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.
135
References
Inositol 1,3,4,5-tetrakisphosphate-induced Ca2+ sequestration into bovine adrenal-medullary secretory vesicles.
TL;DR: Ca2+ sequestration through receptor-operated Ca2+ channels or activation of the Ca(2+)-exchange mechanism by Ins(1,3,4,5)P4 was as effective at 4 degrees C as at 24 degrees C in sequestering Ca 2+ into secretory vesicles, implying Ca2+.
Cyclic GMP-dependent protein kinase phosphorylates phospholamban in isolated sarcoplasmic reticulum from cardiac and smooth muscle.
TL;DR: The phosphate incorporation into phospholamban and the stimulatory effects of both kinases on the Ca2+ pump are not additive, suggesting that G-kinases phosphorylates the same serine residue as A-kinase.
Complete primary structure of a human plasma membrane Ca2+ pump.
Anil K. Verma,Adelaida G. Filoteo,David R. Stanford,Eric D. Wieben,John T. Penniston,Emanuel E. Strehler,R. Fischer,R. Heim,G. Vogel,S Mathews +9 more
TL;DR: Comparison of the cloned sequence with peptide sequences from the erythrocyte Ca2+ pump showed that the two proteins have a very high proportion of identical residues but are not 100% identical, indicating that they represent different isozymes.
Exchange characteristics of the noradrenaline-sensitive calcium store in vascular smooth muscle cells or rabbit ear artery.
Rik Casteels,Guillaume Droogmans +1 more
TL;DR: The results suggest that the filling of the store under physiological conditions occurs by a direct pathway between the store and the extracellular medium.
The predicted secondary structures of the nucleotide‐binding sites of six cation‐transporting ATPases lead to a probable tertiary fold
W R Taylor,N M Green +1 more
TL;DR: Comparison of the most highly conserved segments with other nucleotide-binding domains showed that the sequences were consistent with a mononucleotide- binding fold and enabled a number of likely folding topologies to be limited to two or three alternatives.