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An ER Stress/Defective Unfolded Protein Response Model Richard T
ORIGINAL RESEARCH Ethanol Induced Disordering of Pancreatic Acinar Cell Endoplasmic Reticulum: An ER Stress/Defective Unfolded Protein Response Model Richard T. Waldron,1,2 Hsin-Yuan Su,1 Honit Piplani,1 Joseph Capri,3 Whitaker Cohn,3 Julian P. Whitelegge,3 Kym F. Faull,3 Sugunadevi Sakkiah,1 Ravinder Abrol,1 Wei Yang,1 Bo Zhou,1 Michael R. Freeman,1,2 Stephen J. Pandol,1,2 and Aurelia Lugea1,2 1Department of Medicine, Cedars Sinai Medical Center, Los Angeles, California; 2Department of Medicine, or 3Psychiatry and Biobehavioral Sciences, University of California Los Angeles David Geffen School of Medicine, Los Angeles, California Pancreatic acinar cells Pancreatic acinar cells - no pathology - - Pathology - Ethanol feeding ER sXBP1 Pdi, Grp78… (adaptive UPR) aggregates Proper folding and secretion • disordered ER of proteins processed in the • impaired redox folding endoplasmic reticulum (ER) • ER protein aggregation • secretory defects SUMMARY METHODS: Wild-type and Xbp1þ/- mice were fed control and ethanol diets, then tissues were homogenized and fraction- Heavy alcohol consumption is associated with pancreas ated. ER proteins were labeled with a cysteine-reactive probe, damage, but light drinking shows the opposite effects, isotope-coded affinity tag to obtain a novel pancreatic redox ER reinforcing proteostasis through the unfolded protein proteome. Specific labeling of active serine hydrolases in ER with response orchestrated by X-box binding protein 1. Here, fluorophosphonate desthiobiotin also was characterized pro- ethanol-induced changes in endoplasmic reticulum protein teomically. Protein structural perturbation by redox changes redox and structure/function emerge from an unfolded was evaluated further in molecular dynamic simulations. protein response–deficient genetic model. -
Aspirin Intervention for the Reduction of Colorectal Cancer Risk (ASPIRED): a Study Protocol for a Randomized Controlled Trial David A
Drew et al. Trials (2017) 18:50 DOI 10.1186/s13063-016-1744-z STUDYPROTOCOL Open Access ASPirin Intervention for the REDuction of colorectal cancer risk (ASPIRED): a study protocol for a randomized controlled trial David A. Drew1,2, Samantha M. Chin1,2, Katherine K. Gilpin1,2, Melanie Parziale1,2, Emily Pond1,2, Madeline M. Schuck1,2, Kathleen Stewart2, Meaghan Flagg3, Crystal A. Rawlings3, Vadim Backman4, Peter J. Carolan2, Daniel C. Chung2, Francis P. Colizzo III2, Matthew Freedman5, Manish Gala1,2, John J. Garber2, Curtis Huttenhower6, Dmitriy Kedrin2, Hamed Khalili1,2, Douglas S. Kwon3, Sanford D. Markowitz8, Ginger L. Milne9, Norman S. Nishioka2, James M. Richter2, Hemant K. Roy10, Kyle Staller1,2, Molin Wang6,7,11 and Andrew T. Chan1,2,5,11,12* Abstract Background: Although aspirin is recommended for the prevention of colorectal cancer, the specific individuals for whom the benefits outweigh the risks are not clearly defined. Moreover, the precise mechanisms by which aspirin reduces the risk of cancer are unclear. We recently launched the ASPirin Intervention for the REDuction of colorectal cancer risk (ASPIRED) trial to address these uncertainties. Methods/design: ASPIRED is a prospective, double-blind, multidose, placebo-controlled, biomarker clinical trial of aspirin use in individuals previously diagnosed with colorectal adenoma. Individuals (n = 180) will be randomized in a 1:1:1 ratio to low-dose (81 mg/day) or standard-dose (325 mg/day) aspirin or placebo. At two study visits, participants will provide lifestyle, dietary and biometric data in addition to urine, saliva and blood specimens. Stool, grossly normal colorectal mucosal biopsies and cytology brushings will be collected during a flexible sigmoidoscopy without bowel preparation. -
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ID: 19-0149 8 6 Q Pang et al. PHO patients with soft tissue 8:6 736–744 giant tumor caused by HPGD mutation RESEARCH The first case of primary hypertrophic osteoarthropathy with soft tissue giant tumors caused by HPGD loss-of-function mutation Qianqian Pang1,2, Yuping Xu1,3, Xuan Qi1, Yan Jiang1, Ou Wang1, Mei Li1, Xiaoping Xing1, Ling Qin2 and Weibo Xia1 1Department of Endocrinology, Key Laboratory of Endocrinology, Ministry of Health, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences, Beijing, China 2Musculoskeletal Research Laboratory and Bone Quality and Health Assessment Centre, Department of Orthopedics & Traumatology, The Chinese University of Hong Kong, Hong Kong SAR, Hong Kong 3Department of Endocrinology, The First Affiliated Hospital of Shanxi Medicalniversity, U Taiyuan, Shanxi, China Correspondence should be addressed to L Qin or W Xia: [email protected] or [email protected] Abstract Background: Primary hypertrophic osteoarthropathy (PHO) is a rare genetic multi-organic Key Words disease characterized by digital clubbing, periostosis and pachydermia. Two genes, f primary hypertrophic HPGD and SLCO2A1, which encodes 15-hydroxyprostaglandin dehydrogenase (15-PGDH) osteoarthropathy and prostaglandin transporter (PGT), respectively, have been reported to be related to f PHO PHO. Deficiency of aforementioned two genes leads to failure of prostaglandin E2 (PGE2) f HPGD mutation degradation and thereby elevated levels of PGE2. PGE2 plays an important role in f soft tumor tumorigenesis. Studies revealed a tumor suppressor activity of 15-PGDH in tumors, such f COX2 selective inhibitor treatment as lung, bladder and breast cancers. However, to date, no HPGD-mutated PHO patients presenting concomitant tumor has been documented. -
Original Article PDIA3 Knockdown in Dendritic Cells Regulates IL-4 Dependent Mast Cell Degranulation
Int J Clin Exp Med 2019;12(7):8482-8491 www.ijcem.com /ISSN:1940-5901/IJCEM0089109 Original Article PDIA3 knockdown in dendritic cells regulates IL-4 dependent mast cell degranulation Liyuan Tao1,2, Yue Hu1,3, Bin Lv1,3, Lu Zhang1,3, Zhaomeng Zhuang1,3, Meng Li1,3 1Department of Gastroenterology, First Affiliated Hospital of Zhejiang Chinese Medical University, 54 Youdian Road, Hangzhou 310006, China; 2Department of Gastroenterology and Hepatology, Hangzhou Red Cross Hospital, 208 Huancheng Dong Road, Hangzhou 310003, China; 3Key Laboratory of Digestive Pathophysiology of Zhejiang Province, First Affiliated Hospital of Zhejiang Chinese Medical University, 54 Youdian Road, Hangzhou 310006, China Received November 28, 2018; Accepted March 13, 2019; Epub July 15, 2019; Published July 30, 2019 Abstract: Background: A previous study found that expression of protein disulfide isomerase A3 (PDIA3) in den- dritic cells (DCs) is a potential mediator of exaggerated intestinal mucosal immunity response in a rodent model of irritable bowel syndrome (IBS). Aim: The aim of this study was to explore the roles of PDIA3 in the interaction between DCs and mast cells (MCs) in the context of IBS. Methods: This study investigated the effects of shRNA- mediated knockdown of PDIA3 expression in a dendritic cell line and spleen lymphocyte co-cultures. Resultant co-culture supernatants were used to challenge MC. PDIA3 expression was assessed using q-PCR and Western blotting. Expression of surface markers was analyzed by flow cytometry. CD4+ and CD8+ T-cell proliferation were examined using Cell Trace CFSE kits. Cytokine production was determined by ELISA testing. MC viability was ascer- tained using CCK-8 production. -
New Drugs Are Not Enough‑Drug Repositioning in Oncology: an Update
INTERNATIONAL JOURNAL OF ONCOLOGY 56: 651-684, 2020 New drugs are not enough‑drug repositioning in oncology: An update ROMINA GABRIELA ARMANDO, DIEGO LUIS MENGUAL GÓMEZ and DANIEL EDUARDO GOMEZ Laboratory of Molecular Oncology, Science and Technology Department, National University of Quilmes, Bernal B1876, Argentina Received August 15, 2019; Accepted December 16, 2019 DOI: 10.3892/ijo.2020.4966 Abstract. Drug repositioning refers to the concept of discov- 17. Lithium ering novel clinical benefits of drugs that are already known 18. Metformin for use treating other diseases. The advantages of this are that 19. Niclosamide several important drug characteristics are already established 20. Nitroxoline (including efficacy, pharmacokinetics, pharmacodynamics and 21. Nonsteroidal anti‑inflammatory drugs toxicity), making the process of research for a putative drug 22. Phosphodiesterase-5 inhibitors quicker and less costly. Drug repositioning in oncology has 23. Pimozide received extensive focus. The present review summarizes the 24. Propranolol most prominent examples of drug repositioning for the treat- 25. Riluzole ment of cancer, taking into consideration their primary use, 26. Statins proposed anticancer mechanisms and current development 27. Thalidomide status. 28. Valproic acid 29. Verapamil 30. Zidovudine Contents 31. Concluding remarks 1. Introduction 2. Artesunate 1. Introduction 3. Auranofin 4. Benzimidazole derivatives In previous decades, a considerable amount of work has been 5. Chloroquine conducted in search of novel oncological therapies; however, 6. Chlorpromazine cancer remains one of the leading causes of death globally. 7. Clomipramine The creation of novel drugs requires large volumes of capital, 8. Desmopressin alongside extensive experimentation and testing, comprising 9. Digoxin the pioneer identification of identifiable targets and corrobora- 10. -
Inhibitor for Protein Disulfide‑Isomerase Family a Member 3
ONCOLOGY LETTERS 21: 28, 2021 Inhibitor for protein disulfide‑isomerase family A member 3 enhances the antiproliferative effect of inhibitor for mechanistic target of rapamycin in liver cancer: An in vitro study on combination treatment with everolimus and 16F16 YOHEI KANEYA1,2, HIDEYUKI TAKATA2, RYUICHI WADA1,3, SHOKO KURE1,3, KOUSUKE ISHINO1, MITSUHIRO KUDO1, RYOTA KONDO2, NOBUHIKO TANIAI4, RYUJI OHASHI1,3, HIROSHI YOSHIDA2 and ZENYA NAITO1,3 Departments of 1Integrated Diagnostic Pathology, and 2Gastrointestinal and Hepato‑Biliary‑Pancreatic Surgery, Nippon Medical School; 3Department of Diagnostic Pathology, Nippon Medical School Hospital, Tokyo 113‑8602; 4Department of Gastrointestinal and Hepato‑Biliary‑Pancreatic Surgery, Nippon Medical School Musashi Kosugi Hospital, Tokyo 211‑8533, Japan Received April 16, 2020; Accepted October 28, 2020 DOI: 10.3892/ol.2020.12289 Abstract. mTOR is involved in the proliferation of liver 90.2±10.8% by 16F16 but to 62.3±12.2% by combination treat‑ cancer. However, the clinical benefit of treatment with mTOR ment with Ev and 16F16. HuH‑6 cells were resistant to Ev, and inhibitors for liver cancer is controversial. Protein disulfide proliferation was reduced to 86.7±6.1% by Ev and 86.6±4.8% isomerase A member 3 (PDIA3) is a chaperone protein, and by 16F16. However, combination treatment suppressed prolif‑ it supports the assembly of mTOR complex 1 (mTORC1) and eration to 57.7±4.0%. Phosphorylation of S6K was reduced by stabilizes signaling. Inhibition of PDIA3 function by a small Ev in both Li‑7 and HuH‑6 cells. Phosphorylation of 4E‑BP1 molecule known as 16F16 may destabilize mTORC1 and was reduced by combination treatment in both Li‑7 and HuH‑6 enhance the effect of the mTOR inhibitor everolimus (Ev). -
Solarbio Catalogue with PRICES
CAS Name Grade Purity Biochemical Reagent Biochemical Reagent 75621-03-3 C8390-1 3-((3-Cholamidopropyl)dimethylammonium)-1-propanesulfonateCHAPS Ultra Pure Grade 1g 75621-03-3 C8390-5 3-((3-Cholamidopropyl)dimethylammonium)-1-propanesulfonateCHAPS 5g 57-09-0 C8440-25 Cetyl-trimethyl Ammonium Bromide CTAB High Pure Grade ≥99.0% 25g 57-09-0 C8440-100 Cetyl-trimethyl Ammonium Bromide CTAB High Pure Grade ≥99.0% 100g 57-09-0 C8440-500 Cetyl-trimethyl Ammonium Bromide CTAB High Pure Grade ≥99.0% 500g E1170-100 0.5M EDTA (PH8.0) 100ml E1170-500 0.5M EDTA (PH8.0) 500ml 6381-92-6 E8030-100 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 100g 6381-92-6 E8030-500 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 500g 6381-92-6 E8030-1000 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 1kg 6381-92-6 E8030-5000 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 5kg 60-00-4 E8040-100 Ethylenediaminetetraacetic acid EDTA Ultra Pure Grade ≥99.5% 100g 60-00-4 E8040-500 Ethylenediaminetetraacetic acid EDTA Ultra Pure Grade ≥99.5% 500g 60-00-4 E8040-1000 Ethylenediaminetetraacetic acid EDTA Ultra Pure Grade ≥99.5% 1kg 67-42-5 E8050-5 Ethylene glycol-bis(2-aminoethylether)-N,N,NEGTA′,N′-tetraacetic acid Ultra Pure Grade ≥97.0% 5g 67-42-5 E8050-10 Ethylene glycol-bis(2-aminoethylether)-N,N,NEGTA′,N′-tetraacetic acid Ultra Pure Grade ≥97.0% 10g 50-01-1 G8070-100 Guanidine Hydrochloride Guanidine HCl ≥98.0%(AT) 100g 50-01-1 G8070-500 Guanidine Hydrochloride Guanidine HCl ≥98.0%(AT) 500g 56-81-5 -
Taqman® Human and Rat Inflammation Arrays
TaqMan® Gene Signature Arrays TaqMan® Human and Rat Inflammation Arrays These arrays are part of a collection of TaqMan® Gene Signature Group Assays Human Gene Symbols Arrays that enable analysis of hundreds of TaqMan® Gene Channels 7 Expression Assays on a micro fluidic card with minimal effort. L-type calcium 5 CACNA1C, CACNA1D, CACNA2D1, CACNB2, CACNB4 Inflammation is the body’s response to infection, irritation Ligand gated 2 HTR3A, HTR3B or injury; characterized by redness, heat, swelling, pain and Enzymes and inhibitors 41 possible dysfunction of the organs involved. It can be defined Inhibitor 1 A2M Lipase 15 CES1, PLA2G1B, PLA2G2A, PLA2G5, as an innate immune response manifested by increased blood PLCB2–4, PLCD1, PLCG1, PLCG2, supply and vascular permeability. This allows fluid and white PLA2G7, PLA2G10, PLA2G4C, blood cells to leave the intravascular compartment and move PLA2G2D, PLCE1 Kinase 4 MAPK1, MAPK3, MAPK8, MAPK14 to the site of injury or infection. Nitric oxide synthase 1 NOS2A Phosphodiesterase 4 PDE4A–D Inflammation is associated with a wide range of disorders Prostaglandin metabolism 9 ALOX12, ALOX5, HPGD, LTA4H, including asthma, allergy, rheumatoid arthritis, gout, sepsis, LTC4S, PTGIS, PTGS1 (COX1), PTGS2 (COX2), TBXAS1 autoimmune disease, cardiovascular disease, diabetes, Protease 7 KLK3, CASP1, KLK1, KLK2, neurologic disease and cancer. Medications targeting KLKB1, KLK14, KLK15 inflammatory diseases include NSAIDS, corticosteroids, Factors 9 ANXA1, ANXA3, ANXA5, TNFSF5, H1-receptor antagonists and ß2-selective adrenergic drugs. IL13, KNG1, NFKB1, TNFSF13B, TNF Current treatments tend to have limited efficacy because Receptors 35 they target symptoms or impair the immune response. GPCR 18 ADRB1, ADRB2, BDKRB1, BDKRB2, CYSLTR1, HRH1–3, LTB4R, An increasing number of new drugs and protein therapies LTB4R2, MC2R (missing on rat are being developed. -
Protein Disulfide-Isomerase A3 Significantly Reduces Ischemia
Neurochemistry International 122 (2019) 19–30 Contents lists available at ScienceDirect Neurochemistry International journal homepage: www.elsevier.com/locate/neuint Protein disulfide-isomerase A3 significantly reduces ischemia-induced damage by reducing oxidative and endoplasmic reticulum stress T Dae Young Yooa,b,1, Su Bin Choc,1, Hyo Young Junga, Woosuk Kima, Kwon Young Leed, Jong Whi Kima, Seung Myung Moone,f, Moo-Ho Wong, Jung Hoon Choid, Yeo Sung Yoona, ∗ ∗∗ Dae Won Kimh, Soo Young Choic, , In Koo Hwanga, a Department of Anatomy and Cell Biology, College of Veterinary Medicine, Research Institute for Veterinary Science, Seoul National University, Seoul, 08826, South Korea b Department of Anatomy, College of Medicine, Soonchunhyang University, Cheonan, Chungcheongnam, 31151, South Korea c Department of Biomedical Sciences, Research Institute for Bioscience and Biotechnology, Hallym University, Chuncheon, 24252, South Korea d Department of Anatomy, College of Veterinary Medicine and Institute of Veterinary Science, Kangwon National University, Chuncheon, 24341, South Korea e Department of Neurosurgery, Dongtan Sacred Heart Hospital, College of Medicine, Hallym University, Hwaseong, 18450, South Korea f Research Institute for Complementary & Alternative Medicine, Hallym University, Chuncheon, 24253, South Korea g Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, 24341, South Korea h Department of Biochemistry and Molecular Biology, Research Institute of Oral Sciences, College of Dentistry, Gangneung-Wonju -
Human Induced Pluripotent Stem Cell–Derived Podocytes Mature Into Vascularized Glomeruli Upon Experimental Transplantation
BASIC RESEARCH www.jasn.org Human Induced Pluripotent Stem Cell–Derived Podocytes Mature into Vascularized Glomeruli upon Experimental Transplantation † Sazia Sharmin,* Atsuhiro Taguchi,* Yusuke Kaku,* Yasuhiro Yoshimura,* Tomoko Ohmori,* ‡ † ‡ Tetsushi Sakuma, Masashi Mukoyama, Takashi Yamamoto, Hidetake Kurihara,§ and | Ryuichi Nishinakamura* *Department of Kidney Development, Institute of Molecular Embryology and Genetics, and †Department of Nephrology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan; ‡Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Hiroshima, Japan; §Division of Anatomy, Juntendo University School of Medicine, Tokyo, Japan; and |Japan Science and Technology Agency, CREST, Kumamoto, Japan ABSTRACT Glomerular podocytes express proteins, such as nephrin, that constitute the slit diaphragm, thereby contributing to the filtration process in the kidney. Glomerular development has been analyzed mainly in mice, whereas analysis of human kidney development has been minimal because of limited access to embryonic kidneys. We previously reported the induction of three-dimensional primordial glomeruli from human induced pluripotent stem (iPS) cells. Here, using transcription activator–like effector nuclease-mediated homologous recombination, we generated human iPS cell lines that express green fluorescent protein (GFP) in the NPHS1 locus, which encodes nephrin, and we show that GFP expression facilitated accurate visualization of nephrin-positive podocyte formation in -
Orlistat, a Novel Potent Antitumor Agent for Ovarian Cancer: Proteomic Analysis of Ovarian Cancer Cells Treated with Orlistat
INTERNATIONAL JOURNAL OF ONCOLOGY 41: 523-532, 2012 Orlistat, a novel potent antitumor agent for ovarian cancer: proteomic analysis of ovarian cancer cells treated with Orlistat HUI-QIONG HUANG1*, JING TANG1*, SHENG-TAO ZHOU1, TAO YI1, HONG-LING PENG1, GUO-BO SHEN2, NA XIE2, KAI HUANG2, TAO YANG2, JIN-HUA WU2, CAN-HUA HUANG2, YU-QUAN WEI2 and XIA ZHAO1,2 1Gynecological Oncology of Biotherapy Laboratory, Department of Gynecology and Obstetrics, West China Second Hospital, Sichuan University, Chengdu, Sichuan; 2State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu, Sichuan, P.R. China Received February 9, 2012; Accepted March 19, 2012 DOI: 10.3892/ijo.2012.1465 Abstract. Orlistat is an orally administered anti-obesity drug larly PKM2. These changes confirmed our hypothesis that that has shown significant antitumor activity in a variety of Orlistat is a potential inhibitor of ovarian cancer and can be tumor cells. To identify the proteins involved in its antitumor used as a novel adjuvant antitumor agent. activity, we employed a proteomic approach to reveal protein expression changes in the human ovarian cancer cell line Introduction SKOV3, following Orlistat treatment. Protein expression profiles were analyzed by 2-dimensional polyacrylamide In the 1920s, the Nobel Prize winner Otto Warburg observed gel electrophoresis (2-DE) and protein identification was a marked increase in glycolysis and enhanced lactate produc- performed on a MALDI-Q-TOF MS/MS instrument. More tion in tumor cells even when maintained in conditions of high than 110 differentially expressed proteins were visualized oxygen tension (termed Warburg effect), leading to widespread by 2-DE and Coomassie brilliant blue staining. -
Monoamine Oxidase a Is Highly Expressed by the Human Corpus Luteum of Pregnancy
REPRODUCTIONRESEARCH Identification and characterization of an oocyte factor required for sperm decondensation in pig Jingyu Li*, Yanjun Huan1,*, Bingteng Xie, Jiaqiang Wang, Yanhua Zhao, Mingxia Jiao, Tianqing Huang, Qingran Kong and Zhonghua Liu Laboratory of Embryo Biotechnology, College of Life Science, Northeast Agricultural University, Harbin, Heilongjiang Province 150030, China and 1Shandong Academy of Agricultural Sciences, Dairy Cattle Research Center, Jinan, Shandong Province 250100, China Correspondence should be addressed to Z Liu; Email: [email protected] or to Q Kong; Email: [email protected] *(J Li and Y Huan contributed equally to this work) Abstract Mammalian oocytes possess factors to support fertilization and embryonic development, but knowledge on these oocyte-specific factors is limited. In the current study, we demonstrated that porcine oocytes with the first polar body collected at 33 h of in vitro maturation sustain IVF with higher sperm decondensation and pronuclear formation rates and support in vitro development with higher cleavage and blastocyst rates, compared with those collected at 42 h (P!0.05). Proteomic analysis performed to clarify the mechanisms underlying the differences in developmental competence between oocytes collected at 33 and 42 h led to the identification of 18 differentially expressed proteins, among which protein disulfide isomerase associated 3 (PDIA3) was selected for further study. Inhibition of maternal PDIA3 via antibody injection disrupted sperm decondensation; conversely, overexpression of PDIA3 in oocytes improved sperm decondensation. In addition, sperm decondensation failure in PDIA3 antibody-injected oocytes was rescued by dithiothreitol, a commonly used disulfide bond reducer. Our results collectively report that maternal PDIA3 plays a crucial role in sperm decondensation by reducing protamine disulfide bonds in porcine oocytes, supporting its utility as a potential tool for oocyte selection in assisted reproduction techniques.