Evidence that Spinach Leaves Express Calreticulin but Not Calsequestrin

Navazio, Lorella; Baldan, Barbara; Dainese, Paola; James, Peter; Damiani, Ernesto; Margreth, Alfredo; Mariani, Paola

doi:10.1104/pp.109.3.983

Cited by 33 publications

(36 citation statements)

References 41 publications

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“…Plant CRTs have been shown to bind calcium with similar characteristics as their mammalian homologs (Chen et al, 1994;Hassan et al, 1995;Navazio et al, 1995;Coughlan et al, 1997;Li and Komatsu, 2000) and recently also to have calcium-storing functions in the ER of plant cells (Persson et al, 2001;Wyatt et al, 2002). In contrast to most animal CRTs, glycosylation of CRTs is generally observed in plants (Navazio et al, 1995(Navazio et al, , 2002Pagny et al, 2000). Plant CRTs are up-regulated in response to a variety of stress-mediated stimuli, e.g.…”

mentioning

confidence: 99%

Phylogenetic Analyses and Expression Studies Reveal Two Distinct Groups of Calreticulin Isoforms in Higher Plants

et al. 2003

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Calreticulin (CRT) is a multifunctional protein mainly localized to the endoplasmic reticulum in eukaryotic cells. Here, we present the first analysis, to our knowledge, of evolutionary diversity and expression profiling among different plant CRT isoforms. Phylogenetic studies and expression analysis show that higher plants contain two distinct groups of CRTs: a CRT1/CRT2 group and a CRT3 group. To corroborate the existence of these isoform groups, we cloned a putative CRT3 ortholog from Brassica rapa. The CRT3 gene appears to be most closely related to the ancestral CRT gene in higher plants. Distinct tissue-dependent expression patterns and stress-related regulation were observed for the isoform groups. Furthermore, analysis of posttranslational modifications revealed differences in the glycosylation status among members within the CRT1/CRT2 isoform group. Based on evolutionary relationship, a new nomenclature for plant CRTs is suggested. The presence of two distinct CRT isoform groups, with distinct expression patterns and posttranslational modifications, supports functional specificity among plant CRTs and could account for the multiple functional roles assigned to CRTs.Calreticulin (CRT) is a highly conserved protein mainly localized to the endoplasmic reticulum (ER) in plants and to the ER/sarcoplasmic reticulum in mammals (for review, see Crofts and Denecke, 1998;Michalak et al., 1999;Hadlington and Denecke, 2000;Johnson et al., 2001). CRT is a multifunctional protein, suggested to be involved in over 40 intra-and extracellular processes in mammalian cells. However, the main focus has been on its role in calcium signaling (Camacho and Lechleiter, 1995;Nakamura et al., 2001;Arnaudeau et al., 2002) and as a chaperone (Hebert et al., 1996;Saito et al., 1999;Nakamura et al., 2001). CRT comprises three major subdomains: a highly conserved N domain, a high-affinity but low-capacity Ca 2ϩ -binding P domain, and a lowaffinity but high-capacity Ca 2ϩ -binding C domain ending with an ER retention signal (Michalak et al., 1999).Although the role of CRTs as chaperone-like proteins and in calcium signaling is well established in mammals, the functions of CRT have been elusive in plants until recently. Plant CRTs have been shown to bind calcium with similar characteristics as their mammalian homologs (Chen et al., 1994;Hassan et al., 1995;Navazio et al., 1995;Coughlan et al., 1997;Li and Komatsu, 2000) and recently also to have calcium-storing functions in the ER of plant cells (Persson et al., 2001;Wyatt et al., 2002). In contrast to most animal CRTs, glycosylation of CRTs is generally observed in plants (Navazio et al., 1995(Navazio et al., , 2002Pagny et al., 2000). Plant CRTs are up-regulated in response to a variety of stress-mediated stimuli, e.g. pathogenrelated signaling molecules (Denecke et al., 1995;Jaubert et al., 2002) and gravistimulation (Heilmann et al., 2001), and are highly expressed during mitosis (Denecke et al., 1995), embryogenesis (Borisjuk et al., 1998), and in floral tissues (Chen et al., 1994;...

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mentioning

confidence: 99%

Phylogenetic Analyses and Expression Studies Reveal Two Distinct Groups of Calreticulin Isoforms in Higher Plants

et al. 2003

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“…The 54 kDa isoform was thought to be unglycosylated form of 56 kDa, due to similarity in pI and antigenicity. The isoforms showed difference in the N-terminal sequence and in Cleveland peptide maps after partial digestion with Staphylococcuc aureus (Navazio et al 1995). N-glycosylation of 54 kDa isoform has not been reported earlier, however in this study both the isoforms were enriched by con A chromatography and also showed positive signals on con A affinoblot.…”

Section: Protein Involved In Abiotic and Biotic Stress Tolerancementioning

confidence: 46%

“…binding proteins (Campbell et al 1983). Two polypeptides at 56 and 54 kDa showed blue stain with stains all similar to 56 and 54 kDa calreticulin isoforms in spinach leaves (Navazio et al 1995). The molecular weight of the polypeptides were similar to the spot (spot 11) from which calreticulin was identified on 2-D gel (Fig.…”

Section: Protein Involved In Abiotic and Biotic Stress Tolerancementioning

confidence: 69%

Hippophae rhamnoides N-glycoproteome analysis: a small step towards sea buckthorn proteome mining

Sougrakpam

Deswal

2016

Physiol Mol Biol Plants

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Hippophae rhamnoides is a hardy shrub capable of growing under extreme environmental conditions namely, high salt, drought and cold. Its ability to grow under extreme conditions and its wide application in pharmaceutical and nutraceutical industry calls for its indepth analysis. N-glycoproteome mining by con A affinity chromatography from seedling was attempted. The glycoproteome was resolved on first and second dimension gel electrophoresis. A total of 48 spots were detected and 10 non-redundant proteins were identified by MALDI-TOF/ TOF. Arabidopsis thaliana protein disulfide isomerase-like 1-4 (ATPDIL1-4) electron transporter, protein disulphide isomerase, calreticulin 1 (CRT1), glycosyl hydrolase family 38 (GH 38) protein, phantastica, maturase k, Arabidopsis trithorax related protein 6 (ATXR 6), cysteine protease inhibitor were identified out of which ATXR 6, phantastica and putative ATPDIL1-4 electron transporter are novel glycoproteins. Calcium binding protein CRT1 was validated for its calcium binding by stains all staining. GO analysis showed involvement of GH 38 and ATXR 6 in glycan and lysine degradation pathways. This is to our knowledge the first report of glycoproteome analysis for any Elaeagnaceae member.

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“…Antibodies against the intraluminal ER Ca 2ϩ -binding proteins calreticulin (Navazio et al, 1995) and BiP (Denecke et al, 1991) were also used, but both of these reticuloplasmins were found to be spread throughout the gradient (data not shown). This wide distribution is likely to be due to the release of soluble proteins from the ER lumen during homogenization.…”

Section: Distribution Of Er and Vacuolar Membrane Markers After Contimentioning

confidence: 99%

“…Nevertheless, in the last few years, the biochemical characterization and molecular cloning from plants of the ER luminal Ca 2ϩ buffering protein calreticulin (Chen et al, 1994;Navazio et al, 1995) and of P-type Ca 2ϩ -ATPase pumps located at ER membranes (Thomson et al, 1993;Liang et al, 1997;Harper et al, 1998;Hong et al, 1999), have confirmed the potential importance of the ER in cellular Ca 2ϩ relations. The discovery of a voltage-gated Ca 2ϩ channel that mediates Ca 2ϩ release from the ER of tendrils of Bryonia dioica (Klü sener et al, 1995) has served to reinforce the possibility of a role for the ER in higher plant Ca 2ϩ signaling.…”

mentioning

confidence: 99%

Mobilization of Ca2+ by Cyclic ADP-Ribose from the Endoplasmic Reticulum of Cauliflower Florets

2001

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The NAD ϩ metabolite cADP-Rib (cADPR) elevates cytosolic free Ca 2ϩ in plants and thereby plays a central role in signal transduction pathways evoked by the drought and stress hormone abscisic acid. cADPR is known to mobilize Ca 2ϩ from the large vacuole of mature cells. To determine whether additional sites for cADPR-gated Ca 2ϩ release reside in plant cells, microsomes from cauliflower (Brassica oleracea) inflorescences were subfractionated on sucrose density gradients, and the distribution of cADPR-elicited Ca 2ϩ release was monitored. cADPR-gated Ca 2ϩ release was detected in the heavy-density fractions associated with rough endoplasmic reticulum (ER). cADPR-dependent Ca 2ϩ 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 Ca 2ϩ

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Evidence that Spinach Leaves Express Calreticulin but Not Calsequestrin

Cited by 33 publications

References 41 publications

Phylogenetic Analyses and Expression Studies Reveal Two Distinct Groups of Calreticulin Isoforms in Higher Plants

Phylogenetic Analyses and Expression Studies Reveal Two Distinct Groups of Calreticulin Isoforms in Higher Plants

Hippophae rhamnoides N-glycoproteome analysis: a small step towards sea buckthorn proteome mining

Mobilization of Ca2+ by Cyclic ADP-Ribose from the Endoplasmic Reticulum of Cauliflower Florets

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