Bioscience Chapter Database :: 3635 Chapters Now Online

Chapter category: Cell Metabolism

Calreticulin in C. elegans

This chapter appears in the following book:

Calreticulin
Second Edition

Edited by: Paul Eggleton and Marek Michalak
ISBN: 0-306-47845-5
» Get more information about this book at landesbioscience.com «

Chapter authors:
Byung-Jae Park, Jin Il Lee and Joohong Ahnn


[+] view image
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 and fertile, offering the opportunity for scientists to study in vivo functions of calreticulin at more depth. crt-1 null mutants showed temperature-sensitive fertility defects, and transcription of crt-1 was upregulated in stress conditions such as high temperature and ethanol treatment suggesting that calreticulin may be functioning in stress response. Mutants of the calreticulin gene were also shown to suppress necrotic cell death in neurons. The use of pharmological agents and the genetic application of mutants involved in ER calcium homeostasis showed that calreticulin was critical in the regulation of ER calcium levels during the neuronal degeneration process. Double mutants of crt-1 mutants and itr-1 IP3 receptor mutants displayed synergistic severity in defecation rhythm defects further suggesting the role of calreticulin in ER calcium homeostasis. Further genetic analysis in C. elegans between crt-1 and other components involved in ER calcium regulation should deepen our understanding of calreticulin and calcium homeostasis at both the cellular and organism level.

» Access chapter for $19



Additional chapters 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 ...

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 calreticu...

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. H...

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 t...

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...

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...

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 c...

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,...

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 re...

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 retic...

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 ...

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 ...

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 addit...

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 ...

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 presentati...

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 c...

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 ...

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 glycopr...

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(...

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 an...

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 ...

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,...

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 Sur...


SIGN IN

Email:


Password:


lost password?




[ Home | Authors | Editors | Custom Books | Chapter Reprints | Subscribe | Contact | Biotoons ]