Regina Qu'appelle Health Region Tests

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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.

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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.
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Human Plasma and Recombinant Hemopexins: Heme Binding Revisited
International Journal of Molecular Sciences Article Human Plasma and Recombinant Hemopexins: Heme Binding Revisited Elena Karnaukhova 1,*, Catherine Owczarek 2, Peter Schmidt 2, Dominik J. Schaer 3 and Paul W. Buehler 4,5,* 1 Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, USA 2 CSL Limited, Bio21 Institute, Parkville, Victoria 3010, Australia; [email protected] (C.O.); [email protected] (P.S.) 3 Division of Internal Medicine, University Hospital of Zurich, 8091 Zurich, Switzerland; [email protected] 4 Department of Pathology, The University of Maryland School of Medicine, Baltimore, MD 21201, USA 5 The Center for Blood Oxygen Transport and Hemostasis, Department of Pediatrics, The University of Maryland School of Medicine, Baltimore, MD 21201, USA * Correspondence: [email protected] (E.K.); [email protected] (P.W.B.) Abstract: Plasma hemopexin (HPX) is the key antioxidant protein of the endogenous clearance pathway that limits the deleterious effects of heme released from hemoglobin and myoglobin (the term “heme” is used in this article to denote both the ferrous and ferric forms). During intra-vascular hemolysis, heme partitioning to protein and lipid increases as the plasma concentration of HPX declines. Therefore, the development of HPX as a replacement therapy during high heme stress could be a relevant intervention for hemolytic disorders. A logical approach to enhance HPX yield involves recombinant production strategies from human cell lines. The present study focuses on a biophysical assessment of heme binding to recombinant human HPX (rhHPX) produced in the Expi293FTM (HEK293) cell system.
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MASSHEALTH TRANSMITTAL LETTER LAB-22 July 2002 TO
Commonwealth of Massachusetts Executive Office of Health and Human Services Division of Medical Assistance 600 Washington Street Boston, MA 02111 www.mass.gov/dma MASSHEALTH TRANSMITTAL LETTER LAB-22 July 2002 TO: Independent Clinical Laboratories Participating in MassHealth FROM: Wendy E. Warring, Commissioner RE: Independent Clinical Laboratory Manual (Laboratory HCPCS) The federal government has revised the HCFA Common Procedure Coding System (HCPCS) for MassHealth billing. This letter transmits changes for your provider manual that contain the new and revised codes. The revised Subchapter 6 is effective for dates of service on or after April 30, 2002. The codes introduced under the 2002 HCPCS code book are effective for dates of service on or after April 30, 2002. We will accept either the new or the old codes for dates of service through July 28, 2002. For dates of service on or after July 29, 2002, you must use the new codes to receive payment. If you wish to obtain a fee schedule, you may purchase Division of Health Care Finance and Policy regulations from either the Massachusetts State Bookstore or from the Division of Health Care Finance and Policy (see addresses and telephone numbers below). You must contact them first to find out the price of the publication. The Division of Health Care Finance and Policy also has the regulations available on disk. The regulation title for laboratory is 114.3 CMR 20.00: Laboratory. Massachusetts State Bookstore Division of Health Care Finance and Policy State House, Room 116 Two Boylston Street
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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
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Syllabus: Page 23
The University of Texas at El Paso College of Health Sciences Clinical Laboratory Science Program CLSC 3364 Hematology II Course Outline Spring What do you see? What is in your Head? Video or audio recordings will not be permitted. Instructor M. Lorraine Torres, Ed. D, MT (ASCP) College of Health Sciences Room 423 Phone: 747-7282 E-Mail: [email protected] Office Hours TR 3:00 – 4:00 p.m., Friday 2 – 3 p.m. or by appointment Class Schedule Monday and Wednesday 11:00 – 12:30 A.M. HSCI 135 Course Description This course is a sequel to Hematology I. It will include but is not limited to the study of the white blood cells with emphasis on white cell formation and function and the etiology and treatment of white blood cell disorders. This course will also encompass an introduction to hemostasis and laboratory determination of hemostatic disorders. Prerequisite; CLSC 3356 & CLSC 3257. Topical Outline 1. Maturation series and biology of white blood cells 2. Disorders of neutrophils 3. Reactive lymphocytes and Infectious Mononucleosis 4. Acute and chronic leukemias 5. Myelodysplastic syndromes 6. Myeloproliferative disorders 7. Multiple Myeloma and related plasma cell disorders 8. Lymphomas 9. Lipid (lysosomal) storage diseased and histiosytosis 10. Hemostatic mechanisms, platelet biology 11. Coagulation pathways 12. Quantitative and qualitative vascular and platelet disorders (congenital and acquired) 13. Disorders of plasma clotting factors 14. Interaction of the fibrinolytic, coagulation and kinin systems 15. Laboratory methods REQUIRED TEXTBOOKS: same books used for Hematology I Keohane, E.M., Smith, L.J. and Walenga, J.M. 2016. Rodak’s Hematology: Clinical Principles and applications.
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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.
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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
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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.
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Study of Plasma Glycoglobulin Hemochromogens
Proceedings of the National Academy of Sciences Vol. 68, No. 3, pp. 609-613, March 1971 Heme Binding and Transport-A Spectrophotometric Study of Plasma Glycoglobulin Hemochromogens DAVID L. DRABKIN Department of Biochemistry, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pa. 19104 Communicated by Britton Chance, December 16, 1970 ABSTRACT A hitherto unreported phenomenon is the content was only 0.004-0.007 mmol/liter (or 0.04-0.07% of immediate production of the spectrum of ferrohemo- the hemoglobin content of whole blood). At this concentration chromogens (in the presence of sodium dithionite) upon the addition in vitro of hydroxyhemin (pH 7.6-7.8) to the all of the hemoglobin present was probably in the form of plasmas or sera, as well as to certain Cohn plasma protein hemoglobin-haptoglobin (11). In most cases the serum was fractions, of all mammalian species thus far examined. used directly; in some it was found desirable to dilute the This distinctive reaction is characteristic of a coordination serum 1:1 with 0.2 M phosphate buffer, pH 7.6, prior to the complex with heme iron, and is ascribed to a remarkable affinity for heme of certain plasma glycoglobulins, which addition of heme and reductant. Plasma protein fractions IV-1, include hemopexin. Spectrophotometry has permitted IV4, IV-7, and VI of most of the above species [prepared by estimations of the specific heme-binding capacity (as the alcohol-low temperature technique (12-15) and obtained ferrohemochromogen) of the plasmas, the rate of removal mainly from the Nutritional Biochemical Corp. ] were also ex- from plasma of injected heme, and the production of bile amined.
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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.
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Methemalbumin. Ii. Effect of Pamaquine and Quinine on Pathways of Hemoglobin Metabolism
METHEMALBUMIN. II. EFFECT OF PAMAQUINE AND QUININE ON PATHWAYS OF HEMOGLOBIN METABOLISM William D. Blake J Clin Invest. 1948;27(3):144-150. https://doi.org/10.1172/JCI101954. Research Article Find the latest version: https://jci.me/101954/pdf METHEMALBUMIN. II. EFFECT OF PAMAQUINE AND QUININE ON PATHWAYS OF HEMOGLOBIN METABOLISM 1, 2 By WILLIAM D. BLAKE 8 (From the Department of Medicine, New York University College of Medicine, and the Research Service, Third [New York University] Medical Division, Goldwater Memorial Hospital, New York City) (Received for publication March 12, 1947) INTRODUCTION laria during the study but the period immediately fol- lowing malaria was avoided because of the questionable Methemalbuminemia has been described in as- status of certain functions of the liver (10, 11, 12). sociation with massive intravascular hemolysis Serunm bilirubin and bromsulfalein retention tests were (1, 2, 3, 4) or with limited hemolysis in the pres- normal, unless specifically mentioned. ence of liver disease (1, 5). Similarly, the in- Pamaquine naphthoate and quinine sulfate were admin- istered orally, the dosage in each case being expressed jection of large amounts of hemoglobin may result in terms of the free base. Plasma pamaquine (13) and in methemalbuminemia (1), whereas smaller quinine concentrations (14) were estimated at intervals amounts do so only in the presence of a damaged to ascertain reliability of drug intake. Pamaquine dosage liver (6). Hematin injected intravenously rapidly regimens were either 15 mg. every four hours or 10 mg. combines with serum albumin to form methemal- every eight hours. Quinine was given as the sulfate in 0.6 gram doses every eight hours.
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Dietary and Lifestyle Factors Modulate the Activity of the Endogenous
antioxidants Article Dietary and Lifestyle Factors Modulate the Activity of the Endogenous Antioxidant System in Patients with Age-Related Macular Degeneration: Correlations with Disease Severity Zofia Ula ńczyk 1 , Aleksandra Grabowicz 2, El˙zbietaCecerska-Heryć 3, Daria Sleboda-Taront´ 3, El˙zbietaKrytkowska 2, Katarzyna Mozolewska-Piotrowska 2, Krzysztof Safranow 4 , Miłosz Piotr Kawa 1, Barbara Doł˛egowska 3 and Anna Machali ńska 2,* 1 Department of General Pathology, Pomeranian Medical University, 70-111 Szczecin, Poland; zofi[email protected] (Z.U.); [email protected] (M.P.K.) 2 First Department of Ophthalmology, Pomeranian Medical University, 70-111 Szczecin, Poland; [email protected] (A.G.); [email protected] (E.K.); [email protected] (K.M.-P.) 3 Department of Laboratory Medicine, Pomeranian Medical University, 70-111 Szczecin, Poland; [email protected] (E.C.-H.); [email protected] (D.S.-T.);´ [email protected] (B.D.) 4 Department of Biochemistry and Medical Chemistry, Pomeranian Medical University, 70-111 Szczecin, Poland; [email protected] * Correspondence: [email protected] Received: 17 August 2020; Accepted: 2 October 2020; Published: 5 October 2020 Abstract: Age-related macular degeneration (AMD) is a common cause of blindness in the elderly population, but the pathogenesis of this disease remains largely unknown. Since oxidative stress is suggested to play a major role in AMD, we aimed to assess the activity levels of components of the antioxidant system in patients with AMD. We also investigated whether lifestyle and dietary factors modulate the activity of these endogenous antioxidants and clinical parameters of disease severity.
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