Renal Aquaporins
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Activity-Dependent Modulation of Neuronal Sodium Channel Expression Joshua Peter Klein Yale University
Yale University EliScholar – A Digital Platform for Scholarly Publishing at Yale Yale Medicine Thesis Digital Library School of Medicine 5-2004 Activity-dependent modulation of neuronal sodium channel expression Joshua Peter Klein Yale University. Follow this and additional works at: http://elischolar.library.yale.edu/ymtdl Part of the Medicine and Health Sciences Commons Recommended Citation Klein, Joshua Peter, "Activity-dependent modulation of neuronal sodium channel expression" (2004). Yale Medicine Thesis Digital Library. 2198. http://elischolar.library.yale.edu/ymtdl/2198 This Open Access Dissertation is brought to you for free and open access by the School of Medicine at EliScholar – A Digital Platform for Scholarly Publishing at Yale. It has been accepted for inclusion in Yale Medicine Thesis Digital Library by an authorized administrator of EliScholar – A Digital Platform for Scholarly Publishing at Yale. For more information, please contact [email protected]. ACTIVITY-DEPENDENT MODULATION OF NEURONAL SODIUM CHANNEL EXPRESSION A Dissertation Presented to the Faculty of the Graduate School of Yale University in Candidacy for the Degree of Doctor of Philosophy by Joshua Peter Klein Dissertation Director: Stephen G. Waxman, M.D.,Ph.D. May, 2004 Reproduced with permission of the copyright owner. Further reproduction prohibited without permission. ACTiViTY-DEPENDENT MODULATION OF NEURONAL SODIUM CHANNEL EXPRESSION Joshua Peter Klein 2004 ABSTRACT Action potentials initiate via the voltage-dependent opening of plasma membrane-associated sodium channels. The number and type of sodium channels in a neuronal membrane determine the quantity of sodium current that results from a given stimulus. The expression of sodium channels in neurons is plastic, and is not only altered by injury and disease, but also by subtle changes in physiologic environment. -
Kidney, Renal Tubule – Dilation
Kidney, Renal Tubule – Dilation Figure Legend: Figure 1 Kidney, Renal tubule - Dilation in a male B6C3F1 mouse from a chronic study. Dilated tubules are noted as tracts running through the cortex and outer medulla. Figure 2 Kidney, Renal tubule - Dilation in a male F344/N rat from a chronic study. Tubule dilation is present throughout the outer stripe of the outer medulla, extending into the cortex. Figure 3 Kidney, Renal tubule - Dilation in a male B6C3F1 mouse from a chronic study. Slight tubule dilation is associated with degeneration and necrosis. Figure 4 Kidney, Renal tubule - Dilation in a male F344/N rat from a chronic study. Tubule dilation is associated with chronic progressive nephropathy. Comment: Renal tubule dilation may occur anywhere along the nephron or collecting duct system. It may occur in focal areas or as tracts running along the entire length of kidney sections (Figure 1). 1 Kidney, Renal Tubule – Dilation Renal tubule dilation may occur from xenobiotic administration, secondary mechanisms, or an unknown pathogenesis (see Kidney – Nephropathy, Obstructive (Figure 2). Dilation may result from direct toxic injury to the tubule epithelium interfering with absorption and secretion (Figure 3). It may also occur secondary to renal ischemia or from prolonged diuresis related to drug administration. Secondary mechanisms of tubule dilation may result from lower urinary tract obstruction, the deposition of tubule crystals, interstitial inflammation and/or fibrosis, and chronic progressive nephropathy (Figure 4). A few dilated tubules may be regarded as normal histologic variation. Recommendation: Renal tubule dilation should be diagnosed and given a severity grade. The location of tubule dilation should be included in the diagnosis as a site modifier. -
Entrez Symbols Name Termid Termdesc 117553 Uba3,Ube1c
Entrez Symbols Name TermID TermDesc 117553 Uba3,Ube1c ubiquitin-like modifier activating enzyme 3 GO:0016881 acid-amino acid ligase activity 299002 G2e3,RGD1310263 G2/M-phase specific E3 ubiquitin ligase GO:0016881 acid-amino acid ligase activity 303614 RGD1310067,Smurf2 SMAD specific E3 ubiquitin protein ligase 2 GO:0016881 acid-amino acid ligase activity 308669 Herc2 hect domain and RLD 2 GO:0016881 acid-amino acid ligase activity 309331 Uhrf2 ubiquitin-like with PHD and ring finger domains 2 GO:0016881 acid-amino acid ligase activity 316395 Hecw2 HECT, C2 and WW domain containing E3 ubiquitin protein ligase 2 GO:0016881 acid-amino acid ligase activity 361866 Hace1 HECT domain and ankyrin repeat containing, E3 ubiquitin protein ligase 1 GO:0016881 acid-amino acid ligase activity 117029 Ccr5,Ckr5,Cmkbr5 chemokine (C-C motif) receptor 5 GO:0003779 actin binding 117538 Waspip,Wip,Wipf1 WAS/WASL interacting protein family, member 1 GO:0003779 actin binding 117557 TM30nm,Tpm3,Tpm5 tropomyosin 3, gamma GO:0003779 actin binding 24779 MGC93554,Slc4a1 solute carrier family 4 (anion exchanger), member 1 GO:0003779 actin binding 24851 Alpha-tm,Tma2,Tmsa,Tpm1 tropomyosin 1, alpha GO:0003779 actin binding 25132 Myo5b,Myr6 myosin Vb GO:0003779 actin binding 25152 Map1a,Mtap1a microtubule-associated protein 1A GO:0003779 actin binding 25230 Add3 adducin 3 (gamma) GO:0003779 actin binding 25386 AQP-2,Aqp2,MGC156502,aquaporin-2aquaporin 2 (collecting duct) GO:0003779 actin binding 25484 MYR5,Myo1e,Myr3 myosin IE GO:0003779 actin binding 25576 14-3-3e1,MGC93547,Ywhah -
Aquaporin Channels in the Heart—Physiology and Pathophysiology
International Journal of Molecular Sciences Review Aquaporin Channels in the Heart—Physiology and Pathophysiology Arie O. Verkerk 1,2,* , Elisabeth M. Lodder 2 and Ronald Wilders 1 1 Department of Medical Biology, Amsterdam University Medical Centers, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands; [email protected] 2 Department of Experimental Cardiology, Amsterdam University Medical Centers, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands; [email protected] * Correspondence: [email protected]; Tel.: +31-20-5664670 Received: 29 March 2019; Accepted: 23 April 2019; Published: 25 April 2019 Abstract: Mammalian aquaporins (AQPs) are transmembrane channels expressed in a large variety of cells and tissues throughout the body. They are known as water channels, but they also facilitate the transport of small solutes, gasses, and monovalent cations. To date, 13 different AQPs, encoded by the genes AQP0–AQP12, have been identified in mammals, which regulate various important biological functions in kidney, brain, lung, digestive system, eye, and skin. Consequently, dysfunction of AQPs is involved in a wide variety of disorders. AQPs are also present in the heart, even with a specific distribution pattern in cardiomyocytes, but whether their presence is essential for proper (electro)physiological cardiac function has not intensively been studied. This review summarizes recent findings and highlights the involvement of AQPs in normal and pathological cardiac function. We conclude that AQPs are at least implicated in proper cardiac water homeostasis and energy balance as well as heart failure and arsenic cardiotoxicity. However, this review also demonstrates that many effects of cardiac AQPs, especially on excitation-contraction coupling processes, are virtually unexplored. -
Hereditary Kidney Disorders
A. Stavljenić-Rukavina Hereditary kidney disorders How to Cite this article: Hereditary Kidney Disorders- eJIFCC 20/01 2009 http://www.ifcc.org 5. HEREDITARY KIDNEY DISORDERS Ana Stavljenić-Rukavina 5.1 Introduction Hereditary kidney disorders represent significant risk for the development of end stage renal desease (ESRD). Most of them are recognized in childhood, or prenataly particularly those phenotypicaly expressed as anomalies on ultrasound examination (US) during pregnancy. They represent almost 50% of all fetal malformations detected by US (1). Furthermore many of urinary tract malformations are associated with renal dysplasia which leeds to renal failure. Recent advances in molecular genetics have made a great impact on better understanding of underlying molecular mechanisms in different kidney and urinary tract disorders found in childhood or adults. Even some of clinical syndromes were not recognized earlier as genetic one. In monogenic kidney diseases gene mutations have been identified for Alport syndrome and thin basement membrane disease, autosomal dominant polycystic kidney disease, and tubular transporter disorders. There is evident progress in studies of polygenic renal disorders as glomerulopathies and diabetic nephropathy. The expanded knowledge on renal physiology and pathophysiology by analyzing the phenotypes caused by defected genes might gain to earlier diagnosis and provide new diagnostic and prognostic tool. The global increasing number of patients with ESRD urges the identification of molecular pathways involved in renal pathophysiology in order to serve as targets for either prevention or intervention. Molecular genetics nowadays possess significant tools that can be used to identify genes involved in renal disease including gene expression arrays, linkage analysis and association studies. -
Variants in the KCNE1 Or KCNE3 Gene and Risk of Ménière’S Disease: a Meta-Analysis
Journal of Vestibular Research 25 (2015) 211–218 211 DOI 10.3233/VES-160569 IOS Press Variants in the KCNE1 or KCNE3 gene and risk of Ménière’s disease: A meta-analysis Yuan-Jun Li, Zhan-Guo Jin and Xian-Rong Xu∗ The Center of Clinical Aviation Medicine, General Hospital of Air Force, Beijing, China Received 1 August 2015 Accepted 8 December 2015 Abstract. BACKGROUND: Ménière’s disease (MD) is defined as an idiopathic disorder of the inner ear characterized by the triad of tinnitus, vertigo, and sensorineural hearing loss. Although many studies have evaluated the association between variants in the KCNE1 or KCNE3 gene and MD risk, debates still exist. OBJECTIVE: Our aim is to evaluate the association between KCNE gene variants, including KCNE1 rs1805127 and KCNE3 rs2270676, and the risk of MD by a systematic review. METHODS: We searched the literature in PubMed, SCOPUS and EMBASE through May 2015. We calculated pooled odds ra- tios (OR) and 95% confidence intervals (CIs) using a fixed-effects model or a random-effects model for the risk to MD associated with different KCNE gene variants. The heterogeneity assumption decided the effect model. RESULTS: A total of three relevant studies, with 302 MD cases and 515 controls, were included in this meta-analysis. The results indicated that neither the KCNE1 rs1805127 variant (for G vs. A: OR = 0.724, 95%CI 0.320, 1.638, P = 0.438), nor the KCNE3 rs2270676 variant (for T vs. C: OR = 0.714, 95%CI 0.327, 1.559, P = 0.398) was associated with MD risk. -
Inherited Renal Tubulopathies—Challenges and Controversies
G C A T T A C G G C A T genes Review Inherited Renal Tubulopathies—Challenges and Controversies Daniela Iancu 1,* and Emma Ashton 2 1 UCL-Centre for Nephrology, Royal Free Campus, University College London, Rowland Hill Street, London NW3 2PF, UK 2 Rare & Inherited Disease Laboratory, London North Genomic Laboratory Hub, Great Ormond Street Hospital for Children National Health Service Foundation Trust, Levels 4-6 Barclay House 37, Queen Square, London WC1N 3BH, UK; [email protected] * Correspondence: [email protected]; Tel.: +44-2381204172; Fax: +44-020-74726476 Received: 11 February 2020; Accepted: 29 February 2020; Published: 5 March 2020 Abstract: Electrolyte homeostasis is maintained by the kidney through a complex transport function mostly performed by specialized proteins distributed along the renal tubules. Pathogenic variants in the genes encoding these proteins impair this function and have consequences on the whole organism. Establishing a genetic diagnosis in patients with renal tubular dysfunction is a challenging task given the genetic and phenotypic heterogeneity, functional characteristics of the genes involved and the number of yet unknown causes. Part of these difficulties can be overcome by gathering large patient cohorts and applying high-throughput sequencing techniques combined with experimental work to prove functional impact. This approach has led to the identification of a number of genes but also generated controversies about proper interpretation of variants. In this article, we will highlight these challenges and controversies. Keywords: inherited tubulopathies; next generation sequencing; genetic heterogeneity; variant classification. 1. Introduction Mutations in genes that encode transporter proteins in the renal tubule alter kidney capacity to maintain homeostasis and cause diseases recognized under the generic name of inherited tubulopathies. -
Molecular Mechanism of Water Channel Aquaporin-2 Trafficking Yumi Noda1,* and Sei Sasaki1
J Pharmacol Sci 96, 249 – 254 (2004) Journal of Pharmacological Sciences ©2004 The Japanese Pharmacological Society Forum Minireview Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases: Molecular Mechanism of Water Channel Aquaporin-2 Trafficking Yumi Noda1,* and Sei Sasaki1 1Department of Nephrology, Graduate School, Tokyo Medical and Dental University, Tokyo 113-8519, Japan Received September 29, 2004; Accepted October 13, 2004 Abstract. Targeted positioning of water channel aquaporin-2 (AQP2) strictly regulates body water homeostasis. Trafficking of AQP2 to the apical membrane is critical for the reabsorption of water in renal collecting ducts. Besides the cAMP-mediated effect of vasopressin on AQP2 trafficking to the apical membrane, other signaling cascades also induce this sorting. Recently, AQP2-binding proteins that directly regulate this trafficking have been uncovered: SPA-1, a GTPase-activating protein (GAP) for Rap1, and cytoskeletal protein actin. This review summarizes recent advances related to the trafficking mechanism of AQP2 and its defect causing nephrogenic diabetes insipidus (NDI). Keywords: aquaporin-2, PKA phosphorylation, missorting, Rho, cytoskeleton Introduction receptors located in the hypothalamus are activated and stimulate the secretion of antidiuretic hormone arginine Body water homeostasis is essential for survival of vasopressin (AVP) from the posterior pituitary (22, 23). mammals. Water transport occurs through a specialized After it is released systemically, vasopressin binds to channel called aquaporin (AQP) (1 – 4). AQPs play an vasopressin type 2 receptor (V2R) located on the baso- important role in reabsorption of water and in concentra- lateral membrane of the renal collecting duct principal tion of urine in the kidney. Out of 13 aquaporin iso- cells (24). -
Ubiquitination of Aquaporin-2 in the Kidney
Electrolytes & Blood Pressure 7:1-4, 2009 1 Review article 1) Ubiquitination of Aquaporin-2 in the Kidney Yu-Jung Lee, M.D. and Tae-Hwan Kwon, M.D. Department of Biochemistry and Cell Biology, School of Medicine, Kyungpook National University, Daegu, Korea Ubiquitination is known to be important for endocytosis and lysosomal degradation of aquaporin-2 (AQP2). Ubiquitin (Ub) is covalently attached to the lysine residue of the substrate proteins and activation and attach - ment of Ub to a target protein is mediated by the action of three enzymes (i.e., E1, E2, and E3). In particular, E3 Ub-protein ligases are known to have substrate specificity. This minireview will discuss the ubiquitination of AQP2 and identification of potential E3 Ub-protein ligases for 1-deamino-8-D-arginine vasopressin (dDAVP)-dependent AQP2 regulation. Key Words : kidney tubules, collecting; ubiquitination; vasopressins; aquaporin 2 The kidneys are responsible for the regulation of body This process produces concentrated urine and is essential water and electrolyte metabolism. Thus, understanding of for regulation of body water metabolism 6) . In contrast to the underlying mechanisms for renal water transport is the well-established signaling pathways for the vaso- critical. Water permeability along the nephron has already pressin-regulated AQP2 trafficking and up-regulation of been well characterized in the mammalian kidney 1) . AQP2 expression, the underlying mechanisms for AQP2 Approximately, 180 L/day of glomerular filtrate is gen- endocytosis and intracellular degradation of AQP2 protein erated in an adult human, more than 80-90% of the glomer- are unclear. So far, two hormones (prostaglandin E2 and ular filtrate is constitutively reabsorbed by the highly water dopamine) cause AQP2 internalization independent of permeable proximal tubules and descending thin limbs of S256 dephosphorylation 7, 8) . -
Allosteric Mechanism of Water Channel Gating by Ca2+–Calmodulin
Portland State University PDXScholar Chemistry Faculty Publications and Presentations Chemistry 9-2013 Allosteric Mechanism of Water Channel Gating by Ca2+–calmodulin Steve Reichow [email protected] Daniel M. Clemens University of California, Irvine J. Alfredo Freites University of California, Irvine Karin L. Németh-Cahalan University of California, Irvine Matthias Heyden University of California, Irvine See next page for additional authors Let us know how access to this document benefits ouy . Follow this and additional works at: https://pdxscholar.library.pdx.edu/chem_fac Part of the Biochemistry Commons, and the Structural Biology Commons Citation Details Reichow, S. L., Clemens, D. M., Freites, J. A., Németh-Cahalan, K. L., Heyden, M., Tobias, D. J., ... & Gonen, T. (2013). Allosteric mechanism of water-channel gating by Ca2+–calmodulin. Nature structural & molecular biology, 20(9), 1085-1092. This Post-Print is brought to you for free and open access. It has been accepted for inclusion in Chemistry Faculty Publications and Presentations by an authorized administrator of PDXScholar. For more information, please contact [email protected]. Authors Steve Reichow, Daniel M. Clemens, J. Alfredo Freites, Karin L. Németh-Cahalan, Matthias Heyden, Douglas J. Tobias, James E. Hall, and Tamir Gonen This post-print is available at PDXScholar: https://pdxscholar.library.pdx.edu/chem_fac/198 HHS Public Access Author manuscript Author Manuscript Author ManuscriptNat Struct Author Manuscript Mol Biol. Author Author Manuscript manuscript; available in PMC 2014 March 01. Published in final edited form as: Nat Struct Mol Biol. 2013 September ; 20(9): 1085–1092. doi:10.1038/nsmb.2630. Allosteric mechanism of water channel gating by Ca2+– calmodulin Steve L. -
University of Florida Thesis Or Dissertation Formatting
NOVEL GENOME ENGINEERING STRATEGIES TO MODEL REPEAT EXPANSION DISEASES By RUAN OLIVEIRA A DISSERTATION PRESENTED TO THE GRADUATE SCHOOL OF THE UNIVERSITY OF FLORIDA IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY UNIVERSITY OF FLORIDA 2018 © 2018 Ruan Oliveira To my parents, whose hard work and continuous support allowed me to obtain a doctoral degree ACKNOWLEDGMENTS First, I would like to thank my parents, Rosane and Rudimar Oliveira, for their unconditional love and uninterrupted support over the last 26 years. Their commitment to my education makes me prouder than my own graduate degree. Next, I would like to express my deepest gratitude to Andriel Fenner, whose ears endured my daily complaints about graduate school. His continued support kept me sane and his company eased the process of transitioning into adulthood (in progress). Also, I would like to thank Maria Seabra for crossing my path in 2010, when my sophomore version went to a conference in São Paulo and met this loud and contagious woman who was unable to stop talking about her experiences as a Ph.D. student at the University of Florida. If I did not meet Maria, I would have never heard of Gainesville. I would like to thank my Ph.D. mentor, Dr. Maurice Swanson, for giving me freedom to pursue my own ideas and trusting me. I also thank Maury for teaching me how to be a scientist and for his patience with my learning curve. I am grateful to Myrna Stenberg, who taught me discipline and offered me psychological support in the moments I needed the most. -
Embryology of the Kidney Rizaldy Paz Scott | Yoshiro Maezawa | Jordan Kreidberg | Susan E
1 Embryology of the Kidney Rizaldy Paz Scott | Yoshiro Maezawa | Jordan Kreidberg | Susan E. Quaggin CHAPTER OUTLINE MAMMALIAN KIDNEY DEVELOPMENT, 2 MOLECULAR GENETICS OF MODEL SYSTEMS TO STUDY KIDNEY NEPHROGENESIS, 22 DEVELOPMENT, 8 GENETIC ANALYSIS OF MAMMALIAN KIDNEY DEVELOPMENT, 15 KEY POINTS • The development of the kidney relies on reciprocal signaling and inductive interactions between neighboring cells. • Epithelial cells that comprise the tubular structures of the kidney are derived from two distinct cell lineages: the ureteric epithelia lineage that branches and gives rise to collecting ducts and the nephrogenic mesenchyme lineage that undergoes mesenchyme to epithelial transition to form connecting tubules, distal tubules, the loop of Henle, proximal tubules, parietal epithelial cells, and podocytes. • Nephrogenesis and nephron endowment requires an epigenetically regulated balance between nephron progenitor self-renewal and epithelial differentiation. • The timing of incorporation of nephron progenitor cells into nascent nephrons predicts their positional identity within the highly patterned mature nephron. • Stromal cells and their derivatives coregulate ureteric branching morphogenesis, nephrogenesis, and vascular development. • Endothelial cells track the development of the ureteric epithelia and establish the renal vasculature through a combination of vasculogenic and angiogenic processes. • Collecting duct epithelia have an inherent plasticity enabling them to switch between principal and intercalated cell identities. MAMMALIAN KIDNEY DEVELOPMENT The filtration function of the kidneys is accomplished by basic units called nephrons (Fig. 1.1). Humans on average have 1 million nephrons per adult kidney but the range of ANATOMIC OVERVIEW OF THE 4 MAMMALIAN KIDNEY total nephrons is highly variable across human populations. Each mouse kidney may contain up to 12,000–16,000 nephrons The kidney is a sophisticated, highly vascularized organ that depending on the strain.5 This wide range in nephron number plays a central role in overall body homeostasis.