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molecular chaperone and endoplasmic reticulum

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https://www.readbyqxmd.com/read/29774376/roles-of-heat-shock-factor-1-beyond-the-heat-shock-response
#1
REVIEW
János Barna, Péter Csermely, Tibor Vellai
Various stress factors leading to protein damage induce the activation of an evolutionarily conserved cell protective mechanism, the heat shock response (HSR), to maintain protein homeostasis in virtually all eukaryotic cells. Heat shock factor 1 (HSF1) plays a central role in the HSR. HSF1 was initially known as a transcription factor that upregulates genes encoding heat shock proteins (HSPs), also called molecular chaperones, which assist in refolding or degrading injured intracellular proteins. However, recent accumulating evidence indicates multiple additional functions for HSF1 beyond the activation of HSPs...
May 17, 2018: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/29769092/mineralization-of-alpha-1-antitrypsin-inclusion-bodies-in-mmalton-alpha-1-antitrypsin-deficiency
#2
Francesco Callea, Isabella Giovannoni, Paola Francalanci, Renata Boldrini, Gavino Faa, Daniela Medicina, Valerio Nobili, Valeer J Desmet, Kamal Ishak, Kuniaki Seyama, Emanuele Bellacchio
BACKGROUND: Alpha-1-antitrypsin (AAT) deficiency (AATD) of Z, Mmalton, Siiyama type is associated with liver storage of the mutant proteins and liver disease. The Z variant can be diagnosed on isoelectric focusing (IEF) while Mmalton and Siiyama may be missed or misdiagnosed with this technique. Therefore, molecular analysis is mandatory for their characterization. In particular, that holds true for the Mmalton variant as on IEF profile it resembles the wild M2 subtype. METHODS: This is a retrospective analysis involving review of medical records and of liver biopsy specimens from a series of Mmalton, Z and Siiyama Alpha-1-antitrypsin deficiency patients...
May 16, 2018: Orphanet Journal of Rare Diseases
https://www.readbyqxmd.com/read/29761862/cellular-stress-and-apoptosis-contribute-to-the-pathogenesis-of-autism-spectrum-disorder
#3
Daoyin Dong, Horst Ronald Zielke, David Yeh, Peixin Yang
The molecular pathogenesis of autism spectrum disorder, a neurodevelopmental disorder, is still elusive. In this study, we investigated the possible roles of endoplasmic reticulum (ER) stress, oxidative stress, and apoptosis as molecular mechanisms underlying autism. This study compared the activation of ER stress signals (protein kinase R-like endoplasmic reticulum kinase [PERK], activating transcription factor 6 [ATF6], inositol-requiring enzyme 1 alpha [IRE1α]) in different brain regions (prefrontal cortex, hippocampus, cerebellum) in subjects with autism and in age-matched controls...
May 15, 2018: Autism Research: Official Journal of the International Society for Autism Research
https://www.readbyqxmd.com/read/29750876/evaluation-of-molecular-changes-of-distal-organs-after-small-bowel-transplantation-experimental-study
#4
P Urban, M Rabajdová, Š Feterik, G Bódy, T Granda, M Mareková, J Veselá
The ischemia and reperfusion of a jejunal graft during transplantation triggers the stress of endoplasmic reticulum; thus inducing the synthesis of pro-inflammatory cytokines. Spreading of these signals stimulate immunological reactions in distal tissues i.e. lung, liver and spleen. The aim of this study was to detect the molecular changes in liver and spleen induced by transplanted jejunal graft with one or six hours of reperfusion (group Tx1 and Tx6). Analysis of gene expression changes of inflammatory mediators (TNFalpha, IL-10) and specific chaperones (Gadd153, Grp78) derived from endoplasmic reticulum (ER) was done and compared to control group...
May 10, 2018: Physiological Research
https://www.readbyqxmd.com/read/29744892/-epigallocatechin-3-gallate-induces-grp78-accumulation-in-the-er-and-shifts-mesothelioma-constitutive-upr-into-proapoptotic-er-stress
#5
Simona Martinotti, Elia Ranzato, Bruno Burlando
GRP78 is a molecular chaperone of the endoplasmic reticulum (ER) that aids proper folding of nascent polypeptides. When unfolded proteins accumulate, GRP78 triggers unfolded protein response (UPR), involving activation of transcription factors like XBP1 and CHOP that may restore cell homeostasis. Increased expression of GRP78 and mild UPR can be constitutive in cancer cells, hindering apoptosis, and promoting cell survival, for example, by GRP78 relocation to the plasma membrane that activates MAPK and PI3 K/AKT pathways...
May 10, 2018: Journal of Cellular Physiology
https://www.readbyqxmd.com/read/29743537/molecular-mechanism-of-er-stress-induced-pre-emptive-quality-control-involving-association-of-the-translocon-derlin-1-and-hrd1
#6
Hisae Kadowaki, Pasjan Satrimafitrah, Yasunari Takami, Hideki Nishitoh
The maintenance of endoplasmic reticulum (ER) homeostasis is essential for cell function. ER stress-induced pre-emptive quality control (ERpQC) helps alleviate the burden to a stressed ER by limiting further protein loading. We have previously reported the mechanisms of ERpQC, which includes a rerouting step and a degradation step. Under ER stress conditions, Derlin family proteins (Derlins), which are components of ER-associated degradation, reroute specific ER-targeting proteins to the cytosol. Newly synthesized rerouted polypeptides are degraded via the cytosolic chaperone Bag6 and the AAA-ATPase p97 in the ubiquitin-proteasome system...
May 9, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29721972/molecular-chaperone-erp29-a-potential-target-for-cellular-protection-in-retinal-and-neurodegenerative-diseases
#7
Todd McLaughlin, Marek Falkowski, Joshua J Wang, Sarah X Zhang
The molecular chaperone endoplasmic reticulum protein 29 (ERp29) plays a critical role in protein folding, trafficking, and secretion. Though ubiquitously expressed, ERp29 is upregulated in response to ER stress and is found at higher levels in certain cell types such as secretory epithelial cells and neurons. As an ER resident protein, ERp29 shares many structural and functional similarities with protein disulfide isomerases, but is not regarded as part of this family due to several key differences. The broad expression and myriad roles of ERp29 coupled with its upregulation via the unfolded protein response (UPR) upon ER stress have implicated ERp29 in a range of cellular processes and diseases...
2018: Advances in Experimental Medicine and Biology
https://www.readbyqxmd.com/read/29718201/perk-inhibition-delays-neurodegeneration-and-improves-motor-function-in-a-mouse-model-of-marinesco-sj%C3%A3-gren-syndrome
#8
Valentina Grande, Francesca Ornaghi, Liliana Comerio, Elena Restelli, Antonio Masone, Alessandro Corbelli, Daniele Tolomeo, Vanessa Capone, Jeffrey M Axten, Nicholas J Laping, Fabio Fiordaliso, Michele Sallese, Roberto Chiesa
Marinesco-Sjögren syndrome (MSS) is a rare, early-onset, autosomal recessive multisystem disorder characterized by cerebellar ataxia, cataracts and myopathy. Most MSS cases are caused by loss-of-function mutations in the gene encoding SIL1, a nucleotide exchange factor for the molecular chaperone BiP which is essential for correct protein folding in the endoplasmic reticulum. Woozy mice carrying a spontaneous Sil1 mutation recapitulate key pathological features of MSS, including cerebellar atrophy with degeneration of Purkinje cells, and progressive myopathy...
April 28, 2018: Human Molecular Genetics
https://www.readbyqxmd.com/read/29696702/mechanical-properties-of-bip-protein-determined-by-nano-rheology
#9
Nathalie Casanova-Morales, Diego Quiroga-Roger, Hilda M Alfaro-Valdés, Zahra Alavi, Miguel I A Lagos-Espinoza, Giovanni Zocchi, Christian A M Wilson
Immunoglobulin Binding Protein (BiP) is a chaperone and molecular motor belonging to the Hsp70 family, involved in the regulation of important biological processes such as synthesis, folding and translocation of proteins in the Endoplasmic Reticulum. BiP has two highly conserved domains: the N-terminal Nucleotide-Binding Domain (NBD), and the C-terminal Substrate-Binding Domain (SBD), connected by a hydrophobic linker. ATP binds and it is hydrolyzed to ADP in the NBD, and BiP's extended polypeptide substrates bind in the SBD...
April 26, 2018: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/29688606/constitutive-bip-protein-accumulation-in-arabidopsis-mutants-defective-in-a-gene-encoding-chloroplast-resident-stearoyl-acyl-carrier-protein-desaturase
#10
Yuji Iwata, Tsukasa Iida, Toshihiro Matsunami, Yu Yamada, Kei-Ichiro Mishiba, Takumi Ogawa, Tetsuya Kurata, Nozomu Koizumi
The unfolded protein response (UPR) occurs when protein folding and maturation are disturbed in the endoplasmic reticulum (ER). During the UPR, a number of genes including those encoding ER-resident molecular chaperones are induced. In Arabidopsis, BiP3 has been used as a UPR marker gene whose expression is strongly induced in response to ER stress. In this study, we mutagenized Arabidopsis plants expressing β-glucuronidase (GUS) gene under the control of BiP3 promoter and isolated a mutant that exhibits strong GUS activity without treatment with ER stress inducers...
April 24, 2018: Genes to Cells: Devoted to Molecular & Cellular Mechanisms
https://www.readbyqxmd.com/read/29670521/the-prenylflavonoid-xanthohumol-reduces-alzheimer-like-changes-and-modulates-multiple-pathogenic-molecular-pathways-in-the-neuro2a-app-swe-cell-model-of-ad
#11
Xianfeng Huang, Jing Wang, Xiao Chen, Pan Liu, Shujin Wang, Fangchen Song, Zaijun Zhang, Feiqi Zhu, Xinfeng Huang, Jianjun Liu, Guoqiang Song, Peter S Spencer, Xifei Yang
Alzheimer's disease (AD) is a progressive neurodegenerative disorder that has proved refractory to drug treatment. Given evidence of neuroprotection in animal models of ischemic stroke, we assessed the prenylflavonoid xanthohumol from the Common Hop ( Humulus lupulus L.) for therapeutic potential in murine neuroblastoma N2a cells stably expressing human Swedish mutant amyloid precursor protein (N2a/APP), a well-characterized cellular model of AD. The ELISA and Western-blot analysis revealed that xanthohumol (Xn) inhibited Aβ accumulation and APP processing, and that Xn ameliorated tau hyperphosphorylation via PP2A, GSK3β pathways in N2a/APP cells...
2018: Frontiers in Pharmacology
https://www.readbyqxmd.com/read/29643986/ajuba-receptor-mediates-the-internalization-of-tumor-secreted-grp78-into-macrophages-through-different-endocytosis-pathways
#12
Xiaoqin La, Lichao Zhang, Hanqing Li, Zhuoyu Li, Guisheng Song, Peng Yang, Yufei Yang
Glucose-regulated protein 78 (GRP78), an ER chaperone, is overexpressed in cancer cells. Solid tumor cells can secrete GRP78 that can promote tumor angiogenesis, differentiation of bone marrow-derived mesenchymal stem cells, tumor cell proliferation and polarization of tumor-associated macrophages. However, the mechanism by which GRP78 functions as a tumor promoter either by staying on the membrane to stimulate intracellular signals or directly entering into cytosolic remains unknown. Here, we reported that an endotoxin-free His-GRP78 protein was purified in vitro that simulates original secreted GRP78...
March 20, 2018: Oncotarget
https://www.readbyqxmd.com/read/29616092/endoplasmic-reticulum-chaperone-glucose-regulated-protein-78-in-gastric-cancer-an-emerging-biomarker
#13
REVIEW
Yan Wang, Jian-Hong Wang, Xun-Lei Zhang, Xiao-Li Wang, Lei Yang
The endoplasmic reticulum (ER) is the principal organelle responsible for the synthesis, initial post-translational modification, folding, export and secretion of proteins. It is also responsible for the maintenance of cellular homeostasis. In response to cellular stress conditions including glucose deprivation, hypoxia and changes in calcium homeostasis, ER stress machinery is activated and triggers the unfolded protein response, resulting in the restoration of homeostasis or activation of cell death. Glucose-regulated protein 78 (GRP78), a molecular chaperone, may be induced by ER stress at the transcriptional and translational level...
May 2018: Oncology Letters
https://www.readbyqxmd.com/read/29571878/expression-analysis-of-protein-homeostasis-pathways-in-the-peripheral-blood-mononuclear-cells-of-sporadic-amyotrophic-lateral-sclerosis-patients
#14
Abhishek Vats, Mandaville Gourie-Devi, Kavita Ahuja, Ankkita Sharma, Saima Wajid, Nirmal Kumar Ganguly, Vibha Taneja
Misfolded protein aggregates are the hallmark of Amyotrophic Lateral Sclerosis (ALS) which suggests involvement of protein homeostasis pathways in etiology of ALS. However, status of protein homeostasis in peripheral blood of ALS is not well established. We analyzed expression levels of key genes of proteostasis pathways in peripheral blood mononuclear cells (PBMCs) of sporadic ALS (sALS) patients and healthy controls. Increased protein carbonylation was observed in patients reflecting oxidative damage in PBMCs...
April 15, 2018: Journal of the Neurological Sciences
https://www.readbyqxmd.com/read/29570364/protein-quality-control-in-the-endoplasmic-reticulum-of-plants
#15
Richard Strasser
The endoplasmic reticulum (ER) is the site of maturation for roughly onethird of all cellular proteins. ER-resident molecular chaperones and folding catalysts promote folding and assembly in a diverse set of newly synthesized proteins. Because these processes are error-prone, all eukaryotic cells have a quality control system in place that constantly monitors the proteins and decides their fate. Proteins with potentially harmful nonnative conformations are subjected to assisted folding or degraded. Persistent folding-defective proteins are distinguished from folding intermediates and targeted for degradation by a specific process involving clearance from the ER...
March 23, 2018: Annual Review of Plant Biology
https://www.readbyqxmd.com/read/29562214/tissue-specific-molecular-and-cellular-toxicity-of-pb-in-the-oyster-crassostrea-gigas-mrna-expression-and-physiological-studies
#16
Jie Meng, Wen-Xiong Wang, Li Li, Guofan Zhang
Lead (Pb) is one of the ubiquitous and toxic elements in aquatic environment. In oysters, gills and digestive glands are the main target organs for Pb-induced toxicity, but there is limited information on the molecular mechanisms underlying its toxicity. The present study investigated the Pb-induced toxicity mechanisms in the Pacific oyster (Crassostrea gigas) based on transcriptome, phenotypic anchoring, and validation of targeted gene expression. Gene ontology and pathway enrichment analyses revealed the differential Pb toxicity mechanisms in the tissues...
March 13, 2018: Aquatic Toxicology
https://www.readbyqxmd.com/read/29500369/mahanine-drives-pancreatic-adenocarcinoma-cells-into-endoplasmic-reticular-stress-mediated-apoptosis-through-modulating-sialylation-process-and-ca-2-signaling
#17
Sayantani Sarkar Bhattacharya, Chandan Mandal, Reinhard Schwartz Albiez, Suman Kumar Samanta, Chitra Mandal
Endoplasmic reticulum (ER) stress results from protein unfolding/misfolding during cellular maturation, which requires a coordinated action of several chaperones and enzymes and Ca2+ signalling. ER-stress possibly has a positive effect on survival of pancreatic cancer cell. Therefore, detailed insights into this complex signaling network are urgently needed. Here, we systematically analyzed the impact of ER stress-mediated unfolded protein response (UPR) and Ca2+ -signaling cross-talk for the survival of pancreatic adenocarcinoma (PDAC) cells...
March 2, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29481309/tnf-%C3%AE-mediated-er-stress-causes-elimination-of-mycobacterium-fortuitum-reservoirs-by-macrophage-apoptosis
#18
Sung-Man Oh, Yun-Ji Lim, Ji-Ae Choi, Junghwan Lee, Soo-Na Cho, Dam Go, Seon-Hwa Kim, Chang-Hwa Song
Mycobacterium fortuitum (MF), a rapidly growing nontuberculosis mycobacterium, is recognized as an important human pathogen. We investigated whether the endoplasmic reticulum (ER) stress response is associated with the apoptosis of MF-infected macrophages. The expression of ER molecular chaperones was significantly induced by MF infection. We found that MF-induced reactive oxygen species (ROS) generation plays a critical role in the induction of ER stress-mediated apoptosis. Excess TNF-α in the ER led to ER stress-mediated apoptosis during MF infection...
February 26, 2018: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
https://www.readbyqxmd.com/read/29462355/small-molecule-modulator-of-protein-disulfide-isomerase-attenuates-mutant-huntingtin-toxicity-and-inhibits-endoplasmic-reticulum-stress-in-a-mouse-model-of-huntington-s-disease
#19
Xiao Zhou, Gang Li, Anna Kaplan, Michael M Gaschler, Xiaoyan Zhang, Zhipeng Hou, Mali Jiang, Roseann Zott, Serge Cremers, Brent R Stockwell, Wenzhen Duan
Huntington's disease (HD) is caused by a cytosine-adenine-guanine (CAG) trinucleotide repeat expansion in the huntingtin (HTT) gene encoding an elongated polyglutamine tract within the N-terminal of the huntingtin protein (Htt) and leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms. Chronic activation of endoplasmic reticulum (ER) stress by mutant Htt (mHtt) results in cellular dysfunction and ultimately cell death. Protein disulfide isomerase (PDI) is a chaperone protein located in the ER...
May 1, 2018: Human Molecular Genetics
https://www.readbyqxmd.com/read/29453988/silencing-calreticulin-gene-might-protect-cardiomyocytes-from-angiotensin-ii-induced-apoptosis
#20
Wen Zhang, Zhiyue Liu, Yanmei Zhang, Qinxue Bao, Wenchao Wu, He Huang, Xiaojing Liu
AIMS: Calreticulin (CRT), as a chaperone, contributes to protein folding and quality control cycle. CRT is an important factor regulating Ca2+ that participates in cell apoptosis. However, the function of CRT in the heart is still controversial. Therefore, we aimed to investigate the potential role of CRT in angiotensin II-induced cardiomyocytes apoptosis. MAIN METHODS: Primary cultured neonatal cardiomyocytes were stimulated with angiotensin II to induce the apoptosis...
April 1, 2018: Life Sciences
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