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4 edition of Calreticulin modulates cell adhesiveness found in the catalog.

Calreticulin modulates cell adhesiveness

Greta Kaur Jass

Calreticulin modulates cell adhesiveness

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Published by National Library of Canada = Bibliothèque nationale du Canada in Ottawa .
Written in English


Edition Notes

SeriesCanadian theses = Thèses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches.
ID Numbers
Open LibraryOL18673303M
ISBN 100612291960
OCLC/WorldCa46583642

Calreticulin, a Ca(2+)-storage and chaperone protein of the ER, has also been shown to affect cell adhesiveness. To examine the effects of differential expression of calreticulin on cellular. Abstract. It is widely accepted that Ca 2+ is a universal signaling molecule in the cell (Pozzan et al., ).Due to the versatility of Ca 2+ signaling both, Ca 2+ storage and release must be tightly controlled in spatiotemporal manner (Petersen and Burdakov, ).While several organelles participate in control of Ca 2+ homeostasis, the endoplasmic reticulum (ER) appears to be the most. Calreticulin (CRT), a Ca(2+)-binding storage protein and chaperone in the endoplasmic reticulum, modulates cell adhesiveness and integrin-dependent Ca(2+) signaling.


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Calreticulin modulates cell adhesiveness by Greta Kaur Jass Download PDF EPUB FB2

Calreticulin, a Ca(2+) storage protein and chaperone in the endoplasmic reticulum, also modulates cell adhesiveness. Overexpression of calreticulin correlates with (i) increased cell adhesiveness.

Calreticulin modulates cell adhesiveness via regulation of vinculin expression. Opas M 1, Szewczenko-Pawlikowski M, Jass GK, Mesaeli N, Michalak M. Author information. Affiliations. 1 author. Department of Anatomy and Cell Biology, University of Toronto, Ontario, Canada.

Cited by: 1. J Cell Biol. Dec;(6 Pt 2) Calreticulin modulates cell adhesiveness via regulation of vinculin expression. Opas M(1), Szewczenko-Pawlikowski M, Jass GK, Mesaeli N, Michalak by: Calreticulin Modulates Cell Adhesiveness via Regulation of Vinculin Expression Michal Opas,* Malgorzata Szewczenko-Pawlikowski,* Greta K.

Jass,* Nasrin Mesaeli,*. Calreticulin modulates cell adhesiveness via regulation of vinculin expression.

Abstract. Calreticulin is an ubiquitous and highly conserved high capacity Ca(2+)- binding protein that plays a major role in Ca2+ storage within the lumen of the ER.

Here, using L fibroblast cell lines expressing different levels of calreticulin, we show that. Calreticulin modulates cell adhesiveness via regulation of vinculin expression. By Michal Opas, Malgorzata Szewczenko-pawlikowski, Greta K.

Jass, Nasrin Mesaeli and Marek Michalak. Abstract. Abstract. Calreticulin is an ubiquitous and highly conserved high capacity Ca2+-binding protein that plays a major role in Ca 2 ÷ storage within the.

Abstract. To study the role of calreticulin in Ca 2+ homeostasis and apoptosis, we generated cells inducible for full-length or truncated calreticulin and measured Ca 2+ Calreticulin modulates cell adhesiveness book within the cytosol, the endoplasmic reticulum (ER), and mitochondria with “cameleon” indicators.

Induction of calreticulin increased the free Ca 2+ concentration within the ER lumen, [Ca 2+] ER, from ± 31 to. Calreticulin is an abundant 46 kDa, high capacity Ca 2+-binding protein found (with the exception of erythrocytes) in every cell of higher ural predictions for calreticulin suggest that it has at least three structural and functional domains ().The protein has an N-terminal signal sequence that is processed cotranslationally (R.

Clark, University of Texas Health Science. Abstract. Calreticulin, a Ca 2+ storage protein and chaperone in the endoplasmic reticulum, also modulates cell adhesiveness. Overexpression of calreticulin correlates with (i) increased cell adhesiveness, (ii) increased expression of N-cadherin and vinculin, and (iii) decreased protein phosphorylation on tyrosine.

Calreticulin is an unusual luminal ER protein. Several unique functions have been postulated for the protein, including modulation of gene expression (Burns et al., ; Dedhar et al., ; Michalak et al., ), a role in cell adhesion (Coppolino et al., ; Opas et al., ), and maintenance of intracellular Ca 2+ homeostasis including control of store-operated Ca 2+ influx (Liu et al.

cell/matrix interaction, after transplantation has limited the regenerative capacity of these cells in vivo. It is known that adhesion is a key factor for the differentiation of MSCs. In this study, we genetically modified rat mesenchymal stem cells with calreticulin (CRT) ex vivo to enhance the adhesiveness.

1. Introduction. As a Calreticulin modulates cell adhesiveness book 2+-binding protein, calreticulin (CRT) was firstly identified from rabbit skeletal muscle by Ostwald and MacLennan in [].Since then, CRT has been abundantly studied in vertebrates, invertebrates, and higher plants [].CRT can be divided into three domains: the amino-terminal N domain, the flexible mid proline-rich P domain, and the highly acidic carboxyl.

contacts [6]. Bulk of calreticulin has been shown to reside in the ER []. Hence, an alternative has been proposed, that calreticulin may participate in signalling pathway(s) from the lumen of the ER to the cell surface that modulates cell adhesiveness [16].

In the present report, we used transformed L fibroblast cell lines stably and. THE EMERGIN ROLE OF CALRETICULIN IN CANCER CELLS evidence that modification of CALR levels affects cell adhesion on extracellular matrix molecules (ECM)6,7. In fact, is noted that CALR plays a role in the control of cell adhesiveness through regula - tion of fibronectin expressions and collagen depo-sition mediated by Ca2++- regulation and c-SRC.

To determin e whether these functions do, in fact, involve calreticulin, investigators have created calreticulin-deficient mice. In a first step, embryonic stem cells th at lack calreticulin were generated. 5 The phenotype of rhese cells indicates that calreticulin plays a role in both modul ation of cell adhesiveness and in control of Ca 2.

BibTeX @ARTICLE{Opas96calreticulinmodulates, author = {Michal Opas and Malgorzata Szewczenko-pawlikowski and Greta K. Jass and Nasrin Mesaeli and Marek Michalak}, title = {Calreticulin modulates cell adhesiveness via regulation of vinculin expression}, journal = {J.

Cell}, year = {}, pages = {. Calreticulin, however, participates in Ca2+ homeostasis as its level of expression affects cell viability at low concentrations of extracellular Ca2+. Consequently, we infer that it is not the Ca2+ storage function of calreticulin that affects cell adhesiveness.

Neither endogenous calreticulin nor overexpressed green fluorescent protein. Calreticulin is a multifunctional Ca 2+ binding chaperone in the endoplasmic reticulum and expression of the protein is tightly regulated at the transcriptional level.

There are two calreticulin genes, named calreticulin-1 and calreticulin-2 gene. The calreticulin-1 promoter contains a number of putative binding sites for transcription factors including tissue specific factors. Abstract. Calreticulin is a Ca 2+-buffering ER chaperone that also modulates cell order to study the effect of calreticulin on the expression of adhesion-related genes, we created a calreticulin inducible Human Embryonic Kidney (HEK) cell line.

Calreticulin Is a Cell Surface Protein. Expression of CRT has been reported on the surface of several types of cells. 9 12 CRT has an N-terminal signal sequence and potentially can be transported to the cell surface. 2 Gray et al showed that cell surface CRT on fibroblasts binds to the β chain of fibrinogen mediating its mitogenic activity.

10 White et al found that CRT is expressed on the. The ability of calreticulin to suppress tumor metastasis is consistent with its ability to enhance cell adhesion, 42, 43 Increased expression of calreticulin resulted in the increased cell–substratum and cell–cell adhesiveness and was likely a result of an increase in vinculin and N-cadherin,21, 43 proteins essential for cell–cell.

CALRETICULIN AFFECTS CELL ADHESIVENESS THROUGH. Michalak, M. Calreticulin modulates cell adhesiveness via regulation of. vinculin expression. Cell Biol. () – INTRODUCTION. Calreticulin is a calcium-binding protein mainly present in the lumen of the endoplasmic reticulum of the cell that also has functions in other cellular compartments ().Calreticulin’s cytoplasmic role was shown in fibroblasts from mice with homozygous deletions in the calreticulin gene ().These mice had defects in integrin-mediated cell adhesion to extracellular matrix as well.

[2], and it also modulates cell adhesiveness by regulating the expression of several genes encoding adhesion pro-teins, namely vinculin – a cytoskeletal protein and N-cad-herin, a cell membrane protein []. Although calreticulin was originally discovered in striated muscle [], its expression there is very low and no clear role has.

Calreticulin was first isolated 26 years ago. Since its discovery as a minor Ca2+-binding protein of the sarcoplasmic reticulum, the appreciation of its importance has grown, and it is now recognized to be a multifunctional protein, most abundant in the endoplasmic reticulum (ER).

The protein has well-recognized physiological roles in the ER as a molecular chaperone and Ca2+-signalling molecule. Calreticulin is a kDa Ca 2+-binding chaperone of the endoplasmic reticulum protein binds Ca 2+ with high capacity, affects intracellular Ca 2+ homeostasis, and functions as a lectin-like chaperone.

In this study, we describe expression and purification procedures for the isolation of recombinant rabbit calreticulin. In the United States, bladder cancer was among the top 10 most frequently diagnosed cancers in 1 The most common type of bladder cancer is transitional cell carcinoma, a malignant tumor that grows from the epithelium of the bladder.

Approximately 30% of patients present with a muscle-invasive metastasis at the time of diagnosis, and 85% of these patients will die of the disease.

Calreticulin is a Ca 2+-binding chaperone 12 that is located in the lumen of the ER ().It interacts in a Ca 2+-dependent manner with other ER chaperones and modulates their function8, iculin also undergoes dynamic, Ca 2+-dependent interactions with newly synthesized proteins and with ER proteins involved in Ca 2+ transport13, Importantly, calreticulin affects Ca 2+.

Calreticulin is a highly conserved endoplasmic reticulum chaperone protein which participates in various cellular processes. It was first identified as a Ca 2+ -binding protein in Accumulated evidences indicate that calreticulin has great impacts for the development of different cancers and the effect of calreticulin on tumor formation and progression may depend on cell types and.

Calreticulin is an endoplasmic reticulum resident protein of approximately 46 kDa molecular weight with multiple functions, including control of cellular adhesiveness, gene expression, calcium homeostasis regulation, and molecular chaperoning.

23 It acts as a multifunctional protein that behaves as a molecular chaperone and contributes to CD Calreticulin is a highly conserved endoplasmic reticulum chaperone protein which participates in various cellular processes. It was first identified as a Ca 2+-binding protein in Accumulated evidences indicate that calreticulin has great impacts for the development of different cancers and the effect of calreticulin on tumor formation and progression may depend on cell types and clinical.

Books; JCB Journal of Cell Biology; The editors of The Journal of Cell Biology have been notified by Dr. Michal Opas that he and the other authors of the paper referenced above retract the paper.

As a result of this retraction, no data in this paper should be cited in the scientific literature. Calreticulin modulates cell adhesiveness. Calreticulin modulates steroid-sensitive gene expression (Burns et al., a, It will be important to test the effects of the cytoplasmic versus the ER form of calreticulin on cell adhesiveness and Ca 2+ influx to establish if calreticulin may also affect these processes indirectly from the lumen of the ER.

The ability of calreticulin to suppress tumor metastasis is consistent with its ability to enhance cell adhesion. 20, 42, 43 Increased expression of calreticulin resulted in the increased cell–substratum and cell–cell adhesiveness and was likely a result of an increase in vinculin and N-cadherin, 21, 43 proteins essential for cell–cell.

Calreticulin also known as calregulin, CRP55, CaBP3, calsequestrin-like protein, and endoplasmic reticulum resident protein 60 (ERp60) is a protein that in humans is encoded by the CALR gene.

Calreticulin is a multifunctional soluble protein that binds Ca 2+ ions (a second messenger in signal transduction), rendering it Ca 2+ is bound with low affinity, but high capacity, and can. Calreticulin is a Ca(2+)-buffering ER chaperone that also modulates cell adhesiveness.

In order to study the effect of calreticulin on the expression of adhesion-related genes, we created a. Opas et al., Calreticulin modulates cell adhesiveness via regulation of vinculin expression.

Cell Biol. ; Fadel et al., Calreticulin signals from the ER via β-catenin-associated pathways. Biol. Chem. ; Papp, et al. Is all endoplasmic reticulum created equal. The effects of the heterogeneous.

Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion M. et al. Calreticulin modulates cell adhesiveness via regulation of vinculin Calreticulin is a.

Calreticulin is a ubiquitous calcium-binding protein with wide tissue distribution found in all eukaryotic cells with the exception of yeast [], whose remarkable conservation implies an important biological the lumen of the endoplasmic reticulum (ER), calreticulin functions as a calcium buffer and a lectin-like molecular chaperone [], and it also modulates cell adhesiveness by.

Calreticulin is a ubiquitous Ca 2+ binding protein, located in the endoplasmic reticulum lumen, which has been implicated in many diverse functions including: regulation of intracellular Ca 2+ homeostasis, chaperone activity, steroid-mediated gene regulation, and cell adhesion.

To understand the physiological function of calreticulin we used gene targeting to create a knockout mouse for. These functions include chaperon activity, control of intracellular Ca 2+ homeostasis, and regulation of cell adhesiveness by interacting with the integrins at the cytoplasmatic site of the plasma membrane.

Surprisingly, calreticulin controls the steroid‐sensitive gene expression [[43, 44]].Nguyen TO, Capra JD, Sontheimer RD. Calreticulin is transcriptionally upregulated by heat shock, calcium and heavy metals. Mol Immunol. ; – Opas M, Szewczenko-Pawlikowski M, Jass GK, Mesaeli N, Michalak M. Calreticulin modulates cell adhesiveness via regulation of vinculin expression.

J Cell Biol. ; –Protein tyrosine phosphorylation is a major event for the cell adhesive mechanism. 43,44 Cell adhesiveness decreases in CRT-underexpressing mouse L fibroblasts that contain higher levels of active c Mesaeli N., Michalak M.

Calreticulin modulates cell adhesiveness via regulation of vinculin expression. J Cell Biol. ; –