Current Trends in Multiple Myeloma Customizing Treatment Strategies and Optimizing Outcomes
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Supplementary Information Changes in the Plasma Proteome At
Supplementary Information Changes in the plasma proteome at asymptomatic and symptomatic stages of autosomal dominant Alzheimer’s disease Julia Muenchhoff1, Anne Poljak1,2,3, Anbupalam Thalamuthu1, Veer B. Gupta4,5, Pratishtha Chatterjee4,5,6, Mark Raftery2, Colin L. Masters7, John C. Morris8,9,10, Randall J. Bateman8,9, Anne M. Fagan8,9, Ralph N. Martins4,5,6, Perminder S. Sachdev1,11,* Supplementary Figure S1. Ratios of proteins differentially abundant in asymptomatic carriers of PSEN1 and APP Dutch mutations. Mean ratios and standard deviations of plasma proteins from asymptomatic PSEN1 mutation carriers (PSEN1) and APP Dutch mutation carriers (APP) relative to reference masterpool as quantified by iTRAQ. Ratios that significantly differed are marked with asterisks (* p < 0.05; ** p < 0.01). C4A, complement C4-A; AZGP1, zinc-α-2-glycoprotein; HPX, hemopexin; PGLYPR2, N-acetylmuramoyl-L-alanine amidase isoform 2; α2AP, α-2-antiplasmin; APOL1, apolipoprotein L1; C1 inhibitor, plasma protease C1 inhibitor; ITIH2, inter-α-trypsin inhibitor heavy chain H2. 2 A) ADAD)CSF) ADAD)plasma) B) ADAD)CSF) ADAD)plasma) (Ringman)et)al)2015)) (current)study)) (Ringman)et)al)2015)) (current)study)) ATRN↓,%%AHSG↑% 32028% 49% %%%%%%%%HC2↑,%%ApoM↓% 24367% 31% 10083%% %%%%TBG↑,%%LUM↑% 24256% ApoC1↓↑% 16565% %%AMBP↑% 11738%%% SERPINA3↓↑% 24373% C6↓↑% ITIH2% 10574%% %%%%%%%CPN2↓%% ↓↑% %%%%%TTR↑% 11977% 10970% %SERPINF2↓↑% CFH↓% C5↑% CP↓↑% 16566% 11412%% 10127%% %%ITIH4↓↑% SerpinG1↓% 11967% %%ORM1↓↑% SerpinC1↓% 10612% %%%A1BG↑%%% %%%%FN1↓% 11461% %%%%ITIH1↑% C3↓↑% 11027% 19325% 10395%% %%%%%%HPR↓↑% HRG↓% %%% 13814%% 10338%% %%% %ApoA1 % %%%%%%%%%GSN↑% ↓↑ %%%%%%%%%%%%ApoD↓% 11385% C4BPA↓↑% 18976%% %%%%%%%%%%%%%%%%%ApoJ↓↑% 23266%%%% %%%%%%%%%%%%%%%%%%%%%%ApoA2↓↑% %%%%%%%%%%%%%%%%%%%%%%%%%%%%A2M↓↑% IGHM↑,%%GC↓↑,%%ApoB↓↑% 13769% % FGA↓↑,%%FGB↓↑,%%FGG↓↑% AFM↓↑,%%CFB↓↑,%% 19143%% ApoH↓↑,%%C4BPA↓↑% ApoA4↓↑%%% LOAD/MCI)plasma) LOAD/MCI)plasma) LOAD/MCI)plasma) LOAD/MCI)plasma) (Song)et)al)2014)) (Muenchhoff)et)al)2015)) (Song)et)al)2014)) (Muenchhoff)et)al)2015)) Supplementary Figure S2. -
Tests for the Evaluation of Preterm Labor and Premature Rupture of Membranes
Medical Coverage Policy Effective Date ............................................. 7/15/2021 Next Review Date ....................................... 7/15/2022 Coverage Policy Number .................................. 0099 Tests for the Evaluation of Preterm Labor and Premature Rupture of Membranes Table of Contents Related Coverage Resources Overview .............................................................. 1 Recurrent Pregnancy Loss: Diagnosis and Treatment Coverage Policy ................................................... 1 Ultrasound in Pregnancy (including 3D, 4D and 5D General Background ............................................ 2 Ultrasound) Medicare Coverage Determinations .................. 13 Coding/Billing Information .................................. 13 References ........................................................ 15 INSTRUCTIONS FOR USE The following Coverage Policy applies to health benefit plans administered by Cigna Companies. Certain Cigna Companies and/or lines of business only provide utilization review services to clients and do not make coverage determinations. References to standard benefit plan language and coverage determinations do not apply to those clients. Coverage Policies are intended to provide guidance in interpreting certain standard benefit plans administered by Cigna Companies. Please note, the terms of a customer’s particular benefit plan document [Group Service Agreement, Evidence of Coverage, Certificate of Coverage, Summary Plan Description (SPD) or similar plan document] may differ -
Pathological Conditions Involving Extracellular Hemoglobin
Pathological Conditions Involving Extracellular Hemoglobin: Molecular Mechanisms, Clinical Significance, and Novel Therapeutic Opportunities for alpha(1)-Microglobulin Gram, Magnus; Allhorn, Maria; Bülow, Leif; Hansson, Stefan; Ley, David; Olsson, Martin L; Schmidtchen, Artur; Åkerström, Bo Published in: Antioxidants & Redox Signaling DOI: 10.1089/ars.2011.4282 2012 Link to publication Citation for published version (APA): Gram, M., Allhorn, M., Bülow, L., Hansson, S., Ley, D., Olsson, M. L., Schmidtchen, A., & Åkerström, B. (2012). Pathological Conditions Involving Extracellular Hemoglobin: Molecular Mechanisms, Clinical Significance, and Novel Therapeutic Opportunities for alpha(1)-Microglobulin. Antioxidants & Redox Signaling, 17(5), 813-846. https://doi.org/10.1089/ars.2011.4282 Total number of authors: 8 General rights Unless other specific re-use rights are stated the following general rights apply: Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights. • Users may download and print one copy of any publication from the public portal for the purpose of private study or research. • You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal Read more about Creative commons licenses: https://creativecommons.org/licenses/ Take down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. -
An Evolutionary Perspective on Human Cross-Sensitivity to Tree Nut and Seed Allergens," Aliso: a Journal of Systematic and Evolutionary Botany: Vol
Aliso: A Journal of Systematic and Evolutionary Botany Volume 33 | Issue 2 Article 3 2015 An Evolutionary Perspective on Human Cross- sensitivity to Tree Nut and Seed Allergens Amanda E. Fisher Rancho Santa Ana Botanic Garden, Claremont, California, [email protected] Annalise M. Nawrocki Pomona College, Claremont, California, [email protected] Follow this and additional works at: http://scholarship.claremont.edu/aliso Part of the Botany Commons, Evolution Commons, and the Nutrition Commons Recommended Citation Fisher, Amanda E. and Nawrocki, Annalise M. (2015) "An Evolutionary Perspective on Human Cross-sensitivity to Tree Nut and Seed Allergens," Aliso: A Journal of Systematic and Evolutionary Botany: Vol. 33: Iss. 2, Article 3. Available at: http://scholarship.claremont.edu/aliso/vol33/iss2/3 Aliso, 33(2), pp. 91–110 ISSN 0065-6275 (print), 2327-2929 (online) AN EVOLUTIONARY PERSPECTIVE ON HUMAN CROSS-SENSITIVITY TO TREE NUT AND SEED ALLERGENS AMANDA E. FISHER1-3 AND ANNALISE M. NAWROCKI2 1Rancho Santa Ana Botanic Garden and Claremont Graduate University, 1500 North College Avenue, Claremont, California 91711 (Current affiliation: Department of Biological Sciences, California State University, Long Beach, 1250 Bellflower Boulevard, Long Beach, California 90840); 2Pomona College, 333 North College Way, Claremont, California 91711 (Current affiliation: Amgen Inc., [email protected]) 3Corresponding author ([email protected]) ABSTRACT Tree nut allergies are some of the most common and serious allergies in the United States. Patients who are sensitive to nuts or to seeds commonly called nuts are advised to avoid consuming a variety of different species, even though these may be distantly related in terms of their evolutionary history. -
Tissue Distribution of Human Α1 -Microglobulin
Tissue Distribution of Human α1-Microglobulin Kimiteru Takagi, … , Toshihiko Shimoda, Toshio Shikata J Clin Invest. 1979;63(2):318-325. https://doi.org/10.1172/JCI109305. Research Article Human α1-microglobulin was isolated from the urine of patients with tubular proteinuria, and its molecular weight was established by sodium dodecyl sulfate-polyacrylamide gel electrophoresis at 33,000 daltons. The carbohydrate content was 21.7%. Anti-α1-microglobulin serum was prepared and observed to react monospecifically in gel diffusion to purified α1-microglobulin, as well as to normal human serum and urine. Sera from the domestic chicken, mouse, rat, rabbit, dog, calf, cow, goat, sheep, and horse, however, did not react to anti-α1-microglobulin serum in immunodiffusion. The lymphocyte culture supernate was found to contain α1-microglobulin. Both thymus-derived(T)- and bone marrow- derived(B)-lymphocyte culture media clearly displayed a specific precipitin line against anti-α1-microglobulin serum when tested with the Ouchterlony immunodiffusion method. The tissue distribution of α1-microglobulin was studied under immunofluorescence, and a positive staining was recognized on the lymphocyte surface. Identical staining patterns were noted on both T and B lymphocytes, though B lymphocytes took a more intense stain. It would thus seem quite possible that lymphocytes are the primary source of α1-microglobulin and that this is filtered through the glomerular basement membrane and partly reabsorbed by the renal tubules. This, then, would suggest the possibility -
The Double-Edged Sword of Beta2-Microglobulin in Antibacterial Properties and Amyloid Fibril-Mediated Cytotoxicity
International Journal of Molecular Sciences Review The Double-Edged Sword of Beta2-Microglobulin in Antibacterial Properties and Amyloid Fibril-Mediated Cytotoxicity Shean-Jaw Chiou 1,2,*, Huey-Jiun Ko 1,2, Chi-Ching Hwang 1,2 and Yi-Ren Hong 1,2,3,4,* 1 Department of Biochemistry, Faculty of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung 807, Taiwan; [email protected] (H.-J.K.); [email protected] (C.-C.H.) 2 Department of Medical Research, Kaohsiung Medical University Hospital, Kaohsiung 807, Taiwan 3 Graduate Institute of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung 807, Taiwan 4 Department of Biological Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan * Correspondence: [email protected] (S.-J.C.); [email protected] (Y.-R.H.) Abstract: Beta2-microglobulin (B2M) a key component of major histocompatibility complex class I molecules, which aid cytotoxic T-lymphocyte (CTL) immune response. However, the majority of studies of B2M have focused only on amyloid fibrils in pathogenesis to the neglect of its role of antimicrobial activity. Indeed, B2M also plays an important role in innate defense and does not only function as an adjuvant for CTL response. A previous study discovered that human aggregated B2M binds the surface protein structure in Streptococci, and a similar study revealed that sB2M-9, derived from native B2M, functions as an antibacterial chemokine that binds Staphylococcus aureus. An investigation of sB2M-9 exhibiting an early lymphocyte recruitment in the human respiratory epithelium with bacterial challenge may uncover previously unrecognized aspects of B2M in the Citation: Chiou, S.-J.; Ko, H.-J.; body’s innate defense against Mycobactrium tuberculosis. -
Breakdown of Supersaturation Barrier Links Protein Folding to Amyloid Formation
ARTICLE https://doi.org/10.1038/s42003-020-01641-6 OPEN Breakdown of supersaturation barrier links protein folding to amyloid formation Masahiro Noji1,11, Tatsushi Samejima1, Keiichi Yamaguchi1,12, Masatomo So 1, Keisuke Yuzu2, Eri Chatani2, Yoko Akazawa-Ogawa3, Yoshihisa Hagihara3, Yasushi Kawata4, Kensuke Ikenaka5, Hideki Mochizuki5, ✉ József Kardos6, Daniel E. Otzen 7, Vittorio Bellotti 8,9, Johannes Buchner 10 & Yuji Goto 1,12 1234567890():,; The thermodynamic hypothesis of protein folding, known as the “Anfinsen’s dogma” states that the native structure of a protein represents a free energy minimum determined by the amino acid sequence. However, inconsistent with the Anfinsen’s dogma, globular proteins can misfold to form amyloid fibrils, which are ordered aggregates associated with diseases such as Alzheimer’s and Parkinson’s diseases. Here, we present a general concept for the link between folding and misfolding. We tested the accessibility of the amyloid state for various proteins upon heating and agitation. Many of them showed Anfinsen-like reversible unfolding upon heating, but formed amyloid fibrils upon agitation at high temperatures. We show that folding and amyloid formation are separated by the supersaturation barrier of a protein. Its breakdown is required to shift the protein to the amyloid pathway. Thus, the breakdown of supersaturation links the Anfinsen’s intramolecular folding universe and the intermolecular misfolding universe. 1 Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan. 2 Department of Chemistry, Graduate School of Science, Kobe University, Hyogo 657-8501, Japan. 3 National Institute of Advanced Industrial Science and Technology (AIST), 1-8-31 Midorigaoka, Ikeda, Osaka 563- 8577, Japan. -
(12) United States Patent (10) Patent No.: US 7,537,914 B1 Roux Et Al
USOO7537914B1 (12) United States Patent (10) Patent No.: US 7,537,914 B1 ROux et al. (45) Date of Patent: May 26, 2009 (54) NUCLEICACID AND ALLERGENIC (58) Field of Classification Search ................ 435/69.1, POLYPEPTIDESENCODED THEREBY IN 435/252.3,320.1; 530/350; 536/23.5 CASHEW NUTS (ANACARDIUM See application file for complete search history. OCCIDENTALE) (56) References Cited (75) Inventors: Kenneth Roux, Tallahassee, FL (US); U.S. PATENT DOCUMENTS Shridhar K. Sathe, Tallahassee, FL (US); Jason M. Robotham, Tallahassee, 6,362,399 B1* 3/2002 Kinney et al. ............... 800/312 FL (US); Suzanne S. Teuber, Davis, CA (US) OTHER PUBLICATIONS Wang etal, J Allergy Clin Immunol 110: 160-6, 2002.* (73) Assignee: Florida State University Research Chica et al. Curr Opin Biotechnol 16(4):378-84. Aug. 2005.* Foundation, Inc., Tallahassee, FL (US) Witkowski et al. Biochemistry 38(36): 11643-50, Sep. 7, 1999.* Stanley et al. Arch Biochem Biophys 342(2): 244-53, Jun. 1997.* (*) Notice: Subject to any disclaimer, the term of this patent is extended or adjusted under 35 * cited by examiner U.S.C. 154(b) by 323 days. Primary Examiner Phuong Huynh (74) Attorney, Agent, or Firm Allen, Dyer, Doppelt, (21) Appl. No.: 10/529,602 Milbrath & Gilchrist, PA. (22) PCT Filed: Nov. 4, 2003 (57) ABSTRACT (86). PCT No.: PCT/USO3F34960 The invention describes an isolated nucleic acid sequence S371 (c)(1), comprising the nucleotide sequence of SEQ ID NO:1 or a (2), (4) Date: Mar. 30, 2005 degenerate variant of SEQ ID NO:1. The nucleic acid sequence encodes an Ig-Ebinding immunogenic polypeptide (87) PCT Pub. -
Regina Qu'appelle Health Region Tests
Regina Qu'Appelle Health Region Tests Acetaminophen Haptoglobin Alpha-Feto Protein (AFP) HbA1C AGBM Hemoglobin Electrophoresis Albumin Hemosiderin (urine) Alkaline Phosphatase (ALP) Kleihauer-Betke Test Alpha-1 Antitrypsin Lactate Alanine Aminotransferase (ALT) Luteinizing Hormone (LH) Amylase Lipid Panel (Chol, Trig, HDL, LDL ) Anti-mitochondrial antibodies Lithium Anti-RNP Liver Panel (Bili, ALT, ALP) Anti-scleroderma-70 antibodies Magnesium Anti-smooth muscle antibodies Malaria Blood Smear APTT - fresh specimen Methemalbumin Aspartate aminotransferase (AST) Microalbumin Bence Jones Protein (50-100mls 24 hour urine) Microalbumin/Creatinine Ratio Beta HCG Hypercoagulation Studies Direct Bilirubin Osmolality (Serum and Urine) Total Bilirubin Peripheral Smear review by pathologist CA-125 Phenobarbital Calcium Phenytoin (Dilantin) Carbamazepine (Tegretol) Phosphorus CBC Prolactin Carcinoembryonic Antigen (CEA) Prostate Specific Antigen (PSA) Cholinesterase w/ Dibucaine # Prothrombin Time Creatine kinase (CK) Protein Electrophoresis (PE, SPE) Creatinine (Serum and Urine) Protein Creatinine Clearance Renal Panel Cryoglobulin Reticulocyte Count Cyclosporin Sickle Cell Screen D-Dimer Sirolimus Digoxin (Lanoxin) Tacrolimus Electrolytes Theophylline Estradiol Thyroid Screen (TSH) Ferritin Tobramycin FSH Urea G-6-PD Uric Acid Gentamycin Valproic Acid (Epival, Depakene) G-Glutamyl Transferase (GGT) Vancomycin Glucose Viscosity Frozen Specimens Amikacin Factor Assays Lupus Anticoagulant Ammonia Fibrinogen Protein C Anticardiolipin Ab Heparin Assay Protein S Antiphospholipid Ab Hypercoagulation Screen Von Willebrand's Factor Anti-thrombin III H. Pylori Beta-2 Microglobulin Lactic Acid For more information refer to the RQHR Laboratory Services Manual or access the link below: RQHR Laboratory Specimen Requirements LABLisOP2002A3 RQHR Tests Laboratory Services, Regina Qu'Appelle Health Region 03/05/2016. -
Impact of High Pressure Processing on Immunoreactivity and Some Physico-Chemical Properties of Almond Milk THESIS Presented in P
Impact of High Pressure Processing on Immunoreactivity and Some Physico-chemical Properties of Almond Milk THESIS Presented in Partial Fulfillment of the Requirements for the Degree Master of Science in the Graduate School of The Ohio State University By Santosh Dhakal Graduate Program in Food Science and Technology The Ohio State University 2013 Master's Examination Committee: Professor V. M. Balasubramaniam, Advisor Professor Sheryl Barringer Professor Monica Giusti Copyrighted by Santosh Dhakal 2013 ABSTRACT Almond milk as a beverage has recently gained attention with increase in consumer awareness about health benefits of plant based beverages. The objective of this research was to investigate the influence of high pressure processing (HPP) on residual mmunoreactivity, protein solubility, and other selected quality attributes. Almond milk was prepared by disintegrating 10% almonds with water and were subjected to high pressure processing (HPP; 450 and 600 MPa at 30oC up to 600 s) and thermal processing (TP; 72, 85 and 99 oC, 0.1 MPa up to 600 s). After HPP (for all holding times), amandin, a key thermally resistant almond allergen, can no longer be detected by the anti-conformational epitopes MAb in ELISA while signal generated from the anti-linear epitopes MAb was reduced by half (P < 0.05). On the other hand, most TP samples did not show significant reductions in immunoreactivity (P > 0.05) unless processed at 85 and 99 °C for 300 s. Western blot (applicable for soluble proteins) and dot blot (applicable for soluble and insoluble proteins) also confirmed the loss of immunoreactivity by both antibodies for HPP almond milk. -
Gene Duplication and an Accelerated Evolutionary Rate in 11S Globulin Genes Are Associated with Higher Protein Synthesis in Dicots As Compared to Monocots
Gene duplication and an accelerated evolutionary rate in 11S globulin genes are associated with higher protein synthesis in dicots as compared to monocots Article Published Version Li, C., Li, M., Dunwell, J. and Zhang, Y.-M. (2012) Gene duplication and an accelerated evolutionary rate in 11S globulin genes are associated with higher protein synthesis in dicots as compared to monocots. BMC Evolutionary Biology, 12 (15). ISSN 1471-2148 doi: https://doi.org/10.1186/1471- 2148-12-15 Available at http://centaur.reading.ac.uk/26292/ It is advisable to refer to the publisher’s version if you intend to cite from the work. See Guidance on citing . To link to this article DOI: http://dx.doi.org/10.1186/1471-2148-12-15 Publisher: BioMed Central Ltd All outputs in CentAUR are protected by Intellectual Property Rights law, including copyright law. Copyright and IPR is retained by the creators or other copyright holders. Terms and conditions for use of this material are defined in the End User Agreement . www.reading.ac.uk/centaur CentAUR Central Archive at the University of Reading Reading’s research outputs online Li et al. BMC Evolutionary Biology 2012, 12:15 http://www.biomedcentral.com/1471-2148/12/15 RESEARCHARTICLE Open Access Gene duplication and an accelerated evolutionary rate in 11S globulin genes are associated with higher protein synthesis in dicots as compared to monocots Chun Li1,2†, Meng Li1†, Jim M Dunwell3 and Yuan-Ming Zhang1* Abstract Background: Seed storage proteins are a major source of dietary protein, and the content of such proteins determines both the quantity and quality of crop yield. -
Structural Characterization of Bacterial Defense Complex Marko Nedeljković
Structural characterization of bacterial defense complex Marko Nedeljković To cite this version: Marko Nedeljković. Structural characterization of bacterial defense complex. Biomolecules [q-bio.BM]. Université Grenoble Alpes, 2017. English. NNT : 2017GREAV067. tel-03085778 HAL Id: tel-03085778 https://tel.archives-ouvertes.fr/tel-03085778 Submitted on 22 Dec 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. THÈSE Pour obtenir le grade de DOCTEUR DE LA COMMUNAUTE UNIVERSITE GRENOBLE ALPES Spécialité : Biologie Structurale et Nanobiologie Arrêté ministériel : 25 mai 2016 Présentée par Marko NEDELJKOVIĆ Thèse dirigée par Andréa DESSEN préparée au sein du Laboratoire Institut de Biologie Structurale dans l'École Doctorale Chimie et Sciences du Vivant Caractérisation structurale d'un complexe de défense bactérienne Structural characterization of a bacterial defense complex Thèse soutenue publiquement le 21 décembre 2017, devant le jury composé de : Monsieur Herman VAN TILBEURGH Professeur, Université Paris Sud, Rapporteur Monsieur Laurent TERRADOT Directeur de Recherche, Institut de Biologie et Chimie des Protéines, Rapporteur Monsieur Patrice GOUET Professeur, Université Lyon 1, Président Madame Montserrat SOLER-LOPEZ Chargé de Recherche, European Synchrotron Radiation Facility, Examinateur Madame Andréa DESSEN Directeur de Recherche, Institut de Biologie Structurale , Directeur de These 2 Contents ABBREVIATIONS ..............................................................................................................................