Protein Disulfide-Isomerase A6 Recombinant Protein Cat

Total Page：16

File Type：pdf, Size：1020Kb

Protein Disulfide-Isomerase A6 Recombinant Protein Cat. No.: 91-476 Protein Disulfide-Isomerase A6 Recombinant Protein Specifications SPECIES: Human SOURCE SPECIES: Human Cells SEQUENCE: Leu20-Leu440 FUSION TAG: C-6 His tag TESTED APPLICATIONS: APPLICATIONS: This recombinant protein can be used for biological assays. For research use only. PREDICTED MOLECULAR 47.2 kD WEIGHT: Properties Greater than 95% as determined by reducing SDS-PAGE. PURITY: Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. PHYSICAL STATE: Liquid Supplied as a 0.2 um filtered solution of 20mM TrisHCl, 150mM NaCl, 10% Glycerol, pH BUFFER: 8.0. It is not recommended to reconstitute to a concentration less than 100 ug/ml. September 27, 2021 1 https://www.prosci-inc.com/protein-disulfide-isomerase-a6-recombinant-protein-91-476.html Store at -20˚C, stable for 6 months after receipt. STORAGE CONDITIONS: Please aliquot the reconstituted solution to minimize freeze-thaw cycles. Additional Info OFFICIAL SYMBOL: PDIA6 Protein Disulfide-Isomerase A6, Endoplasmic Reticulum Protein 5, ER Protein 5, ERp5, ALTERNATE NAMES: Protein Disulfide Isomerase P5, Thioredoxin Domain-Containing Protein 7, PDIA6, P5, TXNDC7 ACCESSION NO.: Q15084 GENE ID: 10130 Background and References Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its BACKGROUND: functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 27, 2021 2 https://www.prosci-inc.com/protein-disulfide-isomerase-a6-recombinant-protein-91-476.html.

Copy Link

Recommended publications

In Silico Prediction of High-Resolution Hi-C Interaction Matrices
ARTICLE https://doi.org/10.1038/s41467-019-13423-8 OPEN In silico prediction of high-resolution Hi-C interaction matrices Shilu Zhang1, Deborah Chasman 1, Sara Knaack1 & Sushmita Roy1,2* The three-dimensional (3D) organization of the genome plays an important role in gene regulation bringing distal sequence elements in 3D proximity to genes hundreds of kilobases away. Hi-C is a powerful genome-wide technique to study 3D genome organization. Owing to 1234567890():,; experimental costs, high resolution Hi-C datasets are limited to a few cell lines. Computa- tional prediction of Hi-C counts can offer a scalable and inexpensive approach to examine 3D genome organization across multiple cellular contexts. Here we present HiC-Reg, an approach to predict contact counts from one-dimensional regulatory signals. HiC-Reg pre- dictions identify topologically associating domains and significant interactions that are enri- ched for CCCTC-binding factor (CTCF) bidirectional motifs and interactions identified from complementary sources. CTCF and chromatin marks, especially repressive and elongation marks, are most important for HiC-Reg’s predictive performance. Taken together, HiC-Reg provides a powerful framework to generate high-resolution profiles of contact counts that can be used to study individual locus level interactions and higher-order organizational units of the genome. 1 Wisconsin Institute for Discovery, 330 North Orchard Street, Madison, WI 53715, USA. 2 Department of Biostatistics and Medical Informatics, University of Wisconsin-Madison, Madison, WI 53715, USA. *email: [email protected] NATURE COMMUNICATIONS | (2019) 10:5449 | https://doi.org/10.1038/s41467-019-13423-8 | www.nature.com/naturecommunications 1 ARTICLE NATURE COMMUNICATIONS | https://doi.org/10.1038/s41467-019-13423-8 he three-dimensional (3D) organization of the genome has Results Temerged as an important component of the gene regulation HiC-Reg for predicting contact count using Random Forests.
[Show full text]
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
[Show full text]
Investigation of Peptidyl-Prolyl Cis/Trans Isomerases in the Virulence of Staphylococcus
Investigation of Peptidyl-prolyl cis/trans isomerases in the virulence of Staphylococcus aureus A Dissertation presented to the faculty of the College of Arts and Sciences of Ohio University In partial fulfillment of the requirements for the degree Doctor of Philosophy Rebecca A. Keogh August 2020 © 2020 Rebecca A. Keogh. All Rights Reserved. 2 This Dissertation titled Investigation of Peptidyl-prolyl cis/trans isomerases in the virulence of Staphylococcus aureus by REBECCA A. KEOGH has been approved for the Department of Biological Sciences and the College of Arts and Sciences by Ronan K. Carroll Assistant Professor of Biological Sciences Florenz Plassmann Dean, College of Arts and Sciences 3 ABSTRACT REBECCA A. KEOGH, Doctorate of Philosophy, August 2020, Biological Sciences Investigation of peptidyl-prolyl cis/trans isomerases in the virulence of Staphylococcus aureus Director of Dissertation: Ronan K. Carroll Staphylococcus aureus is a leading cause of both hospital and community- associated infections that can manifest in a wide range of diseases. These diseases range in severity from minor skin and soft tissue infections to life-threatening sepsis, endocarditis and meningitis. Of rising concern is the prevalence of antibiotic resistant S. aureus strains in the population, and the lack of new antibiotics being developed to treat them. A greater understanding of the ability of S. aureus to cause infection is crucial to better inform treatments and combat these antibiotic resistant superbugs. The ability of S. aureus to cause such diverse infections can be attributed to the arsenal of virulence factors produced by the bacterium that work to both evade the human immune system and assist in pathogenesis.
[Show full text]
Preclinical Evaluation of Protein Disulfide Isomerase Inhibitors for the Treatment of Glioblastoma by Andrea Shergalis
Preclinical Evaluation of Protein Disulfide Isomerase Inhibitors for the Treatment of Glioblastoma By Andrea Shergalis A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Medicinal Chemistry) in the University of Michigan 2020 Doctoral Committee: Professor Nouri Neamati, Chair Professor George A. Garcia Professor Peter J. H. Scott Professor Shaomeng Wang Andrea G. Shergalis [email protected] ORCID 0000-0002-1155-1583 © Andrea Shergalis 2020 All Rights Reserved ACKNOWLEDGEMENTS So many people have been involved in bringing this project to life and making this dissertation possible. First, I want to thank my advisor, Prof. Nouri Neamati, for his guidance, encouragement, and patience. Prof. Neamati instilled an enthusiasm in me for science and drug discovery, while allowing me the space to independently explore complex biochemical problems, and I am grateful for his kind and patient mentorship. I also thank my committee members, Profs. George Garcia, Peter Scott, and Shaomeng Wang, for their patience, guidance, and support throughout my graduate career. I am thankful to them for taking time to meet with me and have thoughtful conversations about medicinal chemistry and science in general. From the Neamati lab, I would like to thank so many. First and foremost, I have to thank Shuzo Tamara for being an incredible, kind, and patient teacher and mentor. Shuzo is one of the hardest workers I know. In addition to a strong work ethic, he taught me pretty much everything I know and laid the foundation for the article published as Chapter 3 of this dissertation. The work published in this dissertation really began with the initial identification of PDI as a target by Shili Xu, and I am grateful for his advice and guidance (from afar!).
[Show full text]
Atrazine and Cell Death Symbol Synonym(S)
Supplementary Table S1: Atrazine and Cell Death Symbol Synonym(s) Entrez Gene Name Location Family AR AIS, Andr, androgen receptor androgen receptor Nucleus ligand- dependent nuclear receptor atrazine 1,3,5-triazine-2,4-diamine Other chemical toxicant beta-estradiol (8R,9S,13S,14S,17S)-13-methyl- Other chemical - 6,7,8,9,11,12,14,15,16,17- endogenous decahydrocyclopenta[a]phenanthrene- mammalian 3,17-diol CGB (includes beta HCG5, CGB3, CGB5, CGB7, chorionic gonadotropin, beta Extracellular other others) CGB8, chorionic gonadotropin polypeptide Space CLEC11A AW457320, C-type lectin domain C-type lectin domain family 11, Extracellular growth factor family 11, member A, STEM CELL member A Space GROWTH FACTOR CYP11A1 CHOLESTEROL SIDE-CHAIN cytochrome P450, family 11, Cytoplasm enzyme CLEAVAGE ENZYME subfamily A, polypeptide 1 CYP19A1 Ar, ArKO, ARO, ARO1, Aromatase cytochrome P450, family 19, Cytoplasm enzyme subfamily A, polypeptide 1 ESR1 AA420328, Alpha estrogen receptor,(α) estrogen receptor 1 Nucleus ligand- dependent nuclear receptor estrogen C18 steroids, oestrogen Other chemical drug estrogen receptor ER, ESR, ESR1/2, esr1/esr2 Nucleus group estrone (8R,9S,13S,14S)-3-hydroxy-13-methyl- Other chemical - 7,8,9,11,12,14,15,16-octahydro-6H- endogenous cyclopenta[a]phenanthren-17-one mammalian G6PD BOS 25472, G28A, G6PD1, G6PDX, glucose-6-phosphate Cytoplasm enzyme Glucose-6-P Dehydrogenase dehydrogenase GATA4 ASD2, GATA binding protein 4, GATA binding protein 4 Nucleus transcription TACHD, TOF, VSD1 regulator GHRHR growth hormone releasing
[Show full text]
Analysis of Dynamic Molecular Networks for Pancreatic Ductal
Pan et al. Cancer Cell Int (2018) 18:214 https://doi.org/10.1186/s12935-018-0718-5 Cancer Cell International PRIMARY RESEARCH Open Access Analysis of dynamic molecular networks for pancreatic ductal adenocarcinoma progression Zongfu Pan1†, Lu Li2†, Qilu Fang1, Yiwen Zhang1, Xiaoping Hu1, Yangyang Qian3 and Ping Huang1* Abstract Background: Pancreatic ductal adenocarcinoma (PDAC) is one of the deadliest solid tumors. The rapid progression of PDAC results in an advanced stage of patients when diagnosed. However, the dynamic molecular mechanism underlying PDAC progression remains far from clear. Methods: The microarray GSE62165 containing PDAC staging samples was obtained from Gene Expression Omnibus and the diferentially expressed genes (DEGs) between normal tissue and PDAC of diferent stages were profled using R software, respectively. The software program Short Time-series Expression Miner was applied to cluster, compare, and visualize gene expression diferences between PDAC stages. Then, function annotation and pathway enrichment of DEGs were conducted by Database for Annotation Visualization and Integrated Discovery. Further, the Cytoscape plugin DyNetViewer was applied to construct the dynamic protein–protein interaction networks and to analyze dif- ferent topological variation of nodes and clusters over time. The phosphosite markers of stage-specifc protein kinases were predicted by PhosphoSitePlus database. Moreover, survival analysis of candidate genes and pathways was per- formed by Kaplan–Meier plotter. Finally, candidate genes were validated by immunohistochemistry in PDAC tissues. Results: Compared with normal tissues, the total DEGs number for each PDAC stage were 994 (stage I), 967 (stage IIa), 965 (stage IIb), 1027 (stage III), 925 (stage IV), respectively. The stage-course gene expression analysis showed that 30 distinct expressional models were clustered.
[Show full text]
Universidade Federal De Uberlândia Instituto De Biotecnologia Pós-Graduação Em Biotecnologia
UNIVERSIDADE FEDERAL DE UBERLÂNDIA INSTITUTO DE BIOTECNOLOGIA PÓS-GRADUAÇÃO EM BIOTECNOLOGIA MONIZE ANGELA DE ANDRADE IDENTIFICAÇÃO DE CNVR ASSOCIADAS À QUALIDADE DE CARCAÇA E CARNE EM BOVINOS DA RAÇA NELORE PATOS DE MINAS - MG ABRIL DE 2019 MONIZE ANGELA DE ANDRADE IDENTIFICAÇÃO DE CNVR ASSOCIADAS À QUALIDADE DE CARCAÇA E CARNE EM BOVINOS DA RAÇA NELORE Dissertação de Mestrado apresentada ao Programa de Pós-graduação em Biotecnologia como requisito parcial para obtenção do título de Mestre em Biotecnologia. Profa. Dra. Fernanda Marcondes de Rezende PATOS DE MINAS – MG ABRIL DE 2019 MONIZE ANGELA DE ANDRADE IDENTIFICAÇÃO DE CNVR ASSOCIADAS À QUALIDADE DE CARCAÇA E CARNE EM BOVINOS DA RAÇA NELORE Dissertação de Mestrado apresentada ao Programa de Pós-graduação em Biotecnologia como requisito parcial para obtenção do título de Mestre em Biotecnologia. Aprovado em 26/04/2019 BANCA EXAMINADORA ______________________________________________________ Profa Dra Fernanda Marcondes de Rezende ______________________________________________________ Profa Dra Tatiane Cristina Seleguim Chud _______________________________________________________ Profa Dra Terezinha Aparecida Teixeira PATOS DE MINAS – MG ABRIL DE 2019 Dados Internacionais de Catalogação na Publicação (CIP) Sistema de Bibliotecas da UFU, MG, Brasil. A553i Andrade, Monize Angela de, 1993- 2019 Identificação de CNVR associadas à qualidade de carcaça e carne em bovinos da raça nelore [recurso eletrônico] / Monize Angela de Andrade. - 2019. Orientadora: Fernanda Marcondes de Rezende. Dissertação (mestrado) - Universidade Federal de Uberlândia, Programa de Pós-Graduação em Biotecnologia. Modo de acesso: Internet. Disponível em: http://dx.doi.org/10.14393/ufu.di.2019.28 Inclui bibliografia. Inclui ilustrações. 1. Biotecnologia. 2. Gado - Carcaças - Qualidade. 3. Nelore (Zebu). 4. Carne bovina - Qualidade. 5.
[Show full text]
Revealing Bacterial Targets of Growth Inhibitors Encoded by Bacteriophage T7
Revealing bacterial targets of growth inhibitors encoded by bacteriophage T7 Shahar Molshanski-Mora, Ido Yosefa, Ruth Kiroa, Rotem Edgara, Miriam Manora, Michael Gershovitsb, Mia Lasersonb, Tal Pupkob, and Udi Qimrona,1 aDepartment of Clinical Microbiology and Immunology, Sackler School of Medicine, and bDepartment of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel Edited* by Sankar Adhya, National Institutes of Health, National Cancer Institute, Bethesda, MD, and approved November 24, 2014 (received for reviewJuly 13, 2014) Today’s arsenal of antibiotics is ineffective against some emerging suggest that there are other phage products that may inhibit strains of antibiotic-resistant pathogens. Novel inhibitors of bacte- other bacterial targets. rial growth therefore need to be found. The target of such bacterial- A model for the systematic study of host–virus interactions growth inhibitors must be identified, and one way to achieve this and for elucidating phage antibacterial strategies is provided by is by locating mutations that suppress their inhibitory effect. Here, bacteriophage T7 and its host, Escherichia coli. The laboratory we identified five growth inhibitors encoded by T7 bacteriophage. strain E. coli K-12 shares many essential genes with pathogenic High-throughput sequencing of genomic DNA of resistant bacterial species, such as E. coli O157:H7 and O104:H4, and therefore, mutants evolving against three of these inhibitors revealed unique growth inhibitors against it should prove effective against these mutations in three specific genes. We found that a nonessential host pathogens as well. E. coli has been studied extensively, and the gene, ppiB, is required for growth inhibition by one bacteriophage putative functions or tentative physiological roles of over half of pcnB inhibitor and another nonessential gene, , is required for its 4,453 genes have been identified.
[Show full text]
Roles of Xbp1s in Transcriptional Regulation of Target Genes
biomedicines Review Roles of XBP1s in Transcriptional Regulation of Target Genes Sung-Min Park , Tae-Il Kang and Jae-Seon So * Department of Medical Biotechnology, Dongguk University, Gyeongju 38066, Gyeongbuk, Korea; [email protected] (S.-M.P.); [email protected] (T.-I.K.) * Correspondence: [email protected] Abstract: The spliced form of X-box binding protein 1 (XBP1s) is an active transcription factor that plays a vital role in the unfolded protein response (UPR). Under endoplasmic reticulum (ER) stress, unspliced Xbp1 mRNA is cleaved by the activated stress sensor IRE1α and converted to the mature form encoding spliced XBP1 (XBP1s). Translated XBP1s migrates to the nucleus and regulates the transcriptional programs of UPR target genes encoding ER molecular chaperones, folding enzymes, and ER-associated protein degradation (ERAD) components to decrease ER stress. Moreover, studies have shown that XBP1s regulates the transcription of diverse genes that are involved in lipid and glucose metabolism and immune responses. Therefore, XBP1s has been considered an important therapeutic target in studying various diseases, including cancer, diabetes, and autoimmune and inﬂammatory diseases. XBP1s is involved in several unique mechanisms to regulate the transcription of different target genes by interacting with other proteins to modulate their activity. Although recent studies discovered numerous target genes of XBP1s via genome-wide analyses, how XBP1s regulates their transcription remains unclear. This review discusses the roles of XBP1s in target genes transcriptional regulation. More in-depth knowledge of XBP1s target genes and transcriptional regulatory mechanisms in the future will help develop new therapeutic targets for each disease. Citation: Park, S.-M.; Kang, T.-I.; Keywords: XBP1s; IRE1; ATF6; ER stress; unfolded protein response; UPR; RIDD So, J.-S.
[Show full text]
PDIA2 Rabbit Pab
Leader in Biomolecular Solutions for Life Science PDIA2 Rabbit pAb Catalog No.: A12789 Basic Information Background Catalog No. This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic A12789 reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, two catalytically Observed MW active thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention 58kDa sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming disulfide bonds through its thiol isomerase, oxidase, and Calculated MW reductase activity. 57kDa/58kDa Category Primary antibody Applications WB, IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 64714 Q13087 IF 1:50 - 1:200 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 326-525 of human PDIA2 (NP_006840.2). Synonyms PDIA2;PDA2;PDI;PDIP;PDIR Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using PDIA2 antibody (A12789) at 1:3000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 90s. Immunofluorescence analysis of NIH/3T3 cells using PDIA2 antibody (A12789) at dilution of 1:100.
[Show full text]
BMC Medical Genomics Biomed Central
BMC Medical Genomics BioMed Central Research article Open Access Identification and validation of suitable endogenous reference genes for gene expression studies in human peripheral blood Boryana S Stamova*1, Michelle Apperson1, Wynn L Walker1, Yingfang Tian1, Huichun Xu1, Peter Adamczy1, Xinhua Zhan1, Da-Zhi Liu, Bradley P Ander1, Isaac H Liao1, Jeffrey P Gregg2, Renee J Turner1, Glen Jickling1, Lisa Lit1 and Frank R Sharp1 Address: 1Department of Neurology and M.I.N.D. Institute, University of California at Davis Medical Center, Sacramento, CA 95817, USA and 2Department of Pathology, and M.I.N.D. Institute, University of California at Davis Medical Center, Sacramento, CA 95817, USA Email: Boryana S Stamova* - [email protected]; Michelle Apperson - [email protected]; Wynn L Walker - [email protected]; Yingfang Tian - [email protected]; Huichun Xu - [email protected]; Peter Adamczy - [email protected]; Xinhua Zhan - [email protected]; Da-Zhi Liu - [email protected]; Bradley P Ander - [email protected]; Isaac H Liao - [email protected]; Jeffrey P Gregg - [email protected]; Renee J Turner - [email protected]; Glen Jickling - [email protected]; Lisa Lit - [email protected]; Frank R Sharp - [email protected] * Corresponding author Published: 5 August 2009 Received: 12 January 2009 Accepted: 5 August 2009 BMC Medical Genomics 2009, 2:49 doi:10.1186/1755-8794-2-49 This article is available from: http://www.biomedcentral.com/1755-8794/2/49 © 2009 Stamova et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
[Show full text]
Protein Expression Changes Induced in a Malignant Melanoma Cell Line
Pisano et al. BMC Cancer (2016) 16:317 DOI 10.1186/s12885-016-2362-6 RESEARCH ARTICLE Open Access Protein expression changes induced in a malignant melanoma cell line by the curcumin analogue compound D6 Marina Pisano1, Antonio Palomba2,3, Alessandro Tanca2, Daniela Pagnozzi2, Sergio Uzzau2, Maria Filippa Addis2, Maria Antonietta Dettori1, Davide Fabbri1, Giuseppe Palmieri1 and Carla Rozzo1* Abstract Background: We have previously demonstrated that the hydroxylated biphenyl compound D6 (3E,3′E) -4,4′-(5,5′,6,6′-tetramethoxy-[1,1′-biphenyl]-3,3′-diyl)bis(but-3-en-2-one), a structural analogue of curcumin, exerts a strong antitumor activity on melanoma cells both in vitro and in vivo. Although the mechanism of action of D6 is yet to be clarified, this compound is thought to inhibit cancer cell growth by arresting the cell cycle in G2/M phase, and to induce apoptosis through the mitochondrial intrinsic pathway. To investigate the changes in protein expression induced by exposure of melanoma cells to D6, a differential proteomic study was carried out on D6-treated and untreated primary melanoma LB24Dagi cells. Methods: Proteins were fractionated by SDS-PAGE and subjected to in gel digestion. The peptide mixtures were analyzed by liquid chromatography coupled with tandem mass spectrometry. Proteins were identified and quantified using database search and spectral counting. Proteomic data were finally uploaded into the Ingenuity Pathway Analysis software to find significantly modulated networks and pathways. Results: Analysis of the differentially expressed protein profiles revealed the activation of a strong cellular stress response, with overexpression of several HSPs and stimulation of ubiquitin-proteasome pathways.
[Show full text]