Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Leonard Dode"'
Publikováno v:
Cell Calcium. 41:405-416
The secretory-pathway Ca2+-ATPases (SPCAs) represent a recently recognized family of phosphorylation-type ATPases that supply the lumen of the Golgi apparatus with Ca2+ and Mn2+ needed for the normal functioning of this structure. Mutations of the hu
Autor:
Virginie Monceau, Regis Bobe, Judith K. Gwathmey, Elisabeth Corvazier, Jocelyne Enouf, Aly Raies, Jens Peter Andersen, Johannes D. Clausen, Roger J. Hajjar, Raymonde Bredoux, Leonard Dode, Chiraz Chaabane, Saoussen Dally, Frederica Del Monte, Mohammed Fanchaouy, Pascal Gélébart
Publikováno v:
Aarhus University
We recently documented the expression of a novel human mRNA variant encoding a yet uncharacterized SERCA [SR (sarcoplasmic reticulum)/ER (endoplasmic reticulum) Ca2+-ATPase] protein, SERCA2c [Gélébart, Martin, Enouf and Papp (2003) Biochem. Biophys
Autor:
Jan B. Parys, Luc Raeymaekers, Ludwig Missiaen, Jo Vanoevelen, H De Smedt, Leonard Dode, Geert Callewaert, Frank Wuytack
Publikováno v:
Cell Calcium. 38:489-495
The Golgi apparatus is, like the endoplasmic reticulum, an inositol-1,4,5-trisphosphate-sensitive Ca2+ store, but its role in setting up Ca2+ signals is not well understood. We have now measured histamine-induced Ca2+ signals in HeLa cells pretreated
Publikováno v:
Cell Calcium. 38:291-302
Of the three mammalian members belonging to the sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) family, SERCA2 is evolutionary the oldest and shows the most wide tissue-expression pattern. Two major SERCA2 splice variants are well-characterized: the
Autor:
Jo Vanoevelen, Kurt Van Baelen, Leonard Dode, Ludwig Missiaen, Frank Wuytack, R.J. Fairclough, Luc Raeymaekers
Publikováno v:
Journal of Biological Chemistry. 280:22800-22808
Accumulation of Ca(2+) into the Golgi apparatus is mediated by sarco(endo)plasmic reticulum Ca(2+)-ATPases (SERCAs) and by secretory pathway Ca(2+)-ATPases (SPCAs). Mammals and birds express in addition to the housekeeping SPCA1 (human gene name ATP2
Autor:
Jo Vanoevelen, H De Smedt, Luc Raeymaekers, Jan B. Parys, Ludwig Missiaen, K. Van Baelen, Rosario Rizzuto, Leonard Dode, K. Van Acker, Frank Wuytack, Geert Callewaert
Publikováno v:
Cell Calcium. 36:479-487
Extracellular agonists mobilize Ca2+ from SERCA-comprising intracellular Ca2+ stores located in both the Golgi apparatus and the endoplasmic reticulum. Ca2+ release from both these compartments was studied in HeLa cells stably expressing the luminesc
Autor:
Ludwig Missiaen, Jan B. Parys, Humbert De Smedt, Frank Wuytack, Luc Raeymaekers, Kurt Van Baelen, Leonard Dode, Geert Callewaert, Jo Vanoevelen
Publikováno v:
Scopus-Elsevier
Recent evidence highlights the functional importance of the Golgi apparatus as an agonist-sensitive intracellular Ca(2+) store. Besides Ca(2+)-release channels and Ca(2+)-binding proteins, the Golgi complex contains Ca(2+)-uptake mechanisms consistin
Autor:
Jo Vanoevelen, Luc Raeymaekers, Jan B. Parys, Geert Callewaert, Siegfried Segaert, Frank Wuytack, Humbert De Smedt, Ludwig Missiaen, Leonard Dode, Kurt Van Baelen
Publikováno v:
Biochemical and Biophysical Research Communications. 322:1204-1213
Both the endoplasmic reticulum and the Golgi apparatus are agonist-sensitive intracellular Ca2+ stores. The Golgi apparatus has Ca2+-release channels and a Ca2+-uptake mechanism consisting of sarco(endo)plasmic-reticulum Ca2+-ATPases (SERCA) and secr
Autor:
Regis Bobe, Raymonde Bredoux, Jocelyne Enouf, Jens Peter Andersen, Tünde Kovács, Johannes D. Clausen, Leonard Dode, Elisabeth Corvazier
Publikováno v:
Journal of Biological Chemistry. 279:24297-24306
Understanding of Ca(2+) signaling requires the knowledge of proteins involved in this process. Among these proteins are sarco/endoplasmic reticulum Ca(2+)-ATPases (SERCAs) that pump Ca(2+) into the endoplasmic reticulum (ER). Recently, the human SERC
Autor:
Jittima Dhitavat, Bente Vilsen, Alain Hovnanian, Jens Peter Andersen, Natalie Leslie, Leonard Dode
Publikováno v:
Journal of Biological Chemistry. 278:47877-47889
Steady-state and rapid kinetic studies were conducted to functionally characterize the overall and partial reactions of the Ca2+ transport cycle mediated by the human sarco(endo)plasmic reticulum Ca2+-ATPase 2 (SERCA2) isoforms, SERCA2a and SERCA2b,