Calreticulin
Second Edition
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Edited By:Paul EggletonPeninsula Medical School, Universities of Exeter and Plymouth, Exeter, UK Marek Michalak University of Alberta ISBN: 978-0-306-47845-1 Published: 2003-07-14 This book may be purchased as an eBook (pdf) for $99, or individual chapters (pdf) may be purchased from the list below for $19. |
Chapters available from this book
Calreticulin Deficient Mouse
Lei Guo
Calreticulin, from its initial discovery, has been considered a multifunctional protein.1 Indeed, many diverse functions have been attributed to this protein, including roles in protein folding and quality control, in modulation of adhesion, in regulation of endoplasmic reticulum (ER) Ca2+ sto...
Calreticulin in C. elegans
Byung-Jae Park, Jin Il Lee and Joohong Ahnn
The nematode C. elegans is an ideal organism to study the in vivo genetic and biochemical functions of calreticulin. In vitro studies show that the C. elegans CRT-1 protein, like other calreticulins, is a calcium-binding molecular chaperone. Mutants of crt-1 in C. elegans mutants are viable an...
The Hookworm Calreticulin Conundrum
D.I. Pritchard, N. Girod, A. Brown, R. Caddick, D.S.W. Hooi, R.J. Quinnell, S.J. Johnson and P. Eggleton
Hookworm parasites possess effective defence mechanisms against host innate and adaptive immune responses such as complement activation, eosinophilia and the respiratory burst in granulocytes. However there does appear to be a strong relationship between helminthic infection and the allergic p...
Role of Calreticulin in Leishmania Parasite Secretory Pathway and Pathogenesis
Alain Debrabant, Nancy Lee, Dennis M. Dwyer and Hira L. Nakhasi
The trypanosomatid parasites Leishmania and Trypanosoma are the causative agents of human diseases such as leishmaniasis, Chagas disease or African sleeping sickness. Some proteins secreted by these protozoan parasites represent virulence factors and contribute to the survival of these pathoge...
Calreticulin Regulation of Lung Endothelial NOS Activity
Jawaharlal M. Patel, Jianliang Zhang, Yong D. Li and Edward R. Block
Increased synthesis of a multifunctional calcium binding protein calreticulin has been reported under diverse physiologic and pathophysiologic conditions in various tissues in cluding stimulation of vascular endothelium by angiotensin IV (Ang-IV), a metabolic product of Ang-II. Ang-IV-mediated ...
Cell Surface Calreticulin: Role in Signaling Thrombospondin Anti-Adhesive Activity
Silvia M. Goicoechea and J.E. Murphy-Ullrich
Cell adhesion is a multi-step process initiated by receptor binding to extracellular matrix (ECM) components. This triggers intracellular signaling cascades leading to spreading and organization of the cytoskeleton with focal adhesions. Essential cellular processes such as locomotion, gene exp...
Calreticulin’s Role(s) in Autoimmune Disorders
Richard D. Sontheimer, Doina Racila, Emil Racila, Paul Eggleton
For over ten years autoantibodies (Aab) against calreticulin (CRT) have been reported in a number of autoimmune disorders including rheumatoid arthritis, Sjögren’s syndrome, celiac disease and complete congenital heart block. The most studied group is patients with systemic lupus erythematosus...
Calreticulin and Tumor Suppression
Giovanna Tosato, Lei Yao and Sandra E. Pike
Lymphoblastic cell lines derived by Epstein-Barr virus (EBV) immortalization of normal B lymphocytes can reproducibly inhibit tumor growth in nude mice. This anti-tumor activity is due, in part, to a mediator present in the culture supernatant of EBV-immortalized lymphoblastic cells identified...
A Role for Calreticulin in the Clearance of Apoptotic Cells and in the Innate Immune System
Peter M. Henson
Calreticulin has been shown to bind the collagenous tails of members of the collectin family of pattern recognition molecules. Its presence on cell surfaces then, implies a potential role for recognition of the collectins, and anything they may have bound via their globular head groups. In add...
Calreticulin in Cytotoxic Lymphocyte-Mediated Cytotoxicity
Dorothy Hudig and Reza Karimi
New functions are implicated for calreticulin, based on its release from cytotoxic NK and T cells. Calreticulin is the only one of six "KDEL" (Lys-Asp-Glu-Leu carboxy terminal) endoplasmic reticulum chaperone proteins present in cytotoxic granules of these lymphocytes. Calreticulin is released...
ER Calcium and ER Chaperones: New Players in Apoptosis?
Nicolas Demaurex, Maud Frieden and Serge Arnaudeau
By using calcium ions as an intracellular messenger, cells walk a tight rope between life and death. Because critical cellular functions depend on the precise delivery of Ca2+ at the right time and place, calcium ions must navigate at all times between intracellular calcium stores and target p...
Calnexin and Calreticulin, ER Associated Modulators of Calcium Transport in the ER
Patricia Camacho, Linu John, Yun Li, R. Madelaine Paredes
Calreticulin (CRT) and calnexin (CNX) are members of a family of endoplasmic reticulum (ER) chaperones that fold newly synthesized polypeptides. Aside from their role as foldases in the ER, our laboratory has shown that all members of this family of proteins modulate Ca2+ oscillations. In Xeno...
Modulation of Calcium Homeostasis by the Endoplasmic Reticulum in Health and Disease
György Szabadkai, Mounia Chami, Paolo Pinton and Rosario Rizzuto
The endoplasmic reticulum (ER) is the main intracellular agonist-sensitive Ca2+ store, and is involved in the regulation of a wide range of cellular functions depending on cytosolic Ca2+. In addition, it has recently been recognized that Ca2+ regulates also processes occurring in the ER lumen, s...
Calreticulin and the Endoplasmic Reticulum in Plant Cell Biology
Paola Mariani, Lorella Navazio and Anna Zuppini
Calreticulin is ubiquitously expressed in plants. The plant homologue shares with its animal counterpart a similar structural organization and basic functioning. A wide range of developmental and environmental stimuli differentially affect the expression of calreticulin in plant cells, highlight...
The Role of Calnexin and Calreticulin
Raju Adhikari and Tim Elliott
Assembly of Major Histocompatibility Complex (MHC) class I heavy chain (HC) with b2-microglobulin (b2m) and subsequent acquisition of optimal peptides is necessary for class I antigen presentation to cytotoxic T cells (CTLs). Calnexin and calreticulin are two major chaperones involved in the a...
Calreticulin-Mediated Nuclear Protein Export
Ben E. Black and Bryce M. Paschal
The role of calreticulin (CRT) as a molecular chaperone that functions in the endoplasmic reticulum (ER) is well established. This involves transient binding of CRT to hydrophobic residues and carbohydrate chains in polypeptides undergoing folding reactions in the lumen of the ER. The issue of...
Roles of Calreticulin and Calnexin in Myeloperoxidase Synthesis
William M. Nauseef
Polymorphonuclear leukocytes (PMNs) represent the essential cellular component of acute inflammation. As such, PMNs mediate a wide array of functions critical for effective antimicrobial activity and integral for noninfectious proinflammatory events. PMNs contribute to normal host defense using cell...
Calnexin and Calreticulin, Molecular Chaperones of the Endoplasmic Reticulum
Michael R. Leach and David B. Williams
In this chapter we present the evidence that calnexin (CNX) and calreticulin (CRT) function as molecular chaperones to assist in the folding and subunit assembly of the majority of Asn-linked glycoproteins that pass through the endoplasmic reticulum. Mechanistic insights into how this function is a...
Sub-Cellular Distribution of Calreticulin
Sylvia Papp and Michal Opas
Calreticulin is a KDEL-containing protein, yet in many cell types and under variable conditions, it has been found outside of its major residence, the endoplasmic reticulum. While the mechanism(s) behind this ER evasion remain elusive, the importance of calreticulin in certain extra-ER locatio...
Calnexin, an ER Integral Membrane Chaperone in Health and Disease
John J.M. Bergeron and David Y. Thomas
This review discusses the ER protein calnexin that is related in structure and function to calreticulin. In vivo and in vitro experiments from many laboratories have provided evidence that calnexin and calreticulin interact transiently with glycoproteins while they are folding in the ER a that this ...
A Chaperone System for Glycoprotein Folding: The Calnexin/Calreticulin Cycle
Lars Ellgaard and Ari Helenius
The endoplasmic reticulum (ER) contains a particularly wide range of molecular chaperones and other proteins that assist the folding and quality control of newly synthesized protein. Some, like BiP/GRP78 and GRP94, belong to classical chaperone families. Others, like protein disulfide isomeras...
Biochemical and Molecular Properties of Calreticulin
Steven J. Johnson and Kjell O. Håkansson
Calreticulin is a highly abundant Ca2+-storage protein found in all cells of higher organisms, with the exception of erythrocytes. It is predominantly located in the endoplasmic reticulum where, in tandem with the homologue calnexin, it performs an important role in glycoprotein folding, such ...
Introduction to Calreticulin
Paul Eggleton and Marek Michalak
Over 30 years ago calreticulin, then known as the high affinity calcium binding protein (HACBP), was identified and purified from isolated skeletal muscle sarcoplasmic reticulum vesicles.1,2 Surprisingly, it took almost 20 years to realize that the protein is a major component of the endoplasm...
