Basal Transcription of the Mouse Sarco(endo)plasmic Reticulum Ca2+-ATPase Type 3 Gene in Endothelial Cells Is Controlled by Ets-1 and Sp1

Hadri, Lahouaria; Ozog, Anne; Soncin, Fabrice; Lompré, Anne‐Marie

doi:10.1074/jbc.m204731200

Cited by 23 publications

(24 citation statements)

References 52 publications

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“…38 -49 The TATA-less human and mouse SERCA3 promoters contain several Sp1-binding sequences, which have been shown, along with ETS-binding sites, to direct basal SERCA3 expression in mouse vascular endothelial cells. 22,50 The inhibition by mithramycin-A of the constitutive residual expression of SERCA3 in COLO-205 cells, which is quantitatively similar to that observed in well-differentiated colon carcinoma tissue, suggests that Sp1-like factor-dependent transcription drives SERCA3 expression observed also in well differentiated tumors. Importantly, short chain fatty acid (ie, butyrate or valerate)-induced expression of SERCA3 in cells that initially express undetectable amounts of SERCA3 protein was also inhibited in a dose-dependent manner by mithramycin-A.…”

Section: Discussionmentioning

confidence: 53%

“…[25][26][27] Because Sp1-like factors are involved in the expression of SERCA3 in normal vascular endothelial cells, 22 the effect of mithramycin-A on short chain fattyacid-induced SERCA3 expression in colon and gastric cancer cell lines was studied by Western blotting. As shown in Figure 3A, the induction of SERCA3 expression in the DLD-1 colon cancer cell line by sodium valerate could be inhibited by mithramycin-A in a dose-dependent manner in the submicromolar concentration range.…”

Section: Inhibition Of Serca3 Expression By Mithramycin-amentioning

confidence: 99%

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The Loss of Sarco/Endoplasmic Reticulum Calcium Transport ATPase 3 Expression Is an Early Event during the Multistep Process of Colon Carcinogenesis

Brouland¹,

Gélébart²,

Kovàcs³

et al. 2005

The American Journal of Pathology

116

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Calcium accumulation in the endoplasmic reticulum is accomplished by sarco/endoplasmic reticulum calcium transport ATPases (SERCA enzymes). To better characterize the role of SERCA3 in colon carcinogenesis, its expression has been investigated in colonic epithelium, benign lesions, adenomas, and adenocarcinomas. In addition, the regulation of SERCA3 expression was analyzed in the context of the adenomatous polyposis coli/␤-catenin/T-cell factor 4 (TCF4) pathway and of specificity protein 1 (Sp1)-like factordependent transcription. We report that SERCA3 expression increased along the crypts as cells differentiated in normal colonic mucosa and in hyperplastic polyps, was moderately and heterogeneously expressed in colonic adenomas with expression levels inversely correlated with the degree of dysplasia, was barely detectable in well and moderately differentiated adenocarcinomas, and was absent in poorly differentiated tumors. Inhibition of Sp1-like factor-dependent transcription blocked SERCA3 expression during cell differentiation, and Calcium homeostasis of the endoplasmic reticulum (ER) is involved in several essential cell functions. Calcium stored in the ER is required for chaperone-assisted maturation of newly synthesized proteins transiting through the organelle. 1-3 Moreover, second messenger-induced calcium release from the ER through inositol-tris-phosphate-and ryanodine receptor-type calcium channels constitutes an integral part of many intracellular signal transduction pathways and networks. 4,5 Because ER calcium homeostasis is therefore involved in many constitutive or inducible cell functions, calcium accumulation into this organelle, assured by sarco/endoplasmic reticulum calcium transport ATPase (SERCA)-type calcium pumps is essential for numerous cellular activities such as secretion, neuronal plasticity, stress responses, proliferation, differentiation, or various forms of cell death. 6 -12 Three SERCA genes are known that code by alternative splicing several isoforms, the expression of which is tissue dependent and developmentally regulated. 13

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Section: Discussionmentioning

confidence: 53%

Section: Inhibition Of Serca3 Expression By Mithramycin-amentioning

confidence: 99%

The Loss of Sarco/Endoplasmic Reticulum Calcium Transport ATPase 3 Expression Is an Early Event during the Multistep Process of Colon Carcinogenesis

Brouland¹,

Gélébart²,

Kovàcs³

et al. 2005

The American Journal of Pathology

116

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“…However, the SERCA3f protein should be of importance based on the study of h3f mRNA distribution, which demonstrates its expression in almost all human cell and tissue types. Hence, in contrast with previous suggestions, it is more and more evident that human SERCA3 gene products are not only expressed in a restricted number of adult tissues (33)(34)(35)(36)(37).…”

Section: Discussioncontrasting

confidence: 45%

Identification, Expression, Function, and Localization of a Novel (Sixth) Isoform of the Human Sarco/Endoplasmic Reticulum Ca2+ATPase 3 Gene

Bobe

Bredoux

Corvazier

et al. 2004

Journal of Biological Chemistry

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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 SERCA3 gene was shown to give rise to five isoforms (SERCA3a-e (h3a-h3e)). Here we demonstrate the existence of an additional new member, termed SERCA3f (h3f). By reverse transcriptase-PCR using monocytic U937 cell RNA, h3f mRNA was found to exclude the antepenultimate exon 21. h3f mRNA expression appeared as a human-specific splice variant. It was not found in rats or mice. h3f mRNA gave rise to an h3f protein differing in its C terminus from h3a-h3e. Of particular interest, h3f diverged in the first amino acids after the first splice site but presented the same last 21 amino acids as h3b. Consequently, we further investigated the structure-function-location relationships of the h3b and h3f isoforms. and (ii) the low apparent Ca 2؉ affinity and the enhanced rate of dephosphorylation of the E 2 P phosphoenzyme intermediate. Subcellular location of h3b and h3f by immunofluorescence and/or confocal microscopy using the h3b-and h3f-specific polyclonal and the pan-h3 monoclonal (PL/ IM430) antibodies suggested overlapping but distinct ER location. The endogenous expression of h3f protein was also proved in U937 cells. Altogether these data suggest that the SERCA3 isoforms have a more widespread role in cellular Ca 2؉ signaling than previously appreciated.Cell Ca 2ϩ signaling is a dynamic oscillatory process regulating a variety of important cellular functions such as secretion, contraction, metabolism, neuronal plasticity, and gene transcription (1). Accordingly, Ca 2ϩ signaling is strictly controlled in space, time, and amplitude. This very tight control is necessary to enable cells to extract relevant information from the Ca 2ϩ signal but also implies that disturbances in the intracellular Ca 2ϩ signaling can lead to a plethora of consequences.Understanding Ca 2ϩ signaling requires the basic knowledge of structures involved in this process. Among these structures are the Ca 2ϩ transport proteins inserted in the membranes of the endoplasmic reticulum (ER), 1 the intracellular reservoir of Ca 2ϩ ions. These include Ca 2ϩ channels (ryanodine and inositol 1,4,5-trisphosphate receptor channels) and Ca 2ϩ pumps (sarco/endoplasmic reticulum Ca 2ϩ -ATPases (SERCAs)). Although much data are available on the role of the channels in the elaboration of the Ca 2ϩ signal, little is known concerning how the signal may be modified by expression of SERCAs with different functional properties.In recent years, enormous advances in our understanding of SERCA structure-function relationships were made, including new insights regarding their three-dimensional structure (2, 3). Furthermore, relevant physiological functions of SERCAs have been defined through their potential role in various human diseases (4-6). However, some of the results contrast with those obtained in mice using SERCA1-3 knock ...

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“…The SERCA isoforms differ mainly by their affinity for Ca 2+ (2b > 2a = 1 >> 3) and their Ca 2+ transport turnover rates, SERCA2b having the lowest transport capacity of all SERCAs [350] . Both SERCA2a and SERCA3 have been found in isolated and in situ ECs [106,[351][352][353][354][355][356] , albeit SERCA3 transcript levels decrease during EC proliferation in culture and in hypertension [106,112] . SERCA3 expression is regulated by Ca 2+ itself in a calcineurin/NFAT-dependent manner [357] and its genetic deletion leads to a decrease in agonist-induced elevation in [Ca 2+ ]i and NO synthesis [358] .…”

Section: +mentioning

confidence: 99%

Update on vascular endothelial Ca²⁺signalling: A tale of ion channels, pumps and transporters

Moccia

Berra‐Romani²,

Tanzi³

2012

WJBC

110

192

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A monolayer of endothelial cells (ECs) lines the lumen of blood vessels and forms a multifunctional transducing organ that mediates a plethora of cardiovascular processes. The activation of ECs from as state of quiescence is, therefore, regarded among the early events leading to the onset and progression of potentially lethal diseases, such as hypertension, myocardial infarction, brain stroke, and tumor. Intracellular Ca 2+ signals have long been know to play a central role in the complex network of signaling pathways regulating the endothelial functions. Notably, recent work has outlined how any change in the pattern of expression of endothelial channels, transporters and pumps involved in the modulation of intracellular Ca 2+ levels may dramatically affect whole body homeostasis. Vascular ECs may react to both mechanical and chemical stimuli by generating a variety of intracellular Ca 2+ signals, ranging from brief, localized Ca 2+ pulses to prolonged Ca 2+ oscillations engulfing the whole cytoplasm. The well-defined spatiotemporal profile of the subcellular Ca 2+ signals elicited in ECs by specific extracellular inputs depends on the interaction between Ca 2+ releasing channels, which are located both on the plasma membrane and in a number of intracellular organelles, and Ca 2+ removing systems. The present article aims to summarize both the past and recent literature in the field to provide a clear-cut picture of our current knowledge on the molecular nature and the role played by the components of the Ca 2+ machinery in vascular ECs under both physiological and pathological conditions.

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Basal Transcription of the Mouse Sarco(endo)plasmic Reticulum Ca2+-ATPase Type 3 Gene in Endothelial Cells Is Controlled by Ets-1 and Sp1

Cited by 23 publications

References 52 publications

The Loss of Sarco/Endoplasmic Reticulum Calcium Transport ATPase 3 Expression Is an Early Event during the Multistep Process of Colon Carcinogenesis

The Loss of Sarco/Endoplasmic Reticulum Calcium Transport ATPase 3 Expression Is an Early Event during the Multistep Process of Colon Carcinogenesis

Identification, Expression, Function, and Localization of a Novel (Sixth) Isoform of the Human Sarco/Endoplasmic Reticulum Ca2+ATPase 3 Gene

Update on vascular endothelial Ca²⁺signalling: A tale of ion channels, pumps and transporters

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Basal Transcription of the Mouse Sarco(endo)plasmic Reticulum Ca2+-ATPase Type 3 Gene in Endothelial Cells Is Controlled by Ets-1 and Sp1

Cited by 23 publications

References 52 publications

The Loss of Sarco/Endoplasmic Reticulum Calcium Transport ATPase 3 Expression Is an Early Event during the Multistep Process of Colon Carcinogenesis

The Loss of Sarco/Endoplasmic Reticulum Calcium Transport ATPase 3 Expression Is an Early Event during the Multistep Process of Colon Carcinogenesis

Identification, Expression, Function, and Localization of a Novel (Sixth) Isoform of the Human Sarco/Endoplasmic Reticulum Ca2+ATPase 3 Gene

Update on vascular endothelial Ca2+signalling: A tale of ion channels, pumps and transporters

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Product

Resources

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Update on vascular endothelial Ca²⁺signalling: A tale of ion channels, pumps and transporters