Journal Article10.1016/0163-7258(91)90014-D
Ca2+ extrusion across plasma membrane and Ca2+ uptake by intracellular stores.
Ludwig Missiaen,Frank Wuytack,Luc Raeymaekers,Humbert De Smed,Guy Droogmans,I Declerck,Rik Casteels +6 more
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TL;DR: The aim of this review is to summarize the various systems that remove Ca2+ from the cytoplasm by summarizing the functional regulation of these systems and the recent progress obtained with molecular-biology techniques, which pointed to the existence of different isoforms of the Ca 2+ pump.
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About: This article is published in Pharmacology & Therapeutics. The article was published on 01 Jan 1991.
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Citations
Mutations in ATP2A2, encoding a Ca2+ pump, cause Darier disease
Anavaj Sakuntabhai,Victor L. Ruiz-Perez,S. Carter,N. Jacobsen,Susan Burge,Sarah Monk,Martin D. Smith,Colin S. Munro,Michael Conlon O'Donovan,Nicholas John Craddock,Raju Kucherlapati,Jonathan L. Rees,Michael John Owen,G M Lathrop,Anthony P. Monaco,Tom Strachan,Alain Hovnanian +16 more
TL;DR: It is demonstrated that mutations in ATP2A2 cause Darier disease and disclose a role for this pump in a Ca2+-signalling pathway regulating cell-to-cell adhesion and differentiation of the epidermis.
741
Gentamicin and bone morphogenic protein-2 (BMP-2)-delivering heparinized-titanium implant with enhanced antibacterial activity and osteointegration.
TL;DR: Dual drug (antibiotics and osteoinductive protein)-eluting Ti substrates such as GS/BMP-2/Hep-Ti are a promising material for the enhanced osteointegration and implant longevity in orthopedics and dentistry.
168
Structure and function of inositol triphosphate receptors
Colin W. Taylor,Alan Richardson +1 more
TL;DR: The ligand recognition characteristics of Ins(1,4,5) P 3 receptors and their functional properties in their native environment and after purification are discussed, and these properties are related to what is known of the structure of the receptor.
155
Cellular Uptake of Lead Is Activated by Depletion of Intracellular Calcium Stores
TL;DR: In conclusion, Pb2+ crosses the plasma membrane of GH3, C6, and HEK293 cells via channels that are activated by profound depletion of intracellular Ca2+ stores.
139
The plasma membrane calcium pump--a physiological perspective on its regulation.
TL;DR: This review focuses on the physiological role of the plasma membrane Ca(2+)+ Mg(2+)-dependent adenosine triphosphatase (PM Ca( 2+)-ATPase) in cellular signalling and recent work investigating the possible regulation of the PM Ca2+ pump by G proteins and agonists.
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References
Liposomes as carriers of poorly water-soluble substrates: linear modelling of membrane systems with catalytic or binding sites of different facedness. Significance of experimental membrane partition coefficients and of kinetic and equilibrium parameters.
TL;DR: A multiphasic modelling approach to systems containing membrane-bound receptors or catalytic sites and a liposomal preparation as a substrate carrier is described and the significance of experimental membrane partition coefficients is discussed.
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The influence of external cations and membrane potential on Ca-activated Na efflux in Myxicola giant axons.
R A Sjodin,R F Abercrombie +1 more
TL;DR: The results suggest that the Cao- activated Na efflux in Myxicola giant axons requires the presence of an external monovalent cation and that the order of effectiveness at a total monovalENT cation concentration of 430 mM is K + Li greater thanLi greater than Choline greater than Na.
Definition of surface-exposed epitopes on the (Ca2+-Mg2+)-ATPase of sarcoplasmic reticulum
TL;DR: Three surface-exposed epitopes have been defined in the nucleotide-binding domain of the ATPase, suggesting considerable surface exposure of this region.
Role of 3′,5′-cyclic amp in glucagon-induced stimulation of ruthenium red-insensitive calcium transport in an endoplasmic reticulum-rich fraction of rat liver
TL;DR: This study shows that Ca2*-transport activity in the subcellular fraction described was enhanced by dibutyryl 3’,5’-cyclic adenosine monophosphate (CAMP), and raised the possibility that Ca’+transport by the endoplasmic-rich intermediate fraction of rat liver may be controlled by a pbosphorylation-depb phosphorylation cycle similar to that which regulates Ca2- transport by
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