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[PMID]: 29054763 [Au] Autor: El-Fattah AAA; Sadik NAH; Sedrak H; Battah A; Nabil M [Ad] Endereço: Biochemistry department, Faculty of Pharmacy, Cairo University, Cairo, Egypt. [Ti] Título: Association of genetic variants of hemostatic genes with myocardial infarction in Egyptian patients. [So] Source: Gene;641:212-219, 2018 Jan 30. [Is] ISSN: 1879-0038 [Cp] País de publicação: Netherlands [La] Idioma: eng [Ab] Resumo: Hemostatic genes polymorphisms are well known to be associated with venous thrombosis, but their association with arterial thrombosis especially myocardial infarction (MI) remains to be clarified. We investigated the role of three hemostatic gene polymorphisms, prothrombin G20210A, factor XIII (FXIII) Val34Leu (G/T), and fibrinogen-ß-455G/A and their coexistence in Egyptian patients with MI. The possible correlation of these polymorphisms with plasma fibrinogen level was also evaluated. The study included 120 patients with MI and 60 healthy volunteers. Gene polymorphisms were tested using multiplex polymerase chain reaction and reverse-hybridization technique. Plasma fibrinogen level was determined by ELISA. Our study showed an increased risk of MI with fibrinogen ß-455G/A heterozygosity as well as FXIII Val34Leu homo and heterozygosity. In addition, the FXIII T allele (Leu34) and fibrinogen ß-455A allele were significantly associated with MI. Conversely, the prevalence of prothrombin mutation did not differ between patients with MI and controls. Combined carriers of FXIII Leu34 and fibrinogen-ß455A alleles were at higher risk of MI, whereas combined FXIII Val34Leu and prothrombin 20210A polymorphisms did not show increased risk for MI compared with controls. Plasma fibrinogen levels were significantly higher in patients with MI than controls. In MI patients, plasma fibrinogen levels were significantly higher in those with FXIII GT/TT or fibrinogen ß-455 GA, while were significantly lower in those with prothrombin 20210 GA compared with patients with wild type genotypes. In conclusion, our results suggest a possible thrombotic predisposition of FXIII Val34Leu, fibrinogen ß-455G/A polymorphisms and their coexistence for MI. These polymorphisms may add complexity to disease pathology by increasing plasma fibrinogen level. Extended studies are needed to confirm our results; nevertheless, these data may be implicated in genetic counseling and screening of high-risk individuals. [Mh] Termos MeSH primário: Fator XIII/genética Fibrinogênio/genética Hemostasia/genética Infarto do Miocárdio/genética Polimorfismo Genético/genética Protrombina/genética [Mh] Termos MeSH secundário: Alelos Estudos de Casos e Controles Egito Feminino Genótipo Heterozigoto Seres Humanos Masculino Meia-Idade Risco [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 9001-26-7 (Prothrombin); 9001-32-5 (Fibrinogen); 9013-56-3 (Factor XIII) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171128 [Lr] Data última revisão: 171128 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 171022 [St] Status: MEDLINE

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[PMID]: 28734018 [Au] Autor: Cushing MM; Fitzgerald MM; Harris RM; Asmis LM; Haas T [Ad] Endereço: Department of Pathology and Laboratory Medicine, Weill Cornell Medical College, New York, New York and. [Ti] Título: Influence of cryoprecipitate, Factor XIII, and fibrinogen concentrate on hyperfibrinolysis. [So] Source: Transfusion;57(10):2502-2510, 2017 Oct. [Is] ISSN: 1537-2995 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: BACKGROUND: Hyperfibrinolysis is a potentially life-threatening condition associated with poor clot integrity and excessive bleeding. Although antifibrinolytics are an effective treatment, more liberal use of these drugs may lead to a prothrombotic risk, and an earlier and potentially safer treatment option would be desirable. Hyperfibrinolysis has been shown to be attenuated by in vitro supplementation of purified human Factor (F)XIII concentrate. Cryoprecipitate represents an alternative source of FXIII and the only approved source of concentrated FXIII in some countries. The aim of this study was to investigate whether cryoprecipitate, FXIII, and fibrinogen concentrate mitigate hyperfibrinolysis. STUDY DESIGN AND METHODS: Ten citrate blood specimens from healthy subjects were spiked with tissue plasminogen activator (t-PA) and subsequently supplemented with cryoprecipitate, FXIII, fibrinogen concentrate, and É›-aminocaproic acid (EACA). Thromboelastometry tests were performed at baseline, after t-PA, and after supplementation. Hyperfibrinolysis was assessed using the clot lysis index at 60 minutes (LI60; reciprocal of maximum lysis). RESULTS: The LI60 was significantly improved (fibrinolysis attenuated) after cryoprecipitate supplementation compared to t-PA alone and compared to FXIII and fibrinogen concentrate. Hyperfibrinolysis was only fully reversed using EACA. In addition, cryoprecipitate demonstrated the least variability in the attenuation of hyperfibrinolysis among 10 healthy subjects, compared to FXIII and fibrinogen concentrate. CONCLUSION: This is the first study to show that cryoprecipitate is able to significantly mitigate hyperfibrinolysis in an in vitro model. Further investigations are warranted to determine whether cryoprecipitate may have a previously unrecognized benefit and should be administered earlier in resuscitation protocols. [Mh] Termos MeSH primário: Fator VIII/farmacologia Fibrinogênio/farmacologia Fibrinólise/efeitos dos fármacos [Mh] Termos MeSH secundário: Ácido Aminocaproico/farmacologia Coleta de Amostras Sanguíneas Fator VIII/uso terapêutico Fator XIII Fibrinogênio/uso terapêutico Seres Humanos Tromboelastografia Ativador de Plasminogênio Tecidual/farmacologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (cryoprecipitate coagulum); 9001-27-8 (Factor VIII); 9001-32-5 (Fibrinogen); 9013-56-3 (Factor XIII); EC 3.4.21.68 (PLAT protein, human); EC 3.4.21.68 (Tissue Plasminogen Activator); U6F3787206 (Aminocaproic Acid) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171023 [Lr] Data última revisão: 171023 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170723 [St] Status: MEDLINE [do] DOI: 10.1111/trf.14259

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[PMID]: 28707410 [Au] Autor: Rabik CA; Atkinson MA; Sule S; Strouse JJ [Ad] Endereço: Department of Pediatrics, Division of Pediatric Hematology. [Ti] Título: Treatment of an acquired Factor XIII inhibitor in an adolescent with systemic lupus erythematosus and renal failure. [So] Source: Transfusion;57(9):2159-2163, 2017 Sep. [Is] ISSN: 1537-2995 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: BACKGROUND: Factor (F)XIII deficiency is a rare inherited bleeding disorder, but can also be acquired due to the development of inhibitors. CASE REPORT: A 17-year-old female with systemic lupus erythematosus and end-stage kidney disease secondary to Class IV lupus nephritis developed spontaneous subcutaneous and muscular hematomas and delayed major bleeding after invasive procedures. She had abnormal kaolin thromboelastography (kTEG; decreased maximal amplitude, representative of clot strength) initially attributed to thrombocytopenia and uremic platelet dysfunction, but her FXIII activity was undetectable, and a high-titer antibody against FXIII was identified. She had improvement in clinical bleeding and in kaolin thromboelastogram result and transient improvement in FXIII activity after each dose of plasma-derived FXIII concentrate (Corifact) or cryoprecipitate. Her inhibitor titers gradually improved with multiple immunosuppressive therapies and plasma exchange. While her FXIII activity level remained mildly decreased, she has not had additional significant bleeding. CONCLUSION: Treatment with either plasma-derived FXIII or cryoprecipitate is an effective treatment to normalize the kTEG variables and clinical bleeding diatheses associated with acquired FXIII inhibitors. Higher doses may be needed in patients with high-titer inhibitor. [Mh] Termos MeSH primário: Autoanticorpos/imunologia Deficiência do Fator XIII/terapia Fator XIII/imunologia [Mh] Termos MeSH secundário: Adolescente Fator XIII/uso terapêutico Deficiência do Fator XIII/etiologia Deficiência do Fator XIII/imunologia Feminino Hematoma Hemorragia/prevenção & controle Seres Humanos Imunossupressores/uso terapêutico Falência Renal Crônica Lúpus Eritematoso Sistêmico Troca Plasmática [Pt] Tipo de publicação: CASE REPORTS [Nm] Nome de substância: 0 (Autoantibodies); 0 (Immunosuppressive Agents); 9013-56-3 (Factor XIII) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171027 [Lr] Data última revisão: 171027 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170715 [St] Status: MEDLINE [do] DOI: 10.1111/trf.14185

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[PMID]: 28653811 [Au] Autor: Horimizu R; Ogawa R; Watanabe Y; Tatsukawa H; Kinoshita M; Hashimoto H; Hitomi K [Ad] Endereço: Graduate School of Pharmaceutical Sciences, Nagoya University, Japan. [Ti] Título: Biochemical characterization of a medaka (Oryzias latipes) orthologue for mammalian Factor XIII and establishment of a gene-edited mutant. [So] Source: FEBS J;284(17):2843-2855, 2017 Sep. [Is] ISSN: 1742-4658 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: In the final process of blood coagulation, fibrin molecules are stabilized via a catalytic reaction by Factor XIIIA (FXIIIA), a member of the transglutaminase (TGase) family that catalyzes protein cross-linking reactions. In this study, we characterized the orthologue of this enzyme in medaka (Oryzias latipes), an established model fish in which a coagulation system is also preserved. The recombinant protein of this orthologue enzyme was produced in baculovirus-infected insect cells and used for analysis of its biochemical properties including activation by thrombin proteolysis and calcium dependence of the TGase enzymatic activity. Immunostaining and immunoblotting revealed that medaka FXIIIA is expressed in the kidney, bone, and esophagus in addition to blood cells. Furthermore, a gene-mutant fish was established using the CRISPR/Cas9 system. The loss of FXIIIA expression was validated in the mutants, and phenotypes, such as absence of fibrin cross-linking, were investigated in the established mutant fish. [Mh] Termos MeSH primário: Fator XIII/química Proteínas de Peixes/química [Mh] Termos MeSH secundário: Sequência de Aminoácidos Animais Sistemas CRISPR-Cas Sequência Conservada Fator XIII/genética Fator XIII/metabolismo Proteínas de Peixes/genética Proteínas de Peixes/metabolismo Expressão Gênica Estudos de Associação Genética Seres Humanos Mutação de Sentido Incorreto Especificidade de Órgãos Proteínas Recombinantes/química Proteínas Recombinantes/genética Proteínas Recombinantes/metabolismo Deleção de Sequência Células Sf9 Spodoptera [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Fish Proteins); 0 (Recombinant Proteins); 9013-56-3 (Factor XIII) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171030 [Lr] Data última revisão: 171030 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170628 [St] Status: MEDLINE [do] DOI: 10.1111/febs.14153

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[PMID]: 28596376 [Au] Autor: Beckers CML; Simpson KR; Griffin KJ; Brown JM; Cheah LT; Smith KA; Vacher J; Cordell PA; Kearney MT; Grant PJ; Pease RJ [Ad] Endereço: From the Leeds Institute for Cardiovascular and Metabolic Medicine, LIGHT Laboratories, University of Leeds, United Kingdom (C.M.L.B., K.R.S., K.J.G., J.M.B., L.T.C., K.A.S., P.A.C., M.T.K., P.J.G., R.J.P.); and Clinical Research Institute of Montreal, McGill University, Canada (J.V.). [Ti] Título: Cre/lox Studies Identify Resident Macrophages as the Major Source of Circulating Coagulation Factor XIII-A. [So] Source: Arterioscler Thromb Vasc Biol;37(8):1494-1502, 2017 Aug. [Is] ISSN: 1524-4636 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: OBJECTIVE: To establish the cellular source of plasma factor (F)XIII-A. APPROACH AND RESULTS: A novel mouse floxed for the gene, FXIII-A (Flox), was crossed with myeloid- and platelet-cre-expressing mice, and cellular FXIII-A mRNA expression and plasma and platelet FXIII-A levels were measured. The platelet factor 4-cre.Flox cross abolished platelet FXIII-A and reduced plasma FXIII-A to 23±3% ( <0.001). However, the effect of platelet factor 4-cre on plasma FXIII-A was exerted outside of the megakaryocyte lineage because plasma FXIII-A was not reduced in the Mpl mouse, despite marked thrombocytopenia. In support of this, platelet factor 4-cre depleted FXIII-A mRNA in brain, aorta, and heart of floxed mice, where FXIII-A cells were identified as macrophages as they costained with CD163. In the integrin αM-cre.Flox and the double copy lysozyme 2-cre.cre.Flox crosses, plasma FXIII-A was reduced to, respectively, 75±5% ( =0.003) and 30±7% ( <0.001), with no change in FXIII-A content per platelet, further consistent with a macrophage origin of plasma FXIII-A. The change in plasma FXIII-A levels across the various mouse genotypes mirrored the change in FXIII-A mRNA expression in aorta. Bone marrow transplantation of FXIII-A bone marrow into FXIII-A mice both restored plasma FXIII-A to normal levels and replaced aortic and cardiac FXIII-A mRNA, while its transplantation into FXIII-A mice did not increase plasma FXIII-A levels, suggesting that a limited population of niches exists that support FXIII-A-releasing cells. CONCLUSIONS: This work suggests that resident macrophages maintain plasma FXIII-A and exclude the platelet lineage as a major contributor. [Mh] Termos MeSH primário: Fator XIII/metabolismo Integrases/genética Macrófagos/metabolismo [Mh] Termos MeSH secundário: Animais Antígenos CD/sangue Antígenos de Diferenciação Mielomonocítica/sangue Plaquetas/metabolismo Transplante de Medula Óssea Antígeno CD11b/sangue Antígeno CD11b/genética Células Cultivadas Fator XIII/genética Feminino Regulação da Expressão Gênica Predisposição Genética para Doença Seres Humanos Integrases/metabolismo Macrófagos/transplante Masculino Camundongos da Linhagem 129 Camundongos Endogâmicos C57BL Camundongos Transgênicos Fenótipo Fator Plaquetário 4/sangue Fator Plaquetário 4/genética RNA Mensageiro/sangue RNA Mensageiro/genética Receptores de Superfície Celular/sangue Receptores de Trombopoetina/sangue Receptores de Trombopoetina/genética Trombocitopenia/sangue Trombocitopenia/genética Tirosina Quinase 3 Semelhante a fms/sangue Tirosina Quinase 3 Semelhante a fms/genética [Pt] Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antigens, CD); 0 (Antigens, Differentiation, Myelomonocytic); 0 (CD11b Antigen); 0 (CD163 antigen); 0 (Mpl protein, mouse); 0 (RNA, Messenger); 0 (Receptors, Cell Surface); 0 (Receptors, Thrombopoietin); 104641-95-4 (factor XIII subunit A); 37270-94-3 (Platelet Factor 4); 9013-56-3 (Factor XIII); EC 2.7.10.1 (fms-Like Tyrosine Kinase 3); EC 2.7.7.- (Cre recombinase); EC 2.7.7.- (Integrases) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170610 [St] Status: MEDLINE [do] DOI: 10.1161/ATVBAHA.117.309271

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[PMID]: 28580719 [Au] Autor: Nair PM; Pandya SG; Dallo SF; Reddoch KM; Montgomery RK; Pidcoke HF; Cap AP; Ramasubramanian AK [Ad] Endereço: Department of Biomedical Engineering, University of Texas at San Antonio, San Antonio, TX, USA. [Ti] Título: Platelets stored at 4°C contribute to superior clot properties compared to current standard-of-care through fibrin-crosslinking. [So] Source: Br J Haematol;178(1):119-129, 2017 Jul. [Is] ISSN: 1365-2141 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Currently, platelets for transfusion are stored at room temperature (RT) for 5-7 days with gentle agitation, but this is less than optimal because of loss of function and risk of bacterial contamination. We have previously demonstrated that cold (4°C) storage is an attractive alternative because it preserves platelet metabolic reserves, in vitro responses to agonists of activation, aggregation and physiological inhibitors, as well as adhesion to thrombogenic surfaces better than RT storage. Recently, the US Food and Drug Administration clarified that apheresis platelets stored at 4°C for up to 72 h may be used for treating active haemorrhage. In this work, we tested the hypothesis that cold-stored platelets contribute to generating clots with superior mechanical properties compared to RT-stored platelets. Rheological studies demonstrate that the clots formed from platelets stored at 4°C for 5 days are significantly stiffer (higher elastic modulus) and stronger (higher critical stress) than those formed from RT-stored platelets. Morphological analysis shows that clot fibres from cold-stored platelets were denser, thinner, straighter and with more branch points or crosslinks than those from RT-stored platelets. Our results also show that the enhanced clot strength and packed structure is due to cold-induced plasma factor XIII binding to platelet surfaces, and the consequent increase in crosslinking. [Mh] Termos MeSH primário: Plaquetas/fisiologia Preservação de Sangue/métodos Agregação Plaquetária/fisiologia [Mh] Termos MeSH secundário: Plaquetas/metabolismo Plaquetas/ultraestrutura Adesão Celular/fisiologia Fator XIII/metabolismo Fibrina/metabolismo Hemorreologia/fisiologia Seres Humanos Microscopia Eletrônica de Varredura/métodos Refrigeração Temperatura Ambiente Trombina/biossíntese [Pt] Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE [Nm] Nome de substância: 9001-31-4 (Fibrin); 9013-56-3 (Factor XIII); EC 3.4.21.5 (Thrombin) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170906 [Lr] Data última revisão: 170906 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170606 [St] Status: MEDLINE [do] DOI: 10.1111/bjh.14751

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[PMID]: 28516512 [Au] Autor: Mitchell JL; Wright S; Kazi S; Watson HG; Mutch NJ [Ad] Endereço: Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK. [Ti] Título: Defective α antiplasmin cross-linking and thrombus stability in a case of acquired factor XIII deficiency. [So] Source: Br J Haematol;178(5):794-799, 2017 Sep. [Is] ISSN: 1365-2141 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Acquired factor XIII (FXIII) deficiency is a rare and life-threatening condition that is often misdiagnosed or missed completely. A 72-year-old woman presented with symptoms of major unprovoked bleeding but routine coagulation screening tests and platelet count were normal. Low activated FXIII (FXIIIa) activity levels and abnormal urea clot stability led to diagnosis of acquired FXIII deficiency. A modified Bethesda inhibitor titre of 1.6 Bethesda units/ml indicated the presence of a FXIII inhibitor. Bleeding responded to a single dose of FXIII concentrate and immunosuppression with prednisolone induced remission. A subsequent relapse was treated with combined prednisolone and Rituximab resulting in a prolonged, ongoing remission. Here we analyse the mechanisms underlying this idiopathic case of acquired FXIII deficiency. Prospective analysis of patient plasma revealed minimal FXIIIa activity and antigen in presentation and relapse samples. Thrombi formed from these samples lysed rapidly and showed an absence of cross-linked α AP. Western blotting revealed the presence of FXIII-B, indicating only FXIII-A and FXIII-A B were affected. FXIII activity and antigen levels normalised on remission. Our data suggest the presence of inhibitor-induced clearance of FXIII from plasma. As a consequence, reduced thrombus stability was evident due to defective α AP cross-linking, thereby explaining symptoms of excessive bleeding. [Mh] Termos MeSH primário: Deficiência do Fator XIII/sangue Trombose/sangue alfa 2-Antiplasmina/deficiência [Mh] Termos MeSH secundário: Idoso Fator XIII/metabolismo Deficiência do Fator XIII/complicações Feminino Fibrinólise/fisiologia Hemorragia/sangue Hemorragia/etiologia Seres Humanos Trombose/etiologia alfa 2-Antiplasmina/metabolismo [Pt] Tipo de publicação: CASE REPORTS; JOURNAL ARTICLE [Nm] Nome de substância: 0 (alpha-2-Antiplasmin); 9013-56-3 (Factor XIII) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171002 [Lr] Data última revisão: 171002 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170519 [St] Status: MEDLINE [do] DOI: 10.1111/bjh.14759

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[PMID]: 28421433 [Au] Autor: Vasilyeva AD; Bychkova AV; Bugrova AE; Indeykina MI; Chikunova AP; Leonova VB; Kostanova EA; Biryukova MI; Konstantinova ML; Kononikhin AS; Nikolaev EN; Rosenfeld MA [Ad] Endereço: N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia. [Ti] Título: Modification of the catalytic subunit of plasma fibrin-stabilizing factor under induced oxidation. [So] Source: Dokl Biochem Biophys;472(1):40-43, 2017 Jan. [Is] ISSN: 1608-3091 [Cp] País de publicação: Russia (Federation) [La] Idioma: eng [Ab] Resumo: For the first time, by using mass-spectrometry method, the oxidation-mediated modification of the catalytic FXIII-A subunit of plasma fibrin-stabilizing factor, pFXIII, has been studied. The oxidative sites were identified to belong to all structural elements of the catalytic subunit: the ß-sandwich (Tyr104, Tyr117, and Cys153), the catalytic core domain (Met160, Trp165, Met266, Cys328, Asp352, Pro387, Arg409, Cys410, Tyr442, Met475, Met476, Tyr482, and Met500), the ß-barrel 1 (Met596), and the ß-barrel 2 (Met647, Pro676, Trp692, Cys696, and Met710), which correspond to 3.9%, 1.11%, 0.7%, and 3.2%, respectively, of oxidative modifications as compared to the detectable amounts of amino acid residues in each of the structural domains. Lack of information on some parts of the molecule may be associated with the spatial unavailability of residues, complicating analysis of the molecule. The absence of oxidative sites localized within crucial areas of the structural domains may be brought about by both the spatial inaccessibility of the oxidant to amino acid residues in the zymogen and the screening effect of the regulatory FXIII-B subunit. [Mh] Termos MeSH primário: Domínio Catalítico Fator XIII/química [Mh] Termos MeSH secundário: Fator XIII/metabolismo Seres Humanos Oxirredução Conformação Proteica Subunidades Proteicas/química Subunidades Proteicas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Protein Subunits); 9013-56-3 (Factor XIII) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 171019 [Lr] Data última revisão: 171019 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170420 [St] Status: MEDLINE [do] DOI: 10.1134/S160767291701015X

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[PMID]: 28406553 [Au] Autor: Jennings I; Kitchen S; Menegatti M; Palla R; Walker I; Makris M; Peyvandi F [Ad] Endereço: UK NEQAS (Blood Coagulation), Sheffield, UK. [Ti] Título: Detection of Factor XIII deficiency: data from multicentre exercises amongst UK NEQAS and PRO-RBDD project laboratories. [So] Source: Int J Lab Hematol;39(4):350-358, 2017 Aug. [Is] ISSN: 1751-553X [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: INTRODUCTION: FXIII deficiency is a rare bleeding disorders, and specific FXIII assays are recommended to detect this deficiency. We investigated the performance and accuracy of FXIII investigations in two exercises, comparing centres enrolled in the PRO-RBDD project (prospective data collection on patients with fibrinogen and Factor XIII deficiencies), and UK NEQAS BC centres. METHODS: Samples from a FXIII deficient subject and a normal donor were sent to participating centres, to investigate for FXIII deficiency, and interpret their results. Median, coefficient of variation and range were determined. RESULTS: Results were returned from 98 UK NEQAS BC and 28 PRO-RBDD centres. Up to 40% of UK NEQAS BC and 52% of PRO-RBDD centres reported clot solubility results - with diagnostic errors by two NEQAS BC centres (false negatives for the FXIII deficient sample) and one PRO-RBDD centre (false positive for the normal sample). Over 70% of UK NEQAS BC centres and PRO-RBDD centres performed FXIII assays. Median results were similar between the two groups, with the exception of sample 3 in survey 2 (5.5 vs. 14.0 µ/dl for UK NEQAS BC and PRO-RBDD centres respectively, P < 0.001). Diagnostic errors were made by 2 UK NEQAS BC centres. CONCLUSION: Approximately 70% of centres now employ FXIII assays, complying with international recommendations. However, solubility tests continue to be used. Our data show this can be successful, depending on the sensitivity of the method in use. Diagnostic errors are made by centres using both solubility screens and FXIII assays, and laboratories should ensure good quality assurance procedures to improve diagnostic accuracy. [Mh] Termos MeSH primário: Deficiência do Fator XIII/diagnóstico [Mh] Termos MeSH secundário: Coagulação Sanguínea Testes de Coagulação Sanguínea/métodos Testes de Coagulação Sanguínea/normas Serviços de Laboratório Clínico/normas Fator XIII Deficiência do Fator XIII/sangue Feminino Pesquisas sobre Serviços de Saúde Seres Humanos Laboratórios Masculino Garantia da Qualidade dos Cuidados de Saúde Reprodutibilidade dos Testes Reino Unido [Pt] Tipo de publicação: JOURNAL ARTICLE; MULTICENTER STUDY [Nm] Nome de substância: 9013-56-3 (Factor XIII) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171019 [Lr] Data última revisão: 171019 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170414 [St] Status: MEDLINE [do] DOI: 10.1111/ijlh.12633

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[PMID]: 28380473 [Au] Autor: Ogawa Y; Yanagisawa K; Souri M; Mihara M; Naito C; Takizawa M; Ishizaki T; Mitsui T; Handa H; Osaki T; Nojima Y; Ichinose A [Ad] Endereço: Department of Medicine and Clinical Science, Gunma University Graduate School of Medicine, Maebashi, Japan. [Ti] Título: Successful Management of a Patient with Autoimmune Hemorrhaphilia due to Anti-Factor XIII/13 Antibodies Complicated by Pulmonary Thromboembolism. [So] Source: Acta Haematol;137(3):141-147, 2017. [Is] ISSN: 1421-9662 [Cp] País de publicação: Switzerland [La] Idioma: eng [Ab] Resumo: Autoimmune hemophilia-like disease (hemorrhaphilia) due to anti-factor XIII (FXIII) antibodies (AH13) is a very rare, life-threatening bleeding disorder. A 77-year-old woman developed macrohematuria and a right renal pelvic hematoma. The coagulation times were not prolonged, but FXIII activity and antigen levels were severely and moderately reduced to 9 and 29% of normal values, respectively. Accordingly, the FXIII-specific activity turned out to be low. FXIII inhibitor and anti-FXIII-A subunit autoantibodies were detected by a 1:1 crossmixing test and immunoblot and immunochromatographic assays. She was therefore diagnosed with "definite AH13" and treated with plasma-derived FXIII concentrates to arrest the hemorrhage. In addition to a highly compressed inferior vena cava by a huge renal pelvic hematoma, deep vein thrombosis (DVT) and pulmonary thromboembolism (PE) were identified by systemic computed tomography. The patient was immediately started on anticoagulation therapy with low-dose heparin. Emboli disappeared quickly, probably because under-crosslinked thrombi caused by severe FXIII deficiency are vulnerable to fibrinolysis. After about 1.5 years, anti-FXIII-A subunit autoantibodies still remained despite the use of rituximab, steroid pulse therapy, oral prednisolone, and oral cyclophosphamide treatments. In conclusion, an extremely rare AH13 case complicated by DVT and PE was successfully managed by balancing anticoagulation therapy with hemostatic therapy. [Mh] Termos MeSH primário: Autoanticorpos/sangue Doenças Autoimunes/complicações Doenças Autoimunes/terapia Deficiência do Fator XIII/complicações Deficiência do Fator XIII/terapia Fator XIII/antagonistas & inibidores Fator XIII/imunologia Embolia Pulmonar/complicações [Mh] Termos MeSH secundário: Idoso Anticoagulantes/uso terapêutico Autoanticorpos/imunologia Doenças Autoimunes/imunologia Ciclofosfamida/uso terapêutico Fator XIII/uso terapêutico Deficiência do Fator XIII/imunologia Feminino Hematoma/complicações Hematoma/diagnóstico por imagem Heparina/uso terapêutico Seres Humanos Nefropatias/complicações Nefropatias/diagnóstico por imagem Rituximab/uso terapêutico Trombose Venosa/complicações [Pt] Tipo de publicação: CASE REPORTS; JOURNAL ARTICLE [Nm] Nome de substância: 0 (Anticoagulants); 0 (Autoantibodies); 4F4X42SYQ6 (Rituximab); 8N3DW7272P (Cyclophosphamide); 9005-49-6 (Heparin); 9013-56-3 (Factor XIII) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170724 [Lr] Data última revisão: 170724 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170406 [St] Status: MEDLINE [do] DOI: 10.1159/000455938

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