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Titolo:
Mobilization of Ca2+ by cyclic ADP-ribose from the endoplasmic reticulum of cauliflower florets
Autore:
Navazio, L; Mariani, P; Sanders, D;
Indirizzi:
Univ York, Dept Biol, Plant Lab, York YO10 5YW, N Yorkshire, England Univ York York N Yorkshire England YO10 5YW O10 5YW, N Yorkshire, England Univ Padua, Dipartimento Biol, I-35131 Padua, Italy Univ Padua Padua Italy I-35131 , Dipartimento Biol, I-35131 Padua, Italy
Titolo Testata:
PLANT PHYSIOLOGY
fascicolo: 4, volume: 125, anno: 2001,
pagine: 2129 - 2138
SICI:
0032-0889(200104)125:4<2129:MOCBCA>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALMODULIN-REGULATED CA2+-ATPASE; CALCIUM-RELEASE CHANNELS; PLASMA-MEMBRANE VESICLES; VACUOLAR ION CHANNELS; ZEA-MAYS-L; HIGHER-PLANTS; INOSITOL 1,4,5-TRISPHOSPHATE; ARABIDOPSIS-THALIANA; STOMATAL CLOSURE; EUGLENA-GRACILIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Sanders, D Univ York, Dept Biol, Plant Lab, POB 373, York YO10 5YW, N Yorkshire, England Univ York POB 373 York N Yorkshire England YO10 5YW re, England
Citazione:
L. Navazio et al., "Mobilization of Ca2+ by cyclic ADP-ribose from the endoplasmic reticulum of cauliflower florets", PLANT PHYSL, 125(4), 2001, pp. 2129-2138

Abstract

The NAD(+) metabolite cADP-Rib (cADPR) elevates cytosolic free Ca2+ in plants and thereby plays a central role in signal transduction pathways evokedby the drought and stress hormone abscisic acid. cADPR is known to mobilize Ca2+ from the large vacuole of mature cells. To determine whether additional sites for cADPR-gated Ca2+ release reside in plant cells, microsomes from cauliflower (Brassica oleracea) inflorescences were subfractionated on sucrose density gradients, and the distribution of cADPR-elicited Ca2+ release was monitored. cADPR-gated Ca2+ release was detected in the heavy-density fractions associated with rough endoplasmic reticulum (ER). cADPR-dependent Ca2+ release co-migrated with two ER markers, calnexin and antimycin A-insensitive NADH-cytochrome c reductase activity. To investigate the possibility that contaminating plasma membrane in the ER-rich fractions was responsible for the observed release, plasma membrane vesicles were purified by aqueous two-phase partitioning, everted with Brij-58, and loaded with Ca2+. These vesicles failed to respond to cADPR. Ca2+ release evoked by cADPR at the ER was fully inhibited by ruthenium red and 8-NH2-cADPR, a specific antagonist of cADPR-gated Ca2+ release in animal cells. The presence of a Ca2release pathway activated by cADPR at higher plant ER reinforces the notion that, alongside the vacuole, the ER participates in Ca2+ signaling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 12:36:59