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Journal articles on the topic 'Molecular Physiology and Pharmacology'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Kiehn, Johann, Antonio E. Lacerda, Barbara Wible, and Arthur M. Brown. "Molecular Physiology and Pharmacology of HERG." Circulation 94, no. 10 (November 15, 1996): 2572–79. http://dx.doi.org/10.1161/01.cir.94.10.2572.

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2

UEDA, Hiroshi, and Makoto INOUE. "Molecular pharmacology and physiology of nociceptin." Folia Pharmacologica Japonica 114, no. 6 (1999): 347–56. http://dx.doi.org/10.1254/fpj.114.347.

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3

Bleakman, D. "Kainate receptor pharmacology and physiology." Cellular and Molecular Life Sciences (CMLS) 56, no. 7-8 (November 1, 1999): 558–66. http://dx.doi.org/10.1007/s000180050453.

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4

Masaki, Tomoh, Masashi Yanagisawa, and Katsutoshi Goto. "Physiology and pharmacology of endothelins." Medicinal Research Reviews 12, no. 4 (July 1992): 391–421. http://dx.doi.org/10.1002/med.2610120405.

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5

Fisher, James W. "Erythropoietin: Physiology and Pharmacology Update." Experimental Biology and Medicine 228, no. 1 (January 2003): 1–14. http://dx.doi.org/10.1177/153537020322800101.

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This minireview is an update of a 1997 review on erythropoletin (EPO) in this journal (1). EPO is a 30,400-dalton glycoprotein that regulates red cell production. In the human, EPO is produced by peritubular cells in the kidneys of the adult and in hepatocytes in the fetus. Small amounts of extra-renal EPO are produced by the liver in adult human subjects. EPO binds to an erythroid progenitor cell surface receptor that includes a p66 chain, and, when activated, the p66 protein becomes dimerized. EPO receptor activation induces a JAK2 tyrosine kinase, which leads to tyrosine phosphorylation of the EPO receptor and several proteins. EPO receptor binding leads to intracellular activation of the Ras/mitogen-activated kinase pathway, which is involved with cell proliferation, phosphatidylinositol 3-kinase, and STATS 1, 3, 5A, and 5B transcriptional factors. EPO acts primarily to rescue erythroid cells from apoptosis (programmed cell death) to increase their survival. EPO acts synergistically with several growth factors (SCF, GM-CSF, 1L-3, and IGF-1) to cause maturation and proliferation of erythroid progenitor cells (primarily colony-forming unit-E). Oxygen-dependent regulation of EPO gene expression is postulated to be controlled by a hypoxia-inducible transcription factor (HIF-1α). Hypoxia-inducible EPO production is controlled by a 50-bp hypoxia-inducible enhancer that is approximately 120 bp 3' to the polyadenylation site. Hypoxia signal transduction pathways involve kinases A and C, phospholipase A2, and transcription factors ATF-1 and CREB-1. A model has been proposed for adenosine activation of EPO production that involves protein kinases A and C and the phospholipase A2 pathway. Other effects of EPO include a hematocrit-independent, vasoconstriction-dependent hypertension, increased endothelin production, upregulation of tissue renin, change in vascular tissue prostaglandins production, stimulation of angiogenesis, and stimulation of endothelial and vascular smooth muscle cell proliferation. Recombinant human EPO (rHuEPO) is currently being used to treat patients with anemias associated with chronic renal failure, AIDS patients with anemia due to treatment with zidovudine, nonmyeloid malignancies in patients treated with chemotherapeutic agents, perioperative surgical patients, and autologous blood donation. A novel erythropolesis-stimulating factor (NESP, darbepoetin) has been synthesized and when compared with rHuEPO, NESP has a higher carbohydrate content (52% vs 40%), a longer plasma half-life, the amino acid sequence differs from that of native human EPO at five positions, and has been reported to maintain hemoglobin levels just as effectively in patients with chronic renal failure as rHuEPO at less frequent dosing. The use of rHuEPO and darbepoetin to enhance athletic performance is officially banned by most sports-governing bodies because the excessive erythrocytosis can lead to increased thrombogenicity and can cause deep vein, coronary, and cerebral thromboses.

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6

Nakanishi, Shigetada. "Molecular physiology of glutamate receptors." Japanese Journal of Pharmacology 67 (1995): 7. http://dx.doi.org/10.1016/s0021-5198(19)35554-4.

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7

Brooks, G. T. "Comprehensive insect physiology, biochemistry and pharmacology." Insect Biochemistry 15, no. 5 (January 1985): i—xiv. http://dx.doi.org/10.1016/0020-1790(85)90131-3.

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8

Ciarimboli, Giuliano. "Physiology, Biochemistry, and Pharmacology of Transporters for Organic Cations." International Journal of Molecular Sciences 22, no. 2 (January 13, 2021): 732. http://dx.doi.org/10.3390/ijms22020732.

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This editorial summarizes the 13 scientific papers published in the Special Issue “Physiology, Biochemistry, and Pharmacology of Transporters for Organic Cations” of the International Journal of Molecular Sciences [...]

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9

Anderson, Warwick P. "Molecular biology in the service of physiology, pharmacology and endocrinology." Clinical and Experimental Pharmacology and Physiology 22, no. 12 (December 1995): 934. http://dx.doi.org/10.1111/j.1440-1681.1995.tb02329.x.

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10

de Almeida, Luiz G. N., Hayley Thode, Yekta Eslambolchi, Sameeksha Chopra, Daniel Young, Sean Gill, Laurent Devel, and Antoine Dufour. "Matrix Metalloproteinases: From Molecular Mechanisms to Physiology, Pathophysiology, and Pharmacology." Pharmacological Reviews 74, no. 3 (June 23, 2022): 712–68. http://dx.doi.org/10.1124/pharmrev.121.000349.

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11

Krzan, M. "Histamine receptors in the heart—Molecular characteristics, physiology and pharmacology." Inflammopharmacology 4, no. 3 (September 1996): 241–57. http://dx.doi.org/10.1007/bf02731874.

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12

Sudakov, S. K. "Physiology and Pharmacology of Positive Reinforcement." Bulletin of Experimental Biology and Medicine 166, no. 6 (April 2019): 709–13. http://dx.doi.org/10.1007/s10517-019-04423-1.

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13

Funder, John W. "Physiology, pharmacology, toxicology and strength of materials." Molecular and Cellular Endocrinology 72, no. 2 (August 1990): C53—C56. http://dx.doi.org/10.1016/0303-7207(90)90095-p.

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14

Deal, K. K., S. K. England, and M. M. Tamkun. "Molecular physiology of cardiac potassium channels." Physiological Reviews 76, no. 1 (January 1, 1996): 49–67. http://dx.doi.org/10.1152/physrev.1996.76.1.49.

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The cardiac action potential results from the complex, but precisely regulated, movement of ions across the sarcolemmal membrane. Potassium channels represent the most diverse class of ion channels in heart and are the targets of several antiarrhythmic drugs. Potassium currents in the myocardium can be classified into one of two general categories: 1) inward rectifying currents such as IK1, IKACh, and IKATP; and 2) primarily voltage-gated currents such as IKs, IKr, IKp, IKur, and Ito. The inward rectifier currents regulate the resting membrane potential, whereas the voltage-activated currents control action potential duration. The presence of these multiple, often overlapping, outward currents in native cardiac myocytes has complicated the study of individual K+ channels; however, the application of molecular cloning technology to these cardiovascular K+ channels has identified the primary structure of these proteins, and heterologous expression systems have allowed a detailed analysis of the function and pharmacology of a single channel type. This review addresses the progress made toward understanding the complex molecular physiology of K+ channels in mammalian myocardium. An important challenge for the future is to determine the relative contribution of each of these cloned channels to cardiac function.

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15

LUNDBERG, JAN M., KJELL ALVING, and REGIS MATRAN. "Pulmonary Physiology and Pharmacology of Neuropeptides." Annals of the New York Academy of Sciences 629, no. 1 Advances in t (July 1991): 332–39. http://dx.doi.org/10.1111/j.1749-6632.1991.tb37987.x.

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16

Van Aubel, Rémon A. M. H., Rosalinde Masereeuw, and Frans G. M. Russel. "Molecular pharmacology of renal organic anion transporters." American Journal of Physiology-Renal Physiology 279, no. 2 (August 1, 2000): F216—F232. http://dx.doi.org/10.1152/ajprenal.2000.279.2.f216.

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Renal organic anion transport systems play an important role in the elimination of drugs, toxic compounds, and their metabolites, many of which are potentially harmful to the body. The renal proximal tubule is the primary site of carrier-mediated transport from blood to urine of a wide variety of anionic substrates. Recent studies have shown that organic anion secretion in renal proximal tubule is mediated by distinct sodium-dependent and sodium-independent transport systems. Knowledge of the molecular identity of these transporters and their substrate specificity has increased considerably in the past few years by cloning of various carrier proteins. However, a number of fundamental questions still have to be answered to elucidate the participation of the cloned transporters in the overall tubular secretion of anionic xenobiotics. This review summarizes the latest knowledge on molecular and pharmacological properties of renal organic anion transporters and homologs, with special reference to their nephron and plasma membrane localization, transport characteristics, and substrate and inhibitor specificity. A number of the recently cloned transporters, such as the p-aminohippurate/dicarboxylate exchanger OAT1, the anion/sulfate exchanger SAT1, the peptide transporters PEPT1 and PEPT2, and the nucleoside transporters CNT1 and CNT2, are key proteins in organic anion handling that possess the same characteristics as has been predicted from previous physiological studies. The role of other cloned transporters, such as MRP1, MRP2, OATP1, OAT-K1, and OAT-K2, is still poorly characterized, whereas the only information that is available on the homologs OAT2, OAT3, OATP3, and MRP3–6 is that they are expressed in the kidney, but their localization, not to mention their function, remains to be elucidated.

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17

SUH, YOO-HUN, YOUNG HAE CHONG, SEONG-HUN KIM, WOONG CHOI, SUNG-JIN JEONG, S. P. FRASER, M. B. A. DJAMGOZ, and KYEONGSIK MIN. "Molecular Physiology, Biochemistry, and Pharmacology of Alzheimer's Amyloid Precursor Protein (APP)." Annals of the New York Academy of Sciences 786, no. 1 Near-Earth Ob (June 1996): 169–83. http://dx.doi.org/10.1111/j.1749-6632.1996.tb39060.x.

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18

Panettieri Jr, Reynold A. "Cellular and molecular mechanisms regulating airway smooth muscle physiology and pharmacology." Journal of Organ Dysfunction 2, no. 1 (January 2006): 37–47. http://dx.doi.org/10.1080/17471060600580698.

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19

Vandenberg, Robert J. "MOLECULAR PHARMACOLOGY AND PHYSIOLOGY OF GLUTAMATE TRANSPORTERS IN THE CENTRAL NERVOUS SYSTEM." Clinical and Experimental Pharmacology and Physiology 25, no. 6 (June 1998): 393–400. http://dx.doi.org/10.1111/j.1440-1681.1998.tb02221.x.

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20

Matic, Ivana, Daniela Strobbe, Michele Frison, and Michelangelo Campanella. "Controlled and Impaired Mitochondrial Quality in Neurons: Molecular Physiology and Prospective Pharmacology." Pharmacological Research 99 (September 2015): 410–24. http://dx.doi.org/10.1016/j.phrs.2015.03.021.

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21

Campbell, Jonathan E., and Daniel J. Drucker. "Pharmacology, Physiology, and Mechanisms of Incretin Hormone Action." Cell Metabolism 17, no. 6 (June 2013): 819–37. http://dx.doi.org/10.1016/j.cmet.2013.04.008.

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22

Kukkonen, Jyrki P. "Recent progress in orexin/hypocretin physiology and pharmacology." BioMolecular Concepts 3, no. 5 (October 1, 2012): 447–63. http://dx.doi.org/10.1515/bmc-2012-0013.

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AbstractOrexin peptides and their cognate receptors were discovered 14 years ago. They soon took a very central position in the regulation of sleep and wakefulness. Active studies have further elucidated these functions as well as the role of orexins in, for instance, appetite, metabolism, analgesia, addiction, and stress response. This review summarizes all the important fields but especially aims at focusing on novel findings and future directions.

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23

Pantic, Igor. "Cancer stem cell hypotheses: Impact on modern molecular physiology and pharmacology research." Journal of Biosciences 36, no. 5 (October 18, 2011): 957–61. http://dx.doi.org/10.1007/s12038-011-9155-5.

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24

Bagrov, Alexei Y., Joseph I. Shapiro, and Olga V. Fedorova. "Endogenous Cardiotonic Steroids: Physiology, Pharmacology, and Novel Therapeutic Targets." Pharmacological Reviews 61, no. 1 (March 2009): 9–38. http://dx.doi.org/10.1124/pr.108.000711.

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25

Robertson, Alan P., and Richard J. Martin. "Ion-channels on parasite muscle: pharmacology and physiology." Invertebrate Neuroscience 7, no. 4 (November 13, 2007): 209–17. http://dx.doi.org/10.1007/s10158-007-0059-x.

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26

Blakely, R. D., L. J. De Felice, and H. C. Hartzell. "Molecular physiology of norepinephrine and serotonin transporters." Journal of Experimental Biology 196, no. 1 (November 1, 1994): 263–81. http://dx.doi.org/10.1242/jeb.196.1.263.

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Cocaine- and antidepressant-sensitive norepinephrine and serotonin transporters (NETs and SERTs) are closely related members of the Na+/Cl- transporter gene family, whose other members include transporters for inhibitory amino acid transmitters, neuromodulators, osmolytes and nutrients. Availability of cloned NET and SERT cDNAs has permitted rapid progress in the definition of cellular sites of gene expression, the generation of transporter-specific antibodies suitable for biosynthetic and localization studies, the examination of structure-function relationships in heterologous expression systems and a biophysical analysis of transporter function. In situ hybridization and immunocytochemical studies indicate a primary expression of NET and SERT genes in brain by noradrenergic and serotonergic neurons, respectively. Both NET and SERT are synthesized as glycoproteins, with multiple glycosylation states apparent for SERT proteins in the brain and periphery. N-glycosylation of NET and SERT appears to be essential for transporter assembly and surface expression, but not for antagonist binding affinity. Homology cloning efforts have revealed novel NET and SERT homologs in nonmammalian species that are of potential value in the delineation of the precise sites for substrate and antagonist recognition, including a Drosophila melanogaster SERT with NET-like pharmacology. Electrophysiological recording of human NETs and SERTs stably expressed in HEK-293 cells reveals that both transporters move charge across the plasma membrane following the addition of substrates; these currents can be blocked by NET-and SERT-selective antagonists as well as by cocaine.

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27

Capela e Silva, Fernando, Elsa Lamy, and Paula Midori Castelo. "Models for Oral Biology Research." Biomedicines 10, no. 5 (April 20, 2022): 952. http://dx.doi.org/10.3390/biomedicines10050952.

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Oral biology is a scientific field that involves several disciplines, such as anatomy, cellular and molecular biology, genetics, microbiology, immunology, biochemistry, pharmacology, physiology and pathology [...]

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28

Spray, David C. "MOLECULAR PHYSIOLOGY OF GAP JUNCTION CHANNELS." Clinical and Experimental Pharmacology and Physiology 23, no. 12 (December 1996): 1038–40. http://dx.doi.org/10.1111/j.1440-1681.1996.tb01165.x.

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29

Richards, Elaine M., Yi Hua, and Maureen Keller-Wood. "Pharmacology and Physiology of Ovine Corticosteroid Receptors." Neuroendocrinology 77, no. 1 (2003): 2–14. http://dx.doi.org/10.1159/000068335.

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30

Hosey, M. Marlene, and Michel Lazdunski. "Calcium channels: Molecular pharmacology, structure and regulation." Journal of Membrane Biology 104, no. 2 (September 1988): 81–105. http://dx.doi.org/10.1007/bf01870922.

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31

Ling, Wei, Yan-Mei Huang, Yong-Chao Qiao, Xiao-Xi Zhang, and Hai-Lu Zhao. "Human Amylin: From Pathology to Physiology and Pharmacology." Current Protein & Peptide Science 20, no. 9 (September 17, 2019): 944–57. http://dx.doi.org/10.2174/1389203720666190328111833.

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The histopathological hallmark of type 2 diabetes is islet amyloid implicated in the developing treatment options. The major component of human islet amyloid is 37 amino acid peptide known as amylin or islet amyloid polypeptide (IAPP). Amylin is an important hormone that is co-localized, copackaged, and co-secreted with insulin from islet β cells. Physiologically, amylin regulates glucose homeostasis by inhibiting insulin and glucagon secretion. Furthermore, amylin modulates satiety and inhibits gastric emptying via the central nervous system. Normally, human IAPP is soluble and natively unfolded in its monomeric state. Pathologically, human IAPP has a propensity to form oligomers and aggregate. The oligomers show misfolded α-helix conformation and can further convert themselves to β-sheet-rich fibrils as amyloid deposits. The pathological findings and physiological functions of amylin have led to the introduction of pramlintide, an amylin analog, for the treatment of diabetes. The history of amylin’s discovery is a representative example of how a pathological finding can translate into physiological exploration and lead to pharmacological intervention. Understanding the importance of transitioning from pathology to physiology and pharmacology can provide novel insight into diabetes mellitus and Alzheimer's disease.

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32

Carrasco, P. "Pharmacology of second generation low molecular weight heparins." Pathophysiology of Haemostasis and Thrombosis 32, no. 5-6 (2002): 401–2. http://dx.doi.org/10.1159/000073609.

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33

Pantic, Igor, David Sarenac, Mila Cetkovic, Milan Milisavljevic, Rastko Rakocevic, and Sandor Kasas. "Silver Nanomaterials in Contemporary Molecular Physiology Research." Current Medicinal Chemistry 27, no. 3 (February 19, 2020): 411–22. http://dx.doi.org/10.2174/0929867325666180719110432.

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Silver nanoparticles have numerous potential applications in engineering, industry, biology and medicine. Because of their unique chemical properties, they have become the focus of many research teams all over the world. Silver nanoparticles may exhibit significant antimicrobial and anticancer effects, and they may be a valuable part of various bioassays and biosensors. However, the research on biological and medical uses of AgNPs is related with numerous potential problems and challenges that need to be overcome in the years ahead. Possible toxic effects of silver nanoparticles on living organisms represent a great concern, both in clinical medicine and public health. Nevertheless, in the future, it may be expected that all metallic nanomaterials, including the ones made from silver will greatly benefit almost all natural scientific fields. In this short review, we focus on the recent research on silver nanoparticles in experimental physiology, as well as other areas of fundamental and clinical medicine.

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34

Ahles, Andrea, and Stefan Engelhardt. "Polymorphic Variants of Adrenoceptors: Pharmacology, Physiology, and Role in Disease." Pharmacological Reviews 66, no. 3 (June 13, 2014): 598–637. http://dx.doi.org/10.1124/pr.113.008219.

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35

BARNES, NEIL, JANE EVANS, JERZY ZAKRZEWSKI, PRISCILLA PIPER, and JOHN COSTELLO. "Pharmacology and Physiology of Leukotrienes and Their Antagonists." Annals of the New York Academy of Sciences 524, no. 1 Biology of th (April 1988): 369–78. http://dx.doi.org/10.1111/j.1749-6632.1988.tb38559.x.

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36

Reinscheid, Rainer K., and Chiara Ruzza. "Pharmacology, Physiology and Genetics of the Neuropeptide S System." Pharmaceuticals 14, no. 5 (April 23, 2021): 401. http://dx.doi.org/10.3390/ph14050401.

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The Neuropeptide S (NPS) system is a rather ‘young’ transmitter system that was discovered and functionally described less than 20 years ago. This review highlights the progress that has been made in elucidating its pharmacology, anatomical distribution, and functional involvement in a variety of physiological effects, including behavior and immune functions. Early on, genetic variations of the human NPS receptor (NPSR1) have attracted attention and we summarize current hypotheses of genetic linkage with disease and human behaviors. Finally, we review the therapeutic potential of future drugs modulating NPS signaling. This review serves as an introduction to the broad collection of original research papers and reviews from experts in the field that are presented in this Special Issue.

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37

Gregory, Karen J., and Cyril Goudet. "International Union of Basic and Clinical Pharmacology. CXI. Pharmacology, Signaling, and Physiology of Metabotropic Glutamate Receptors." Pharmacological Reviews 73, no. 1 (December 23, 2020): 521–69. http://dx.doi.org/10.1124/pr.119.019133.

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38

Koepsell, H., V. Gorboulev, and P. Arndt. "Molecular Pharmacology of Organic Cation Transporters in Kidney." Journal of Membrane Biology 167, no. 2 (January 15, 1999): 103–17. http://dx.doi.org/10.1007/s002329900475.

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39

Lederis, K., J. N. Fryer, and C. R. Yulis. "The fish neuropeptide urotensin I: Its physiology and pharmacology." Peptides 6 (January 1985): 353–61. http://dx.doi.org/10.1016/0196-9781(85)90397-3.

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40

Arterburn, Jeffrey B., and Eric R. Prossnitz. "G Protein–Coupled Estrogen Receptor GPER: Molecular Pharmacology and Therapeutic Applications." Annual Review of Pharmacology and Toxicology 63, no. 1 (January 20, 2023): 295–320. http://dx.doi.org/10.1146/annurev-pharmtox-031122-121944.

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The actions of estrogens and related estrogenic molecules are complex and multifaceted in both sexes. A wide array of natural, synthetic, and therapeutic molecules target pathways that produce and respond to estrogens. Multiple receptors promulgate these responses, including the classical estrogen receptors of the nuclear hormone receptor family (estrogen receptors α and β), which function largely as ligand-activated transcription factors, and the 7-transmembrane G protein–coupled estrogen receptor, GPER, which activates a diverse array of signaling pathways. The pharmacology and functional roles of GPER in physiology and disease reveal important roles in responses to both natural and synthetic estrogenic compounds in numerous physiological systems. These functions have implications in the treatment of myriad disease states, including cancer, cardiovascular diseases, and metabolic disorders. This review focuses on the complex pharmacology of GPER and summarizes major physiological functions of GPER and the therapeutic implications and ongoing applications of GPER-targeted compounds.

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41

Iynedjian, P. B. "Molecular Physiology of Mammalian Glucokinase." Cellular and Molecular Life Sciences 66, no. 1 (August 26, 2008): 27–42. http://dx.doi.org/10.1007/s00018-008-8322-9.

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42

Gamba, Gerardo. "Molecular Physiology and Pathophysiology of Electroneutral Cation-Chloride Cotransporters." Physiological Reviews 85, no. 2 (April 2005): 423–93. http://dx.doi.org/10.1152/physrev.00011.2004.

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Electroneutral cation-Cl−cotransporters compose a family of solute carriers in which cation (Na+or K+) movement through the plasma membrane is always accompanied by Cl−in a 1:1 stoichiometry. Seven well-characterized members include one gene encoding the thiazide-sensitive Na+−Cl−cotransporter, two genes encoding loop diuretic-sensitive Na+−K+−2Cl−cotransporters, and four genes encoding K+−Cl−cotransporters. These membrane proteins are involved in several physiological activities including transepithelial ion absorption and secretion, cell volume regulation, and setting intracellular Cl−concentration below or above its electrochemical potential equilibrium. In addition, members of this family play an important role in cardiovascular and neuronal pharmacology and pathophysiology. Some of these cotransporters serve as targets for loop diuretics and thiazide-type diuretics, which are among the most commonly prescribed drugs in the world, and inactivating mutations of three members of the family cause inherited diseases such as Bartter's, Gitelman's, and Anderman's diseases. Major advances have been made in the past decade as consequences of molecular identification of all members in this family. This work is a comprehensive review of the knowledge that has evolved in this area and includes molecular biology of each gene, functional properties of identified cotransporters, structure-function relationships, and physiological and pathophysiological roles of each cotransporter.

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43

Capozzi, Megan E., David A. D’Alessio, and Jonathan E. Campbell. "The past, present, and future physiology and pharmacology of glucagon." Cell Metabolism 34, no. 11 (November 2022): 1654–74. http://dx.doi.org/10.1016/j.cmet.2022.10.001.

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44

Ciarimboli, Giuliano. "Physiology, Biochemistry and Pharmacology of Transporters for Organic Cations 2.0." International Journal of Molecular Sciences 23, no. 11 (June 6, 2022): 6328. http://dx.doi.org/10.3390/ijms23116328.

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45

Illes, Peter, and J. Alexandre Ribeiro. "Molecular physiology of P2 receptors in the central nervous system." European Journal of Pharmacology 483, no. 1 (January 2004): 5–17. http://dx.doi.org/10.1016/j.ejphar.2003.10.030.

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46

Fay, Fredric S., Shinobu Yagi, Takeo Iloh, John McCarron, Graham McGeown, John Walsh, Mitsuo lkebe, and Edwin D. W. Moore. "Cellular and molecular physiology of calcium signalling in smooth muscle cells." Japanese Journal of Pharmacology 58 (1992): 35–40. http://dx.doi.org/10.1016/s0021-5198(19)59891-2.

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47

Hidaka, H., and T. Ishikawa. "Molecular pharmacology of calmodulin pathways in the cell functions." Cell Calcium 13, no. 6-7 (June 1992): 465–72. http://dx.doi.org/10.1016/0143-4160(92)90059-2.

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48

Piermarini, Peter M., Jerod S. Denton, and Daniel R. Swale. "The Molecular Physiology and Toxicology of Inward Rectifier Potassium Channels in Insects." Annual Review of Entomology 67, no. 1 (January 7, 2022): 125–42. http://dx.doi.org/10.1146/annurev-ento-062121-063338.

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Inward rectifier K+ (Kir) channels have been studied extensively in mammals, where they play critical roles in health and disease. In insects, Kir channels have recently been found to be key regulators of diverse physiological processes in several tissues. The importance of Kir channels in insects has positioned them to serve as emerging targets for the development of insecticides with novel modes of action. In this article, we provide the first comprehensive review of insect Kir channels, highlighting the rapid progress made in understanding their molecular biology, physiological roles, pharmacology, and toxicology. In addition, we highlight key gaps in our knowledge and suggest directions for future research to advance our understanding of Kir channels and their roles in insect physiology. Further knowledge of their functional roles will also facilitate their exploitation as targets for controlling arthropod pests and vectors of economic, medical, and/or veterinary relevance.

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49

Samodelov, Sophia L., Gerd A. Kullak-Ublick, Zhibo Gai, and Michele Visentin. "Organic Cation Transporters in Human Physiology, Pharmacology, and Toxicology." International Journal of Molecular Sciences 21, no. 21 (October 24, 2020): 7890. http://dx.doi.org/10.3390/ijms21217890.

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Individual cells and epithelia control the chemical exchange with the surrounding environment by the fine-tuned expression, localization, and function of an array of transmembrane proteins that dictate the selective permeability of the lipid bilayer to small molecules, as actual gatekeepers to the interface with the extracellular space. Among the variety of channels, transporters, and pumps that localize to cell membrane, organic cation transporters (OCTs) are considered to be extremely relevant in the transport across the plasma membrane of the majority of the endogenous substances and drugs that are positively charged near or at physiological pH. In humans, the following six organic cation transporters have been characterized in regards to their respective substrates, all belonging to the solute carrier 22 (SLC22) family: the organic cation transporters 1, 2, and 3 (OCT1–3); the organic cation/carnitine transporter novel 1 and 2 (OCTN1 and N2); and the organic cation transporter 6 (OCT6). OCTs are highly expressed on the plasma membrane of polarized epithelia, thus, playing a key role in intestinal absorption and renal reabsorption of nutrients (e.g., choline and carnitine), in the elimination of waste products (e.g., trimethylamine and trimethylamine N-oxide), and in the kinetic profile and therapeutic index of several drugs (e.g., metformin and platinum derivatives). As part of the Special Issue Physiology, Biochemistry, and Pharmacology of Transporters for Organic Cations, this article critically presents the physio-pathological, pharmacological, and toxicological roles of OCTs in the tissues in which they are primarily expressed.

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Rattray, Marcus. "The neuropeptide cholecystokinin (CCK): Anatomy and biochemistry, receptors, pharmacology and physiology." Neurochemistry International 17, no. 4 (January 1990): 633–34. http://dx.doi.org/10.1016/0197-0186(90)90053-v.

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