Calreticulin expression in plant cells: developmental regulation, tissue specificity and intracellular distribution

Borisjuk, Nikolai; Sitailo, Leonid A.; Adler, Klaus; Malysheva, L.; Tewes, Annegret; Borisjuk, Ludmilla; Manteuffel, Renate

doi:10.1007/s004250050427

Cited by 106 publications

(77 citation statements)

References 34 publications

(74 reference statements)

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“…5, B with E). Earlier reports have shown that CRT, although present in various tissues in curled-leaf tobacco (Nicotiana plumbaginifolia; Borisjuk et al, 1998), Arabidopsis (Nelson et al, 1997), tobacco (Nicotiana tabacum; Denecke et al, 1995), and barley (Chen et al, 1994), was most abundant in floral tissues. Although none of the latter investigations have performed expression studies for the full set of CRT isoforms, the overall expression patterns reported here are consistent with these reports.…”

Section: Discussionmentioning

confidence: 96%

“…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;Denecke et al, 1995;Nelson et al, 1997). In addition, CRT preferentially localizes to plasmodesmata in maize (Zea mays) root tips and is suggested to be involved in regulation of the closure of plasmodesmata (Baluska et al, 1999).…”

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confidence: 99%

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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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Section: Discussionmentioning

confidence: 96%

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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“…At the whole organism and organ level, there are examples of relatively high expression of calreticulin during development in several species, including plants (47), zebrafish (48), frog (49), and mouse (36,50). However, at the cellular level, the two model systems reported to date exhibited divergent patterns.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Calreticulin Expression during Induction of Differentiation in Human Myeloid Cells

Clark¹,

Li²,

Pearson³

et al. 2002

Journal of Biological Chemistry

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Induction of differentiation of HL-60 human myeloid cells profoundly affected expression of calreticulin, a Ca2؉ -binding endoplasmic reticulum chaperone. Induction with Me 2 SO or retinoic acid reduced levels of calreticulin protein by ϳ60% within 4 days. Pulse-chase studies indicated that labeled calreticulin decayed at similar rates in differentiated and undifferentiated cells (t1 ⁄2 ϳ4.6 days), but the biosynthetic rate was <10% of control after 4 days. Differentiation also induced a rapid decline in calreticulin mRNA levels (90% reduction after 1 day) without a decrease in transcript stability (t1 ⁄2 ϳ5 h). Nuclear run-on analysis demonstrated rapid downregulation of gene transcription (21% of control at 2 h). Differentiation also greatly reduced the Ca 2؉ content of the cells (25% of control), although residual Ca 2؉ pools remained sensitive to thapsigargin, ionomycin, and inositol trisphosphate. Progressive decreases were also observed in levels of calnexin and ERp57, whereas BiP/ GRP78 and protein disulfide isomerase were only modestly affected. Ultrastructural studies showed a substantial reduction in endoplasmic reticulum content of the cells. Thus, terminal differentiation of myeloid cells was associated with decreased endoplasmic reticulum content, selective reductions in molecular chaperones, and diminished intracellular Ca 2؉ stores, perhaps reflecting an endoplasmic reticulum remodeling program as a prominent feature of granulocytic differentiation.Calreticulin is a major Ca 2ϩ -binding protein present in the lumen of the endoplasmic reticulum (ER) 1 of virtually all cell types (1-3). The cDNA sequence predicts an ϳ47-kDa acidic protein with a zonal structure featuring a globular N-terminal domain, a proline-rich P domain, and a highly acidic C domain terminating in a KDEL motif, the ER retention signal (3, 4).Biophysical studies show calreticulin to be a highly asymmetric molecule consistent with this predicted three domain structure. Calreticulin binds Ca 2ϩ with both high and low affinities and with high capacity. A single high affinity site (K d ϳ1 M) is located within the P domain of the molecule and multiple low affinity sites (K d ϳ2 mM, 20 -25 mol of Ca 2ϩ /mol of protein) are present in the highly acidic C domain (3,4). The N domain contains at least one site for binding Zn 2ϩ , which appears to involve 4 of the histidine residues in this region (5, 6). Binding of these ions affects the conformation and stability of the protein (7).Numerous and apparently unrelated functions have been ascribed to calreticulin since it was first identified, but its roles in the regulation of Ca 2ϩ homeostasis and as a molecular chaperone of nascent glycoproteins are the two functions that have been most extensively characterized. Calreticulin appears to regulate intracellular Ca 2ϩ homeostasis through more than one mechanism. The high Ca 2ϩ -binding capacity of calreticulin suggests that it acts as a Ca 2ϩ store or buffer within the ER, and there is evidence that in at least some cell types it is a main so...

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“…It has been reported to be present in other cellular compartments like Golgi complex, nucleus, nuclear membrane, cytoplasm, vesicles and spindle apparatus of the dividing cells, plasma membrane and plasmodesmata (Bush 1995;Denecke et al 1995;Nelson et al 1997). It was reported to be present abundantly in most of the plant parts such as roots, young leaves and different flowering organs and also in germinating seeds (Borisjuk et al 1998). (Opas et al 1996;Michalak et al 1999).…”

Section: Mass Spectrometric (Ms) Identification Of N-glycoproteins Rementioning

confidence: 99%

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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Calreticulin expression in plant cells: developmental regulation, tissue specificity and intracellular distribution

Cited by 106 publications

References 34 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

Regulation of Calreticulin Expression during Induction of Differentiation in Human Myeloid Cells

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

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