Proteomic Profiling for the Identification of Serum Diagnostic Biomarkers for Abdominal and Thoracic Aortic Aneurysms
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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. -
Normal Fibronectin Levels As a Function of Age in the Pediatric Population
Pediatr. Res. 17: 482-485 (1983) Normal Fibronectin Levels as a Function of Age in the Pediatric Population MICHAEL H. MCCAFFERTY,'~"MARTHA LEPOW, THOMAS M. SABA,'21' ESHIN CHO, HILAIRE MEUWISSEN, JOHN WHITE, AND SHARON F. ZUCKERBROD Departments of Physiology and Pediatrics, Albany Medical College of Union University, Albany, New York, USA Summary pediatric population with age has not been reported. This may be important in terms of appropriate interpretation of prevailing Fibronectin is an important non-immune opsonic protein influ- levels in children with various disease states, because normal encing phagocytic clearance of blood-borne nonbacterial particu- concentrations in children may be different from normal levels in lates which may arise in association with septic shock, tissue adults. This study was designed to measure fibronectin levels in a injury, and intravascular coagulation. In the present study, serum large group (n = 114) of normal children in order to define its fibronectin was measured by both electroimmunoassay as well as normal concentration as a function of age. rapid immunoturbidimetric assay in healthy children (n = 114) ranging in age from 1 month to 15 years in order to delineate the temporal alterations in fibronectin with age. Normal adult serum MATERIALS AND METHODS fibronectin concentrations are typically 220 pg/ml + 20 pg/ml. Serum concentration is 3540% lower than normal plasma con- Healthy children (n = 114) ranging in age from 1 month to 15 centration due to the binding of fibronectin to fibrin during clot years were seen as outpatients or as inpatients for minor surgical formation. Children between 1-12 months of age had significantly procedures. -
Mechanism of Interleukin-1- and Tumor Necrosis Factor Α-Dependent Regulation of the Α1-Antichymotrypsin Gene in Human Astrocyt
The Journal of Neuroscience, October 15, 2000, 20(20):7510–7516 Mechanism of Interleukin-1- and Tumor Necrosis Factor ␣- ␣ Dependent Regulation of the 1-Antichymotrypsin Gene in Human Astrocytes Tomasz Kordula,1 Marcin Bugno,1 Russell E. Rydel,2 and James Travis3 1Institute of Molecular Biology, Jagiellonian University, 31-120 Krako´ w, Poland, 2Elan Pharmaceuticals, South San Francisco, California 94080, and 3Department of Biochemistry and Molecular Biology, The University of Georgia, Athens, Georgia 30602 ␣ The expression of 1-antichymotrypsin (ACT) is significantly en- which bind nuclear factor kB (NF-kB) and one that binds activat- hanced in affected brain regions in Alzheimer’s disease. This ing protein 1 (AP-1). All of these elements contribute to the full serine proteinase inhibitor specifically colocalizes with filamen- responsiveness of the ACT gene to both cytokines, as deter- tous -amyloid deposits and recently has been shown to influ- mined by deletion and mutational analysis. The 5Ј NF-kB high- ence both formation and destabilization of -amyloid fibrils. In affinity binding site and AP-1 element contribute most to the the brain, ACT is expressed in astrocytes, and interleukin-1 (IL-1), enhancement of gene transcription in response to TNF and IL-1. tumor necrosis factor ␣ (TNF), oncostatin M (OSM), and IL-6/ In addition, we demonstrate that the 5Ј untranslated region of the soluble IL-6 receptor complexes control synthesis of this inhibi- ACT mRNA does not contribute to cytokine-mediated activation. tor. Here, we characterize a molecular mechanism responsible Finally, we find that overexpression of the NF-kB inhibitor (IkB) for both IL-1 and TNF-induced expression of ACT gene in astro- totally inhibits any activation mediated by the newly identified cytes. -
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 -
Neoplastic Transformation Inactivates Specific Trans-Acting Factor(S
Proc. Nati. Acad. Sci. USA Vol. 85, pp. 1744-1748, March 1988 Biochemistry Neoplastic transformation inactivates specific trans-acting factor(s) required for the expression of the thyroglobulin gene (differentiation/DNA-protein interaction/thyroglobufln) V. ENRICO AVVEDIMENTO*tt, ANNAMARIA MUSTI*, ALFREDO Fusco*, MARCO J. BONAPACE*, AND ROBERTO Di LAURO§¶ *Centro di Endocrinologia ed Oncologia Sperimentale del Consiglio Nazionale delle Ricerce, Dipartimento di Biologia e Patologia Molecolare, II Facolta di Medicina e Chirurgia, Universita di Napoli, Naples, Italy; and fLaboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 Communicated by Maxine F. Singer, October 5, 1987 (receivedfor review February 18, 1987) ABSTRACT The expression of rat thyroglobulin gene is sible for the block of the thyroglobulin expression in trans- repressed following the transformation ofrat thyroid cells with formed thyroid cells. Kirsten murine sarcoma virus. The expression of a reporter We report here data on the expression of the reporter gene gene fused to the thyroglobulin promoter is down-regulated in for chloramphenicol acetyl transferase fused to the Tg pro- transformed thyroid cells in transient or in stable transfection moter, designated Tg P-CAT gene, in transformed cells assays. DNase and exonuclease HI cleavage-protection analysis either in transient or in stable transfection assays. We show: reveals that a promoter binding activity located at -60 base (i) that this marker is down-regulated in transformed thyroid pairs from the transcription start site is substantially reduced cells; (ii) that a specific Tg promoter binding activity is in transformed thyroid cells. The repression in the trans- substantially reduced upon transformation; and (iii) that the formed cells of the reporter gene joined to the thyroglobulin Tg P-CAT gene in transformed cells can be reactivated by promoter can be reversed by fusion with normal differentiated fusion with a normal differentiated thyroid cell. -
Intradiscal Injection of an Autologous Alpha-2-Macroglobulin (A2M) Concentrate Alleviates Back Pain in FAC-Positive Patients
Orthopedics and Rheumatology Open Access Journal ISSN: 2471-6804 Research Article Ortho & Rheum Open Access Volume 4 Issue 2 - January 2017 Copyright © All rights are reserved by Pasquale X Montesano MD DOI: 10.19080/OROAJ.2017.04.555634 Intradiscal Injection of an Autologous Alpha-2- Macroglobulin (A2M) Concentrate Alleviates Back Pain in FAC-Positive Patients Pasquale X Montesano MD, *Jason M Cuellar MD, PhD, Gaetano J Scuderi MD 1Spine Surgeon, Montesano Spine and Sport, USA 2Spine surgeon, Department of Orthopaedic Surgery, Cedars-Sinai Medical Center, USA 3Spine surgeon, USA Submission: December 14, 2016; Published: January 03, 2017 *Corresponding author: Tel: ; Email: Jason M. Cuéllar MD, PhD, 450 N. Roxbury Drive, 3rd floor, Beverly Hills, CA 90210, Abstract Objectives: A cartilage degradation product, the Fibronectin-Aggrecan complex (FAC), has been identified in patients with degenerative disc disease (DDD). Alpha-2-macroglobulin (A2M) can prevent the formation of the G3 domain of aggrecan, reducing the fibronectin-aggrecan G3 complex and therefore may be an efficacious treatment. The present study was designed to determine a.b. The ability of autologousFAC to predict concentrated the response A2M to tothis relieve biologic back therapy. pain in patients with LBP from DDD and Study design/setting: Prospective cohort Patients: Main Outcome 24 patients Measurements: with low back pain and MRI-concordant DDD Oswestry disability index (ODI) and visual analog scores (VAS) were noted at baseline and at 3- and 6-month follow-up.Methods: Primary outcome of clinical improvement was defined as patients with both a decrease in VAS of at least 3 points and ODI >20 points. -
Development and Validation of a Protein-Based Risk Score for Cardiovascular Outcomes Among Patients with Stable Coronary Heart Disease
Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................ -
Glycosylated Fibronectin As a First-Trimester Biomarker for Prediction of Gestational Diabetes
Glycosylated Fibronectin as a First-Trimester Biomarker for Prediction of Gestational Diabetes Juha P. Rasanen, MD, PhD, Caryn K. Snyder, MPH, Paturi V. Rao, MD, PhD, Raluca Mihalache, MPHN, Seppo Heinonen, MD, PhD, Michael G. Gravett, MD, Charles T. Roberts Jr, PhD, and Srinivasa R. Nagalla, MD OBJECTIVE: To evaluate the potential clinical utility of and placental lactogen were significantly associated serum biomarkers for first-trimester prediction of gesta- (P,.001) with GDM. After adjustment for maternal fac- tional diabetes mellitus (GDM). tors and other biomarkers, glycosylated fibronectin dem- METHODS: Maternal serum concentrations of glycosy- onstrated an independent association with GDM , lated (Sambucus nigra lectin–reactive) fibronectin, adipo- (P .001). Adiponectin, high-sensitivity CRP, and placental nectin, sex hormone–binding globulin, placental lactogen, lactogen demonstrated modest classification perfor- and high-sensitivity C-reactive protein (CRP) were mea- mance compared with glycosylated fibronectin (respec- sured at 5–13 weeks of gestation in a case-control study of tively: area under the curve [AUC] 0.63; 95% confidence 90 pregnant women with subsequent development of interval [CI] 0.53–0.71; AUC 0.68; 95% CI 0.60–0.76; and GDM and in 92 control group participants. Ability to AUC 0.67, 95% CI 0.59–0.75; compared with AUC 0.91; detect GDM was assessed using logistic regression mod- 95% CI 0.87–0.96). Glycosylated fibronectin levels above eling and receiver operating characteristic (ROC) curves. a threshold of 120 mg/L correctly identified 57 GDM case Classification performance and positive and negative pre- group participants with a positive predictive value of dictive values were reported at specific thresholds. -
Alpha-1-Antitrypsin Phenotypes in Patients with Renal Arterial Fibromuscular Dysplasia
Journal of Human Hypertension (2000) 14, 91–94 2000 Macmillan Publishers Ltd All rights reserved 0950-9240/00 $15.00 www.nature.com/jhh ORIGINAL ARTICLE Alpha-1-antitrypsin phenotypes in patients with renal arterial fibromuscular dysplasia A Bofinger, C Hawley, P Fisher, N Daunt, M Stowasser and R Gordon Hypertension Unit, University of Queensland Department of Medicine, Greenslopes Private Hospital, Brisbane, Queensland, Australia ␣ Fibromuscular dysplasia (FMD) is a significant cause of one (1.2%) PiSZ), suggesting that 1-AT deficiency is renal artery stenosis, especially in young females. A not a common aetiological factor in renal arterial FMD. ␣ ␣ rare association between FMD and 1-antitrypsin ( 1- However, despite FMD being three times less common ␣ AT) deficiency has been reported. We compared the 1- in males than females, and carotid artery dissection AT phenotype distribution in 83 patients with renal being a rare occurrence, a male with PiMS deficiency arterial FMD with those published for Australian popu- phenotype presented with internal carotid artery dissec- ␣ lations. 1-AT phenotyping was performed by isoelectric tion and had bilateral renal artery FMD. Further, a patient focusing between pH 4.2 and pH 4.9 on polyacrylamide with PiSZ deficiency phenotype was one of two sisters gels with PiM1M2, PiFM (non-deficiency alleles), PiMS with FMD and was more severely affected than her PiMM and PiMZ (deficiency alleles) markers. Following pheno- normal phenotype sibling. These two patients from the ␣ typing, 1-AT genotyping was performed in 10 patients present series together with nine culled from the litera- ␣ to confirm the presence of S and/or Z alleles. -
Alterations in Seminal Plasma Proteomic Profile in Men with Primary and Secondary Infertility
www.nature.com/scientificreports OPEN Alterations in seminal plasma proteomic profle in men with primary and secondary infertility Ana D. Martins1,2, Manesh Kumar Panner Selvam1, Ashok Agarwal1 ✉ , Marco G. Alves2 & Saradha Baskaran1 Proteome of seminal plasma provides profound information related to the male reproductive health. This pilot study was conducted to characterize proteomic profle of seminal plasma from men with primary, or secondary infertility and compare it with proven fertile men. Study participants (n = 59) were recruited at the Cleveland Clinic and divided according to their fertility status: proven fertile (n = 39); primary infertility (n = 11) and secondary infertility (n = 9). Proteomic shotgun analysis revealed a total of 515 peptides common to primary infertility and control group; whereas 523 peptides were common to secondary infertility and control group. Bioinformatic analysis revealed dysregulation of biological processes such as cell secretion and vesicle mediated transport in primary infertility, whereas immune system response, regulation of proteolysis and iron homeostasis were dysregulated in secondary infertility. Western blot validation showed overexpression of ANXA2 and CDC42, and underexpression of SEMG2 proteins in primary infertility; and overexpression of ANXA2 and APP proteins in secondary infertility. This study elucidates the potential role of diferentially expressed proteins in the seminal plasma as diagnostic biomarker for primary and secondary infertility. Furthermore, our results suggest maturation failure and immune reaction response as the main cause of infertility in men with primary and secondary infertility, respectively. Additional validation of the proteins involved in the above pathways is warranted. Infertility globally afects 15% of couples and is now classifed as a disease of the reproductive system by the World Health Organization (WHO)1. -
(12) United States Patent (10) Patent No.: US 6,518,244 B2 Cardin Et Al
USOO651824.4B2 (12) United States Patent (10) Patent No.: US 6,518,244 B2 Cardin et al. (45) Date of Patent: Feb. 11, 2003 (54) COMBINATIONS OF HEPARIN COFACTOR OTHER PUBLICATIONS II AGONIST AND PLATELET IIB/IIIA Nicolini et al. Chem. Abst. 121:170,096 (1994).* ANTAGONIST, AND USES THEREOF Pavao et al., “A Unique Dermatan Sulfate-Like Glycosami noglycan from Ascidian,” J. Biol. Chem., (Dec. 29, 1995) (75) Inventors: Alan D. Cardin, Cincinnati, OH (US); 270(52):31027-31036. Cornelius L. Van Gorp, Springboro, Pouplard et al., “Antibodies to Platelet Factor 4-Heparin OH (US) After Cardiopulmonary Bypass in Patients Anticoagulated with Unfractionated Heparin or a Low Molecular Weight (73) Assignee: IntimaX Corporation, Cincinnati, OH Heparin:clinical Implications for Heparin-Induced Throm (US) bocytopenia.” Circulation (1999) 99:2539-2536. Prandoni et al., “Dermatan Sulfate: a Safe Approach to Notice: Subject to any disclaimer, the term of this Prevention of Postoperative Deep Vein Thrombosis,” Br. J. patent is extended or adjusted under 35 Surg. (1992) 79(6):505–509. U.S.C. 154(b) by 57 days. Adgey, “Bleeding Complications with New Antithrombotics Used in Ischemic Heart Disease,” Haemostasis (1996) 26(5):237-246. Agnelli et al., “A Randomized Double-Blind, Placebo-Con (21) Appl. No.: 09/802,775 trolled Trial of Dermatan Sulphate for Prevention of Deep (22) Filed: Mar. 9, 2001 Vein Thrombosis in Hip Fracture.” Thromb. Haemostas. (1992) 67:203-208. (65) Prior Publication Data Agnelli, “New Antithrombins and Nonheparin Glycosami noglycans in Clinical Development,” Vessels (1995) 1:9-16. US 2001/0036932 A1 Nov. 1, 2001 Ali et al., “Diffuse Alveolar Hemorrhage Following Admin istration of Tirofiban or Abciximab: a Nemesis of Platelet Related U.S. -
The Fibronectin ED-A Domain Enhances Recruitment of Latent TGF
© 2018. Published by The Company of Biologists Ltd | Journal of Cell Science (2018) 131, jcs201293. doi:10.1242/jcs.201293 RESEARCH ARTICLE The fibronectin ED-A domain enhances recruitment of latent TGF-β-binding protein-1 to the fibroblast matrix Franco Klingberg1,*, Grace Chau1,*, Marielle Walraven1, Stellar Boo1, Anne Koehler1, Melissa L. Chow1, Abby L. Olsen2, Michelle Im1, Monika Lodyga1, Rebecca G. Wells2, Eric S. White3 and Boris Hinz1,‡ ABSTRACT activation from a variety of different precursor cells: (1) the Dysregulated secretion and extracellular activation of TGF-β1 presence of a mechanically resistant ECM (Arora et al., 1999; Li β ̀ stimulates myofibroblasts to accumulate disordered and stiff et al., 2017), (2) biologically active TGF- 1(Desmouliere et al., extracellular matrix (ECM) leading to fibrosis. Fibronectin 1993) and (3) extradomain-A (ED-A)-containing fibronectin (FN; immobilizes latent TGF-β-binding protein-1 (LTBP-1) and thus also known as FN1) (hereafter denoted ED-A FN) (Serini et al., β stores TGF-β1 in the ECM. Because the ED-A fibronectin splice 1998). However, it is still unclear how TGF- 1 and mechanical stress variant is prominently expressed during fibrosis and supports collaborate with ED-A FN to promote myofibroblast activation. myofibroblast activation, we investigated whether ED-A promotes Fibroblasts cultured from different organs and species have been β LTBP-1–fibronectin interactions. Using stiffness-tuneable substrates shown to activate latent TGF- 1 from stores in the ECM by a for human dermal fibroblast cultures, we showed that high ECM process that requires cell contraction and a sufficiently stressed stiffness promotes expression and colocalization of LTBP-1 and ED- ECM (Hinz, 2015; Sarrazy et al., 2014; Wipff et al., 2007).