Calcium, a signaling molecule in the endoplasmic reticulum?

Corbett, Elaine F.; Michalak, Marek

doi:10.1016/s0968-0004(00)01588-7

Cited by 245 publications

(156 citation statements)

References 29 publications

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“…heavy-chain-binding protein), was recognized to be sensitive to ambient Ca 2+ [9]. However, it remains still unclear whether and, if so, how eminent Ca 2+ fluctuations faced by the ER under physiological conditions due to regular cell stimulation [2,3,15] influence ER chaperone activity [8].…”

Section: Discussionmentioning

confidence: 99%

“…A decrease in ambient [Ca 2+ ] renders the calreticulin cycle and associated folding catalysts, i.e. protein disulphide-isomerase and ERp57, inactive [9]. However, these principles of Ca 2+ -dependent protein folding have been assessed mainly on recombinant proteins [7,8,10] or by artificially applying excessive ER stress [11][12][13], while a detailed analysis of its kinetics and correlation with physiological Ca 2+ fluctuations are lacking.…”

Section: Introductionmentioning

confidence: 99%

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Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum

Osibow

Frank

Malli

et al. 2006

Biochemical Journal

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Considering the physiological Ca 2+ dynamics within the ER (endoplasmic reticulum), it remains unclear how efficient protein folding is maintained in living cells. Thus, utilizing the strictly folding-dependent activity and secretion of LPL (lipoprotein lipase), we evaluated the impact of ER Ca 2+ content and mitochondrial contribution to Ca 2+ -dependent protein folding. Exhaustive ER Ca 2+ depletion by inhibition of sarcoplasmic/ endoplasmic reticulum Ca 2+ -ATPases caused strong, but reversible, reduction of cell-associated and released activity of constitutive and adenovirus-encoded human LPL in CHO-K1 (Chinesehamster ovary K1) and endothelial cells respectively, which was not due to decline of mRNA or intracellular protein levels. In contrast, stimulation with the IP 3 (inositol 1,4,5-trisphosphate)-generating agonist histamine only moderately and transiently affected LPL maturation in endothelial cells that paralleled a basically preserved ER Ca 2+ content. However, in the absence of extracellular Ca 2+ or upon prevention of transmitochondrial Ca 2+ flux, LPL maturation discontinued upon histamine stimulation. Collectively, these data indicate that Ca 2+ -dependent protein folding in the ER is predominantly controlled by intraluminal Ca 2+ and is largely maintained during physiological cell stimulation owing to efficient ER Ca 2+ refilling. Since Ca 2+ entry and mitochondrial Ca 2+ homoeostasis are crucial for continuous Ca 2+ -dependent protein maturation in the ER, their pathological alterations may result in dysfunctional protein folding.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum

Osibow

Frank

Malli

et al. 2006

Biochemical Journal

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“…CRT has been suggested to be associated with agonist-triggered Ca 2ϩ channels and might be important for regulating ERderived Ca 2ϩ signals (Michalak et al, 1998;Corbett and Michalak, 2000). Alterations in CRT levels thus might affect both the Ca 2ϩ -holding capacity in the ER and be involved in the regulation of Ca 2ϩ release.…”

Section: Discussionmentioning

confidence: 99%

“…It has a globular N domain and two Ca 2ϩ -binding regions; a high-affinity, low-capacity P domain, and a lowaffinity and high-capacity Ca 2ϩ -binding C domain. The C domain of the mammalian CRT can sequester at least 25 mol Ca 2ϩ per mole protein (for review, see Krause and Michalak, 1997;Michalak et al, 1999;Corbett and Michalak, 2000). Because of its high Ca 2ϩ -binding capacity, CRT has been suggested to be involved in Ca 2ϩ signaling (Camacho and Lechleiter, 1995;Mery et al, 1996;John et al, 1998).…”

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confidence: 99%

The Ca2+ Status of the Endoplasmic Reticulum Is Altered by Induction of Calreticulin Expression in Transgenic Plants

et al. 2001

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To investigate the endoplasmic reticulum (ER) Ca 2ϩ stores in plant cells, we generated tobacco (Nicotiana tabacum; NT1) suspension cells and Arabidopsis plants with altered levels of calreticulin (CRT), an ER-localized Ca 2ϩ -binding protein. NT1 cells and Arabidopsis plants were transformed with a maize (Zea mays) CRT gene in both sense and antisense orientations under the control of an Arabidopsis heat shock promoter. ER-enriched membrane fractions from NT1 cells were used to examine how altered expression of CRT affects Ca 2ϩ uptake and release. We found that a 2.5-fold increase in CRT led to a 2-fold increase in ATP-dependent 45 Ca 2ϩ accumulation in the ER-enriched fraction compared with heat-shocked wild-type controls. Furthermore, after treatment with the Ca 2ϩ ionophore ionomycin, ER microsomes from NT1 cells overproducing CRT showed a 2-fold increase in the amount of 45 Ca 2ϩ released, and a 2-to 3-fold increase in the amount of 45 Ca 2ϩ retained compared with wild type. These data indicate that altering the production of CRT affects the ER Ca 2ϩ pool. In addition, CRT transgenic Arabidopsis plants were used to determine if altered CRT levels had any physiological effects. We found that the level of CRT in heat shock-induced CRT transgenic plants correlated positively with the retention of chlorophyll when the plants were transferred from Ca 2ϩ -containing medium to Ca 2ϩ -depleted medium. Together these data are consistent with the hypothesis that increasing CRT in the ER increases the ER Ca 2ϩ stores and thereby enhances the survival of plants grown in low Ca 2ϩ medium.

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“…The increase of the cytosolic free Ca 2ϩ concentration in response to a stimulus results from the opening of Ca 2ϩ channels present in the plasma membrane and in the membranes of intracellular Ca 2ϩ stores, mainly the endoplasmic reticulum (ER). 1 It has more recently also become clear that the Ca 2ϩ stored in the lumen of many intracellular compartments not only serves as a reservoir of releasable Ca 2ϩ , but also plays a regulatory role in several important cell biological functions. Luminal Ca 2ϩ in the ER as well as in the Golgi or other components of the secretory pathway is required for the proper translation, translocation, folding, and processing of secreted proteins (for review, see Ref.…”

mentioning

confidence: 99%

The Golgi PMR1 P-type ATPase of Caenorhabditis elegans

Baelen

Vanoevelen

Missiaen

et al. 2001

Journal of Biological Chemistry

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In recent years, it has been well established that the Ca 2؉ concentration in the lumen of intracellular organelles is a key determinant of cell function. Despite the fact that essential functions of the Golgi apparatus depend on the Ca 2؉ and Mn 2؉ concentration in its lumen, little is known on the transport system responsible for ion accumulation. The Golgi ion pump PMR1 has been functionally studied only in yeast. In humans, mutations in the orthologous gene ATP2C1 cause HaileyHailey disease. We report here the identification of the PMR1 homologue in the model organism Caenorhabditis elegans and after ectopic expression the direct study of its ion transport in permeabilized COS-1 cells. The C. elegans genome is predicted to contain a single PMR1 orthologue on chromosome I. We found evidence for alternative splicing in the 5-untranslated region, but no indication for the generation of different protein isoforms. C. elegans PMR1 overexpressed in COS-1 cells transports Ca 2؉ and Mn 2؉ with high affinity into the Golgi apparatus in a thapsigargin-insensitive manner. Part of the accumulated Ca 2؉ can be released by inositol 1,4,5-trisphosphate, in agreement with the idea that the Golgi apparatus is an inositol 1,4,5-trisphosphate-sensitive Ca 2؉ store.

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Calcium, a signaling molecule in the endoplasmic reticulum?

Cited by 245 publications

References 29 publications

Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum

Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum

The Ca2+ Status of the Endoplasmic Reticulum Is Altered by Induction of Calreticulin Expression in Transgenic Plants

The Golgi PMR1 P-type ATPase of Caenorhabditis elegans

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