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Nephrology Clinical Laboratory Research Compendium

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Nephrology Clinical Laboratory Research Compendium Nephrology Clinical Laboratory Research Compendium The Nephrology Clinical Laboratory at Cincinnati Children’s Hospital Medical Center has expanded its clinical testing menu to now offer testing on a research basis. The CAP and CLIA certified laboratory operates under Good Clinical Laboratory Practice principles to ensure testing can be used to support findings of clinical trials. CONTACT US Our state of the art laboratory offers a broad testing menu to support research and pharmaceutical projects. We have the capability to perform traditional For more information on research or ELISA’S, multiplexing using the MSD Meso discovery, luminex magnetic bead clinical testing, please contact us at: assays, nephelometry and clinical chemistry. Phone: 513-636-4530 [email protected] The Nephrology Clinical Laboratory Research Compendium offers clinical chemistry, therapeutic drug monitoring, immunology, complement quantitation, www.cincinnatichildrens.org function and activation, specialty proteins and testing for various forms of thrombotic microangiopathies. COMPLEMENT SPECIALTY TESTING Autoantibody Testing Complement Components • Factor H Autoantibody (Quantitative) • C3 Nephritic Factor • C1 inhibitor (quantitative) • Factor B Autoantibody • C1q • C2 Functional Testing • C3 • CH50 • C4 • Alternative Pathway Functional Assay • C5 • MBL Pathway Functional Assay • C6 • C1 inhibitor Functional Assay • C7 • C8 Complement Activation Fragments • C9 • Complement Bb • Factor B • Complement Ba • Factor H • C3a • Factor I • C3c • Properdin • C3d • C4 Binding Protein • C4a • MBL • C4d • iC3b • SC5b-9 SERUM PROTEINS (NEPHELOMETRY) • ADNase B • CDT (Carbohydrate • Prealbumin • β2-Microglobulin • Albumin Deficient Transferrin) • RBP (Retinol Binding Protein) • β2-Microglobulin urine • Albumin Urine • Ceruloplasmin • sTfR (Soluble Transferrin • β trace protein • ASO • Ferritin Receptor) • Ig/light chain, type kappa • Cystatin C • Fibrinogen • Transferrin (for %CDT • Ig/light chain, type lambda • Haptoglobin • Fibronectin calculation) • Ig/light chain, type kappa • High Sensitivity CRP • Hemopexin • Transferrin urine (CardioPhase® hsCRP) • Homocysteine • Transferrin urine • Ig/light chain, type lambda • α1-Antitrypsin • Lipoprotein(a) • α1-Acid glycoprotein urine • AT-III • Myoglobin • α1-Microglobulin urine • Plasminogen • α2-Macroglobulin TTP TDM IMMUNOLOGY • ADAMTS13 Activity • Eculizumab Level • PLA2R Autoantibody • IgM • COVID19 IgG Titer • ADAMTS13 Antibody • Cyclosporine Level (CsA C0) • IgG • IgM CSF • COVID19 IgG • ADAMTS13 Inhibitor • Cyclosporine Level (CsA C2) • IgG CSF • IgA • COVID19 IgA • Sirolimus Level • IgG urine • IgE • COVID19 IgM • Tacrolimus Level • IgG subclasses 1-4 • Rheumatoid factor • Mycophenolic Acid (MPAT) BIOMARKERS • Endothelin-1 • Glucose • Angiotensin 1-9 • Neutrophil Gelatinase-Associated • Microalbumin • Angiotensin I Lipocalin (NGAL) • Vascular Endothelial Growth Factor • Angiotensin II • Kidney Injury Molecule-1 (KIM-1) (VEGF) • Anigiopoitien I • Creatinine • Intracellular Adhesion Molecule 1 • Anigiopoitien I • Macrophage Chemoattractant (CD54) • Angiotensin converting enzyme-1 Protein-1 (MCP-1) • Vascular Cell Adhesion Molecule 1 (ACE 1) • Liver Fatty Acid Binding Protein (CD106) • Angiotensin converting enzyme-2 (LFABP) • Fibroblast Growth Factor 23 (FGF23) (ACE 2) • Transforming Growth Factor-beta 1 • Matrix Metalloproteinase 9 (MMP9) • ACE activity (TGFβ-1) • N-acetyl Glucosaminidase (NAG) • Von Willebrand Factor protein VFW • Uromodulin (Tamm-Horsfall protein) • Renin • Plasminogen activator inhibitor-1 (PAI-1) • Alpha-1 antitrypsin • Aldosterone • Tissue plasminogen activator (T-PA) • Alpha-1 acid glycoprotein • Adiponectin • Cytokeratin 18 (M65) (M30) (orosomucoid) • Interluekin 6 IL-6 • Human CD163 • Hepcidin-25 • Interluekin 18 IL-18 • Human anti-endothelial cell antibody • Troponin T • MCP1 AECA • Vitamin D binding protein • Matrix Metalloproteinase 7 (MMP7) • Adiponectin • Angiotensin 1-7 The above list is not a comprehensive list of biomarkers. Please contact us for special projects and specific testing needs. Call for sample processing and shipping instructions at 513-636-4530. 082020_BRV163497.
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  • Regulation of the Complement System by Pentraxins
    REVIEW published: 02 August 2019 doi: 10.3389/fimmu.2019.01750 Regulation of the Complement System by Pentraxins Karita Haapasalo 1 and Seppo Meri 1,2,3* 1 Department of Bacteriology and Immunology and Translational Immunology Research Program, University of Helsinki, Helsinki, Finland, 2 HUSLAB, Helsinki University Hospital, Helsinki, Finland, 3 Department of Biomedical Sciences, Humanitas University, Milan, Italy The functions of pentraxins, like C-reactive protein (CRP), serum amyloid protein P (SAP) and pentraxin-3 (PTX3), are to coordinate spatially and temporally targeted clearance of injured tissue components, to protect against infections and to regulate related inflammation together with the complement system. For this, pentraxins have a dual relationship with the complement system. Initially, after a focused binding to their targets, e.g., exposed phospholipids or cholesterol in the injured tissue area, or microbial components, the pentraxins activate complement by binding its first component C1q. However, the emerging inflammation needs to be limited to the target area. Therefore, pentraxins inhibit complement at the C3b stage to prevent excessive damage. The complement inhibitory functions of pentraxins are based on their ability to interact with complement inhibitors C4bp or factor H (FH). C4bp binds to SAP, while FH binds to Edited by: both CRP and PTX3. FH promotes opsonophagocytosis through inactivation of C3b to Barbara Bottazzi, Milan University, Italy iC3b, and inhibits AP activity thus preventing formation of the C5a anaphylatoxin and the Reviewed by: complement membrane attack complex (MAC). Monitoring CRP levels gives important Livija Deban, clinical information about the extent of tissue damage and severity of infections. CRP is a Prokarium, United Kingdom valuable marker for distinguishing bacterial infections from viral infections.
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    Factor H and Atypical Hemolytic Uremic Syndrome: Mutations in the C-Terminus Cause Structural Changes and Defective Recognition Functions Miha´ly Jo´zsi,* Stefan Heinen,* Andrea Hartmann,* Clemens W. Ostrowicz,* Steffi Ha¨lbich,* Heiko Richter,* Anja Kunert,* Christoph Licht,† Rebecca E. Saunders,‡ Stephen J. Perkins,‡ Peter F. Zipfel,*§ and Christine Skerka* *Department of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany; †Children’s Hospital of the University of Cologne, Pediatric Nephrology, Cologne, Germany; ‡Department of Biochemistry and Molecular Biology, Royal Free and University College Medical School, University College London, London, United Kingdom; and §Frierich Schiller University, Jena, Germany Atypical hemolytic uremic syndrome is a disease that is characterized by microangiopathic hemolytic anemia, thrombocyto- penia, and acute renal failure. Mutations in the complement regulator factor H are associated with the inherited form of the disease, and >60% of the mutations are located within the C terminus of factor H. The C-terminus of factor H, represented by short consensus repeat 19 (SCR19) and SCR20, harbors multiple functions; consequently, this study aimed to examine the functional effects of clinically reported mutations in these SCR. Mutant factor H proteins (W1157R, W1183L, V1197A, R1210C, R1215G, and P1226S) were recombinantly expressed and functionally characterized. All six mutant proteins showed severely reduced heparin, C3b, C3d, and endothelial cell binding. By peptide spot analyses, four linear regions that are involved in heparin, C3b, and C3d binding were localized in SCR19 and SCR20. A three-dimensional homology model of the two domains suggests that these four regions form a common binding site across both domains.
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  • Supplementary Figure 1. Estimation of the Percentage of Volume of Each Population of Extracellular Vesicles by Dynamic Light Scattering
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  • Complement As a Therapeutic Target in Systemic Autoimmune Diseases
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