A5052943656- Endoplasmic Reticulum Stress and Disease
- Autophagy in Disease and Therapy
- Galectins and Cancer Biology
- Signaling Pathways in Disease
- Ion channel regulation and function
- Pancreatic function and diabetes
- Heat shock proteins research
- Cellular transport and secretion
- Cardiac electrophysiology and arrhythmias
- Cardiomyopathy and Myosin Studies
- Calcium signaling and nucleotide metabolism
- RNA regulation and disease
- Ion Channels and Receptors
- Biochemical and Molecular Research
- Phagocytosis and Immune Regulation
- Connexins and lens biology
- Adipose Tissue and Metabolism
- Mitochondrial Function and Pathology
- Muscle Physiology and Disorders
- Peptidase Inhibition and Analysis
- Monoclonal and Polyclonal Antibodies Research
- Immune Cell Function and Interaction
- Ubiquitin and proteasome pathways
- RNA modifications and cancer
- Toxin Mechanisms and Immunotoxins
University of Alberta
2016-2025
Poznan University of Medical Sciences
2020-2023
University of Exeter
2015-2021
Hubei University of Technology
2019-2020
Canadian VIGOUR Centre
2018
McGill University
2002-2015
Nankai University
2014
Gwangju Institute of Science and Technology
2010
Yale University
1997-2008
Laboratoire de Biochimie
2008
All eukaryotic cells respond to the accumulation of unfolded proteins in endoplasmic reticulum (ER) by signaling an adaptive pathway termed protein response (UPR). In yeast, a type-I ER transmembrane kinase, Ire1p, is proximal sensor lumen that initiates unconventional splicing reaction on HAC1 mRNA. Hac1p transcription factor required for induction UPR genes. higher cells, also induces site-2 protease (S2P)-mediated cleavage ER-localized ATF6 generate N-terminal fragment activates To...
The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of membrane-associated secreted proteins. membrane is also an important site Ca(2+) storage release. Calreticulin unique ER luminal resident protein. protein affects many cellular functions, both lumen outside environment. In lumen, calreticulin performs two major functions: regulation homoeostasis. highly versatile lectin-like chaperone, it participates during variety molecules, including ion channels,...
The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of membrane-associated secreted proteins. membrane is also an important site Ca2+ storage release. Calreticulin unique ER luminal resident protein. protein affects many cellular functions, both lumen outside environment. In lumen, calreticulin performs two major functions: regulation homoeostasis. highly versatile lectin-like chaperone, it participates during variety molecules, including ion channels,...
Calreticulin is a ubiquitous Ca2+ binding protein, located in the endoplasmic reticulum lumen, which has been implicated many diverse functions including: regulation of intracellular homeostasis, chaperone activity, steroid-mediated gene regulation, and cell adhesion. To understand physiological function calreticulin we used targeting to create knockout mouse for calreticulin. Mice homozygous disruption developed omphalocele (failure absorption umbilical hernia) showed marked decrease...
A cDNA clone encoding the high affinity Ca2+-binding protein (HACBP) of rabbit skeletal muscle sarcoplasmic reticulum was isolated and sequenced.The encoded a 418 amino acids, but comparison deduced acid sequence with NH2-terminal purified indicates that 17-residue signal removed during synthesis.This confirmed by studies in vitro translation mRNA protein.Structural predictions did not reveal any potential transmembrane segments protein.The COOH-terminal protein, Lys-Asp-Glu-Leu, is same as...
Recombinant calreticulin and discrete domains of were expressed in Escherichia coli, using the glutathione S-transferase fusion protein system, their Ca2+ binding properties determined.Native bound 1 mol Ca2+/mo1 with high affinity, also approximately 20 low affinity.Both sites present recombinant indicating that proper folding was achieved this system.Calreticulin is structurally divided into three distinct domains: N-domain encompassing first 200 residues; P-domain which enriched proline...
Abstract Background Pancreatic cancer is one of the most lethal malignancies and has an extremely poor diagnosis prognosis. The development resistance to gemcitabine still a major challenge. long noncoding RNA PVT1 was reported be involved in carcinogenesis chemoresistance; however, mechanism by which regulates sensitivity pancreatic remains poorly understood. Methods viability cells assessed MTT assay vitro xenograft tumor formation vivo. expression levels miR-619-5p were detected...
Calreticulin is a Ca2+-binding chaperone in the endoplasmic reticulum (ER), and calreticulin gene knockout embryonic lethal. Here, we used calreticulin-deficient mouse fibroblasts to examine function of as regulator Ca2+ homeostasis. In cells without calreticulin, ER has lower capacity for storage, although free luminal concentration unchanged. Calreticulin-deficient show inhibited release response bradykinin, yet they upon direct activation with inositol 1,4,5-trisphosphate (InsP3). These...
To test the role of ER luminal environment in apoptosis, we generated HeLa cell lines inducible with respect to calreticulin and calnexin investigated their sensitivity drug-dependent apoptosis. Overexpression calreticulin, an protein, resulted increased cells both thapsigargin- staurosporine-induced This correlated release cytochrome c from mitochondria. calnexin, integral membrane had no significant effect on drug-induced In contrast, calreticulin-deficient were significantly resistant...
The widely distributed and highly conserved Ca(2+)-binding protein calreticulin has been suggested to play a role as Ca2+ storage of intracellular Ca+ stores. To test this hypothesis, we have generated mouse L fibroblast cell line stably transfected with expression vector. content the overexpressers was increased by 1.6 +/- 0.2-fold compared mock-transfected cells. total cellular calreticulin-overexpressing control cells, assessed equilibrium 45Ca+2 uptake, 141 8 67 6 pmol Ca2+/10(6)...
Calnexin and calreticulin are homologous molecular chaperones of the endoplasmic reticulum. Their binding to newly synthesized glycoproteins is mediated, at least in part, by a lectin site that recognizes early N-linked oligosaccharide processing intermediate, Glc1Man9GlcNAc2. We compared specificities calnexin an effort determine basis for reported differences their association with various glycoproteins. Using mono-, di-, oligosaccharides inhibit Glc1Man9GlcNAc2 truncated, soluble form...
The loss of tyrosinase, the key enzyme in melanin synthesis, has been implicated dedifferentiation malignant melanocytes. presence tyrosinase transcripts and antigenic peptides melanoma tumors prompted us to investigate whether basis for was proteolytic degradation. Toward this aim, we followed kinetics degradation, processing, chaperone binding, inhibitor sensitivity, subcellular localization normal We found that, amelanotic cell lines, failed reach melanosome, organelle because it retained...