J.; Xu, W.; Ma, D.; Chen, J.; et al. A growing link between circadian rhythms, type 2 diabetes mellitus and Alzheimer’s disease. Int. J. Mol. Sci. 2022, 23, 504. [Google Scholar] [CrossRef] [PubMed]
- Pakdin, M.; Toutounchian, S.; Namazi, S.; Arabpour, Z.; Pouladi, A.; Afsahi, S.; Poudineh, M.; Nasab, M.M.M.; Yaghoobpoor, S.; Deravi, N. Type 2 diabetes mellitus and Alzheimer disease: A review of the potential links. Curr. Diabetes Rev. 2022, 18, e051121197760. [Google Scholar]
- Burillo, J.; Marqués, P.; Jiménez, B.; González-Blanco, C.; Benito, M.; Guillén, C. Insulin resistance and diabetes mellitus in Alzheimer’s disease. Cells 2021, 10, 1236. [Google Scholar] [CrossRef]
- Humpel, C. Intranasal neprilysin rapidly eliminates amyloid-beta plaques, but causes plaque compensations: The explanation why the amyloid-beta cascade may fail? Neural. Regen. Res. 2022, 17, 1881–1884. [Google Scholar] [CrossRef] [PubMed]
- Nagai, N.; Ito, Y.; Tanino, T. Effect of high glucose levels on amyloid β production in retinas of spontaneous diabetes mellitus Otsuka Long-Evans Tokushima fatty rats. Biol. Pharm. Bull. 2015, 38, 601–610. [Google Scholar] [CrossRef]
- Lai, M.C.; Liu, W.Y.; Liou, S.S.; Liu, I.M. The citrus flavonoid hesperetin encounters diabetes-mediated Alzheimer-type neuropathologic changes through relieving advanced glycation end-products Inducing endoplasmic reticulum stress. Nutrients 2022, 14, 745. [Google Scholar] [CrossRef] [PubMed]
- Hur, J.-Y. γ-Secretase in Alzheimer’s disease. Exp. Mol. Med. 2022, 54, 433–446. [Google Scholar] [CrossRef]
- Sasaguri, H.; Hashimoto, S.; Watamura, N.; Sato, K.; Takamura, R.; Nagata, K.; Tsubuki, S.; Ohshima, T.; Yoshiki, A.; Sato, K.; et al. Recent advances in the modeling of Alzheimer’s disease. Front. Neurosci. 2022, 16, 807473. [Google Scholar] [CrossRef]
- Haass, C.; Hung, A.Y.; Schlossmacher, M.G.; Teplow, D.B.; Selkoe, D.J. beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem. 1993, 268, 3021–3024. [Google Scholar] [CrossRef]
- Knops, J.; Suomensaari, S.; Lee, M.; McConlogue, L.; Seubert, P.; Sinha, S. Cell-type and amyloid precursor protein-type specific inhibition of A beta release by bafilomycin A1, a selective inhibitor of vacuolar ATPases. J. Biol. Chem. 1995, 270, 2419–2422. [Google Scholar] [CrossRef] [PubMed]
- Ren, W.; Lou, H.; Ren, X.; Wen, G.; Wu, X.; Xia, X.; Wang, S.; Yu, X.; Yan, L.; Zhang, G.; et al. Ketamine promotes the amyloidogenic pathway by regulating endosomal pH. Toxicology 2022, 471, 153163. [Google Scholar] [CrossRef]
- Ellis, C.R.; Shen, J. pH-Dependent Population Shift Regulates BACE1 Activity and Inhibition. J. Am. Chem. Soc. 2015, 137, 9543–9546. [Google Scholar] [CrossRef]
- Maesako, M.; Houser, M.C.Q.; Turchyna, Y.; Wolfe, M.S.; Berezovska, O. Presenilin/γ-secretase activity is located in acidic compartments of live neurons. J. Neurosci. 2022, 42, 145–154. [Google Scholar] [CrossRef]
- Cai, T.; Hatano, A.; Kanatsu, K.; Tomita, T. Histidine 131 in presenilin 1 is the pH-sensitive residue that causes the increase in Aβ42 level in acidic pH. J. Biochem. 2020, 167, 463–471. [Google Scholar] [CrossRef]
- Marunaka, Y. The proposal of molecular mechanisms of weak organic acids intake-induced improvement of insulin resistance in diabetes mellitus via elevation of interstitial fluid pH. Int. J. Mol. Sci. 2018, 19, 3244. [Google Scholar] [CrossRef]
- Hosogi, S.; Kuwahara, A.; Kuwahara, Y.; Tanaka, S.; Shimamoto, C.; Tagawa, N.; Kato, I.; Yoshimoto, K.; Aoi, W.; Takata, K.; et al. Mumefural prevents insulin resistance and amyloid-beta accumulation in the brain by improving lowered interstitial fluid pH in type 2 diabetes mellitus. Biomed. Res. 2023, 44, 17–29. [Google Scholar] [CrossRef]
- Bazzone, A.; Barthmes, M.; George, C.; Brinkwirth, N.; Zerlotti, R.; Prinz, V.; Cole, K.; Friis, S.; Dickson, A.; Rice, S.; et al. A comparative study on the lysosomal cation channel TMEM175 using automated whole-cell patch-clamp, lysosomal patch-clamp, and solid supported membrane-based electrophysiology: Functional characterization and high-throughput screening assay development. Int. J. Mol. Sci. 2023, 24, 12788. [Google Scholar] [CrossRef] [PubMed]
- Salari, A.; Zhou, K.; Nikolovska, K.; Seidler, U.; Amiri, M. Human colonoid-myofibroblast coculture for study of apical Na+/H+ exchangers of the lower cryptal nNeck region. Int. J. Mol. Sci. 2023, 24, 4266. [Google Scholar] [CrossRef] [PubMed]
- Tovar, L.M.; Burgos, C.F.; Yévenes, G.E.; Moraga-Cid, G.; Fuentealba, J.; Coddou, C.; Bascunan-Godoy, L.; Catrupay, C.; Torres, A.; Castro, P.A. Understanding the role of ATP release through connexins hemichannels during neurulation. Int. J. Mol. Sci. 2023, 24, 2159. [Google Scholar] [CrossRef] [PubMed]
- Baloglu, E. Hypoxic stress-dependent regulation of Na,K-ATPase in ischemic heart disease. Int. J. Mol. Sci. 2023, 24, 7855. [Google Scholar] [CrossRef] [PubMed]
- Lemmens-Gruber, R.; Tzotzos, S. The epithelial sodium channel—An underestimated drug target. Int. J. Mol. Sci. 2023, 24, 7775. [Google Scholar] [CrossRef]
Disclaimer/Publisher’s Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content. |
© 2024 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Marunaka, Y. The Role of Ion-Transporting Proteins in Human Disease. Int. J. Mol. Sci. 2024, 25, 1726. https://doi.org/10.3390/ijms25031726
Marunaka Y. The Role of Ion-Transporting Proteins in Human Disease. International Journal of Molecular Sciences. 2024; 25(3):1726. https://doi.org/10.3390/ijms25031726
Chicago/Turabian StyleMarunaka, Yoshinori. 2024. "The Role of Ion-Transporting Proteins in Human Disease" International Journal of Molecular Sciences 25, no. 3: 1726. https://doi.org/10.3390/ijms25031726