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Relevant bibliographies by topics / KC1 cotransporter

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Academic literature on the topic 'KC1 cotransporter'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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Journal articles on the topic "KC1 cotransporter"

1

Holtzman, Eli J., Sumit Kumar, Carol A. Faaland, et al. "Cloning, characterization, and gene organization of K-Cl cotransporter from pig and human kidney and C. elegans." American Journal of Physiology-Renal Physiology 275, no. 4 (1998): F550—F564. http://dx.doi.org/10.1152/ajprenal.1998.275.4.f550.

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We isolated and characterized the cDNAs for the human, pig, and Caenorhabditis elegansK-Cl cotransporters. The pig and human homologs are 94% identical and contain 1,085 and 1,086 amino acids, respectively. The deduced protein of the C. elegans K-Cl cotransporter clone (CE-KCC1) contains 1,003 amino acids. The mammalian K-Cl cotransporters share ∼45% similarity with CE-KCC1. Hydropathy analyses of the three clones indicate typical KCC topology patterns with 12 transmembrane segments, large extracellular loops between transmembrane domains 5 and 6 (unique to KCC), and large COOH-terminal domain

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2

Race, Joanne E., Fadi N. Makhlouf, Paul J. Logue, Frederick H. Wilson, Philip B. Dunham, and Eli J. Holtzman. "Molecular cloning and functional characterization of KCC3, a new K-Cl cotransporter." American Journal of Physiology-Cell Physiology 277, no. 6 (1999): C1210—C1219. http://dx.doi.org/10.1152/ajpcell.1999.277.6.c1210.

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We isolated and characterized a novel K-Cl cotransporter, KCC3, from human placenta. The deduced protein contains 1,150 amino acids. KCC3 shares 75–76% identity at the amino acid level with human, pig, rat, and rabbit KCC1 and 67% identity with rat KCC2. KCC3 is 40 and 33% identical to two Caenorhabditis elegans K-Cl cotransporters and ∼20% identical to other members of the cation-chloride cotransporter family (CCC), two Na-K-Cl cotransporters (NKCC1, NKCC2), and the Na-Cl cotransporter (NCC). Hydropathy analysis indicates a typical KCC topology with 12 transmembrane domains, a large extracell

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3

Gillen, Christopher M., and Bliss Forbush. "Functional interaction of the K-Cl cotransporter (KCC1) with the Na-K-Cl cotransporter in HEK-293 cells." American Journal of Physiology-Cell Physiology 276, no. 2 (1999): C328—C336. http://dx.doi.org/10.1152/ajpcell.1999.276.2.c328.

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We have studied the regulation of the K-Cl cotransporter KCC1 and its functional interaction with the Na-K-Cl cotransporter. K-Cl cotransporter activity was substantially activated in HEK-293 cells overexpressing KCC1 (KCC1-HEK) by hypotonic cell swelling, 50 mM external K, and pretreatment with N-ethylmaleimide (NEM). Bumetanide inhibited 86Rb efflux in KCC1-HEK cells after cell swelling [inhibition constant ( K i) ∼190 μM] and pretreatment with NEM ( K i ∼60 μM). Thus regulation of KCC1 is consistent with properties of the red cell K-Cl cotransporter. To investigate functional interactions b

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Crable, Scott C., Suzan M. Hammond, Richard Papes, et al. "Multiple isoforms of the KC1 cotransporter are expressed in sickle and normal erythroid cells." Experimental Hematology 33, no. 6 (2005): 624–31. http://dx.doi.org/10.1016/j.exphem.2005.02.006.

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5

Strange, Kevin, Thomas D. Singer, Rebecca Morrison, and Eric Delpire. "Dependence of KCC2 K-Cl cotransporter activity on a conserved carboxy terminus tyrosine residue." American Journal of Physiology-Cell Physiology 279, no. 3 (2000): C860—C867. http://dx.doi.org/10.1152/ajpcell.2000.279.3.c860.

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K-Cl cotransporters (KCC) play fundamental roles in ionic and osmotic homeostasis. To date, four mammalian KCC genes have been identified. KCC2 is expressed exclusively in neurons. Injection of Xenopus oocytes with KCC2 cRNA induced a 20-fold increase in Cl−-dependent, furosemide-sensitive K+ uptake. Oocyte swelling increased KCC2 activity 2–3 fold. A canonical tyrosine phosphorylation site is located in the carboxy termini of KCC2 (R1081–Y1087) and KCC4, but not in other KCC isoforms. Pharmacological studies, however, revealed no regulatory role for phosphorylation of KCC2 tyrosine residues.

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Pan, Dao, Theodosia A. Kalfa, Daren Wang, et al. "Change in Expressional Profile of KCl Cotransporter Genes during Human Erythroid Differentiation." Blood 110, no. 11 (2007): 1709. http://dx.doi.org/10.1182/blood.v110.11.1709.1709.

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Abstract Maintenance of cell volume by regulated cation transport is a fundamental cellular process. The KCl cotransporter (KCC) contributes to red blood cell (RBC) volume regulation, especially in reticulocytes. Erythroid K-Cl cotransport activity is increased in sickle cells (SS RBC) and contribute to SS RBC dehydration, which potentiates sickling. Three cation cotransporter genes, SLC12A4 (KCC1), SLC12A6 (KCC3) and SLC12A7 (KCC4), and several splicing variants, mediate KCC activity in non-neuronal tissues. To determine which KCC isoform(s) predominates in human RBC we examined the quantitat

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7

Delpire, Eric, and Jiangtao Guo. "Cryo-EM structures of DrNKCC1 and hKCC1: a new milestone in the physiology of cation-chloride cotransporters." American Journal of Physiology-Cell Physiology 318, no. 2 (2020): C225—C237. http://dx.doi.org/10.1152/ajpcell.00465.2019.

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New milestones have been reached in the field of cation-Cl− cotransporters with the recently released cryo-electron microscopy (EM) structures of the Danio rerio (zebrafish) Na+-K+-2Cl− cotransporter ( DrNKCC1) and the human K+-Cl− cotransporter (hKCC1). In this review we provide a brief timeline that identifies the multiple breakthroughs in the field of solute carrier 12 transporters that led to the structure resolution of two of its key members. While cation-Cl− cotransporters share the overall architecture of carriers belonging to the amino acid-polyamine-organocation (APC) superfamily and

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8

Joiner, Clinton H., Richard Papes, Scott Crable, Dao Pan, and David B. Mount. "Functional Comparison of Red Cell KCl Cotransporter Isoforms, KCC1, KCC3, and KCC4." Blood 108, no. 11 (2006): 1245. http://dx.doi.org/10.1182/blood.v108.11.1245.1245.

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Abstract The KCl cotransporter mediates volume reduction in normal (AA) reticulocytes, and its abnormal regulation in sickle (SS) reticulocytes contributes to cellular dehydration that facilitates Hb S sickling. mRNA for three KCC genes - KCC1, KCC3, and KCC4 - as well as a splicing isoform, KCC1ex1b, is present in reticulocytes (Exp. Hem.2005; 33:624). Western blotting has demonstrated KCC1 in human RBC membranes (Su et al, AJPhysiol.1999;277:C899) and KCC3 in sheep (Lauf et al, CompBiochemPhysiol2001;130:499); KCC4 protein was found in hRBC membranes by proteomic analysis (Pasini et al, Bloo

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9

Risinger, Mary, Jesse Rinehart, Scott Crable, et al. "Structural and Functional Interactions of KCl Cotransport Proteins KCC1 and KCC3 in Sickle and Normal Erythrocyte Membranes." Blood 112, no. 11 (2008): 2474. http://dx.doi.org/10.1182/blood.v112.11.2474.2474.

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Abstract The KCl cotransporter (KCC) mediates volume reduction in normal reticulocytes and exaggerated KCC activity in sickle red blood cells (SS RBC) (Joiner et al, Blood109:1728, 2007) contributes to pathological dehydration that potentiates sickling. Three separate genes (KCC1, KCC3, KCC4) are expressed in RBC (Crable et al, Exp. Hem.33:624, 2005). KCC1 and KCC3 proteins have been shown to interact in ex vivo expression systems (Simard et al, JBC282(25):18083, 2007), and co-expression of an N-terminal truncation of KCC1 reduces KCC activity mediated by full-length KCC1 or KCC3 (Casula et al

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Mercado, Adriana, Paola de los Heros, Zesergio Melo, et al. "With no lysine L-WNK1 isoforms are negative regulators of the K+-Cl− cotransporters." American Journal of Physiology-Cell Physiology 311, no. 1 (2016): C54—C66. http://dx.doi.org/10.1152/ajpcell.00193.2015.

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The K+-Cl− cotransporters (KCC1-KCC4) encompass a branch of the SLC12 family of electroneutral cation-coupled chloride cotransporters that translocate ions out of the cell to regulate various factors, including cell volume and intracellular chloride concentration, among others. L-WNK1 is an ubiquitously expressed kinase that is activated in response to osmotic stress and intracellular chloride depletion, and it is implicated in two distinct hereditary syndromes: the renal disease pseudohypoaldosteronism type II (PHAII) and the neurological disease hereditary sensory neuropathy 2 (HSN2). The ef

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Dissertations / Theses on the topic "KC1 cotransporter"

1

Drew, Clare G. "Membrane transport in red blood cells." Thesis, University of Oxford, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.275332.

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Godart, Helene. "KCI cotransport regulation in mammalian erythrocyctes." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318547.

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Yih-FungChen and 陳宜芳. "The emerging role of KCl cotransport in tumor biology." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/34372627312940774359.

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博士<br>國立成功大學<br>基礎醫學研究所<br>98<br>The KCl cotransporter (KCC) is a major determinant of osmotic homeostasis and plays an important role in cancer development and progression. My thesis focuses on the emerging role for KCl cotransport in tumor biology and the novel mechanisms by which KCl cotransport regulates cancer malignant behaviors. My thesis includes four parts. (1) KCC4 expression is associated with cancer metastasis and clinical outcome. This part of study aims to investigate the contribution of individual KCC isoforms in cancer metastasis using cervical cancer and ovarian cancer as the

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Hsu, Yueh-Mei, and 徐月梅. "The important role of KCl cotransporters in the development and progression of human epithelial cancer." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/52135509117388502832.

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博士<br>國立成功大學<br>基礎醫學研究所<br>96<br>The KCl cotransporter family (KCC) is responsible for electroneutral K-Cl co-transportation and plays important roles in cell volume regulation, transepithelial transport, and in the regulation of intracellular chloride concentration ([Cl-]i). Of the four mammalian KCl cotransporters, KCC1, KCC3 and KCC4 are widely expressed, whereas KCC2 is neuron specific. Our previous studies have begun to emerge the important roles of KCl cotransporters in tumor development and progression. In this thesis, we first demonstrated that the growth and invasion of cervical cance

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Book chapters on the topic "KC1 cotransporter"

1

Ellory, J. Clive, Andrew C. Hall, Susan A. Ody, Carlos E. Poli de Figueiredos, Susan Chalder, and John Stuart. "KCl Cotransport in HbAA and HbSS Red Cells: Activation by Intracellular Acidity and Disappearance During Maturation." In Advances in Experimental Medicine and Biology. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5985-2_5.

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