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  1 / 1597 MEDLINE  
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[PMID]:29227597
[Au] Autor:Yatsenko TA; Rybachuk VM; Yusova OI; Kharchenko SM; Grinenko TV
[Ti] Título:Effect of fibrin degradation products on fibrinolytic process.
[So] Source:Ukr Biochem J;88(2):16-24, 2016 Mar-Apr.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Fibrin clot lysis by plasminogen/plasmin system results in fibrin degradation products formation with subsequent release into bloodstream. The fragments contain specific binding sites for fibrinolytic system components and can interact with them. In this study, we investigated the way in which fibrin fragments effect fibrinolytic process. We have shown that high molecular weight products of fibrin degradation and fibrin fragments of DDE-complex and DD, but not end product Е3, stimulate plasmin formation. Additionally, components of DDE-complex mixture of fragments Е1 and Е2 have potentiation ability. The intermediate fibrin fragments hmFDPs and DDE attenuate clot lysis by plasmin and hmFDPs protect plasmin from α2-antiplasmin inhibition but under further fragmentation to endpoint fibrin fragments loose this ability. The plasma inhibitors reduce fibrinolytic system activity generated by the degradation products. Thus, fibrin fragments formed during the clot lysis can bind and move out fibrinolytic system components from clot volume and in this way result in clot resistance to hydrolysis.
[Mh] Termos MeSH primário: Produtos de Degradação da Fibrina e do Fibrinogênio/isolamento & purificação
Fibrina/química
Fibrinolisina/química
Plasminogênio/química
Ativador de Plasminogênio Tecidual/química
alfa 2-Antiplasmina/química
[Mh] Termos MeSH secundário: Tampões (Química)
Cromatografia em Gel
Cromatografia por Troca Iônica
Ativação Enzimática
Produtos de Degradação da Fibrina e do Fibrinogênio/química
Fibrinólise/fisiologia
Seres Humanos
Cinética
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Buffers); 0 (Fibrin Fibrinogen Degradation Products); 0 (alpha-2-Antiplasmin); 9001-31-4 (Fibrin); 9001-91-6 (Plasminogen); EC 3.4.21.68 (PLAT protein, human); EC 3.4.21.68 (Tissue Plasminogen Activator); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.02.016


  2 / 1597 MEDLINE  
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[PMID]:28710283
[Au] Autor:Constantinescu P; Brown RA; Wyatt AR; Ranson M; Wilson MR
[Ti] Título:Amorphous protein aggregates stimulate plasminogen activation, leading to release of cytotoxic fragments that are clients for extracellular chaperones.
[So] Source:J Biol Chem;292(35):14425-14437, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The misfolding of proteins and their accumulation in extracellular tissue compartments as insoluble amyloid or amorphous protein aggregates are a hallmark feature of many debilitating protein deposition diseases such as Alzheimer's disease, prion diseases, and type II diabetes. The plasminogen activation system is best known as an extracellular fibrinolytic system but was previously reported to also be capable of degrading amyloid fibrils. Here we show that amorphous protein aggregates interact with tissue-type plasminogen activator and plasminogen, via an exposed lysine-dependent mechanism, to efficiently generate plasmin. The insoluble aggregate-bound plasmin is shielded from inhibition by α -antiplasmin and degrades amorphous protein aggregates to release smaller, soluble but relatively hydrophobic fragments of protein (plasmin-generated protein fragments (PGPFs)) that are cytotoxic. , both endothelial and microglial cells bound and internalized PGPFs before trafficking them to lysosomes. Clusterin and α -macroglobulin bound to PGPFs to significantly ameliorate their toxicity. On the basis of these findings, we hypothesize that, as part of the extracellular proteostasis system, the plasminogen activation system may work synergistically with extracellular chaperones to safely clear large and otherwise pathological protein aggregates from the body.
[Mh] Termos MeSH primário: Fibrinolisina/metabolismo
Microglia/efeitos dos fármacos
Fragmentos de Peptídeos/toxicidade
Ativadores de Plasminogênio/toxicidade
Agregados Proteicos
Ativador de Plasminogênio Tecidual/metabolismo
alfa 2-Antiplasmina/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Clusterina/química
Clusterina/metabolismo
Conalbumina/química
Conalbumina/metabolismo
Endotélio Vascular/efeitos dos fármacos
Endotélio Vascular/metabolismo
Endotélio Vascular/patologia
Endotélio Vascular/ultraestrutura
Fibrinolisina/antagonistas & inibidores
Fibrinolisina/química
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Camundongos
Microglia/metabolismo
Microglia/patologia
Microglia/ultraestrutura
Mutação
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Plasminogênio/química
Plasminogênio/metabolismo
Ativadores de Plasminogênio/química
Ativadores de Plasminogênio/genética
Ativadores de Plasminogênio/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solubilidade
Superóxido Dismutase-1/química
Superóxido Dismutase-1/genética
Superóxido Dismutase-1/metabolismo
Ativador de Plasminogênio Tecidual/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CLU protein, human); 0 (Clusterin); 0 (Peptide Fragments); 0 (Protein Aggregates); 0 (Recombinant Proteins); 0 (SERPINF2 protein, human); 0 (SOD1 protein, human); 0 (alpha-2-Antiplasmin); 1391-06-6 (Conalbumin); 9001-91-6 (Plasminogen); EC 1.15.1.1 (Superoxide Dismutase-1); EC 3.4.21.- (Plasminogen Activators); EC 3.4.21.68 (PLAT protein, human); EC 3.4.21.68 (Tissue Plasminogen Activator); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.786657


  3 / 1597 MEDLINE  
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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


  4 / 1597 MEDLINE  
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[PMID]:28028005
[Au] Autor:Singh S; Houng A; Reed GL
[Ad] Endereço:From Department of Medicine, University of Tennessee Health Science Center, Memphis.
[Ti] Título:Releasing the Brakes on the Fibrinolytic System in Pulmonary Emboli: Unique Effects of Plasminogen Activation and α2-Antiplasmin Inactivation.
[So] Source:Circulation;135(11):1011-1020, 2017 Mar 14.
[Is] ISSN:1524-4539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In patients with hemodynamically significant pulmonary embolism, physiological fibrinolysis fails to dissolve thrombi acutely and r-tPA (recombinant tissue-type plasminogen activator) therapy may be required, despite its bleeding risk. To examine potential mechanisms, we analyzed the expression of key fibrinolytic molecules in experimental pulmonary emboli, assessed the contribution of α2-antiplasmin to fibrinolytic failure, and compared the effects of plasminogen activation and α2-antiplasmin inactivation on experimental thrombus dissolution and bleeding. METHODS: Pulmonary embolism was induced by jugular vein infusion of I-fibrin or fluorescein isothiocyanate-fibrin labeled emboli in anesthetized mice. Thrombus site expression of key fibrinolytic molecules was determined by immunofluorescence staining. The effects of r-tPA and α2-antiplasmin inactivation on fibrinolysis and bleeding were examined in a humanized model of pulmonary embolism. RESULTS: The plasminogen activation and plasmin inhibition system assembled at the site of acute pulmonary emboli in vivo. Thrombus dissolution was markedly accelerated in mice with normal α2-antiplasmin levels treated with an α2-antiplasmin-inactivating antibody ( <0.0001). Dissolution of pulmonary emboli by α2-antiplasmin inactivation alone was comparable to 3 mg/kg r-tPA. Low-dose r-tPA alone did not dissolve emboli, but was synergistic with α2-antiplasmin inactivation, causing more embolus dissolution than clinical-dose r-tPA alone ( <0.001) or α2-antiplasmin inactivation alone ( <0.001). Despite greater thrombus dissolution, α2-antiplasmin inactivation alone, or in combination with low-dose r-tPA, did not lead to fibrinogen degradation, did not cause bleeding (versus controls), and caused less bleeding than clinical-dose r-tPA ( <0.001). CONCLUSIONS: Although the fibrinolytic system assembles at the site of pulmonary emboli, thrombus dissolution is halted by α2-antiplasmin. Inactivation of α2-antiplasmin was comparable to pharmacological r-tPA for dissolving thrombi. However, α2-antiplasmin inactivation showed a unique pattern of thrombus specificity, because unlike r-tPA, it did not degrade fibrinogen or enhance experimental bleeding. This suggests that modifying the activity of a key regulator of the fibrinolytic system, like α2-antiplasmin, may have unique therapeutic value in pulmonary embolism.
[Mh] Termos MeSH primário: Plasminogênio/metabolismo
Embolia Pulmonar/patologia
alfa 2-Antiplasmina/metabolismo
[Mh] Termos MeSH secundário: Animais
Antifibrinolíticos/uso terapêutico
Modelos Animais de Doenças
Feminino
Fibrinogênio/metabolismo
Fibrinólise
Hemoglobinas/análise
Hemorragia
Seres Humanos
Pulmão/metabolismo
Pulmão/patologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Microscopia de Fluorescência
Inibidor 1 de Ativador de Plasminogênio/metabolismo
Embolia Pulmonar/tratamento farmacológico
Embolia Pulmonar/metabolismo
Ativador de Plasminogênio Tecidual/uso terapêutico
alfa 2-Antiplasmina/deficiência
alfa 2-Antiplasmina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifibrinolytic Agents); 0 (Hemoglobins); 0 (Plasminogen Activator Inhibitor 1); 0 (alpha-2-Antiplasmin); 9001-32-5 (Fibrinogen); 9001-91-6 (Plasminogen); EC 3.4.21.68 (Tissue Plasminogen Activator)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1161/CIRCULATIONAHA.116.024421


  5 / 1597 MEDLINE  
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[PMID]:27472428
[Au] Autor:Reed GL; Houng AK; Singh S; Wang D
[Ad] Endereço:Department of Medicine, University of Tennessee Health Sciences Center, Memphis, Tennessee.
[Ti] Título:α2-Antiplasmin: New Insights and Opportunities for Ischemic Stroke.
[So] Source:Semin Thromb Hemost;43(2):191-199, 2017 Mar.
[Is] ISSN:1098-9064
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thrombotic vascular occlusion is the leading cause of ischemic stroke. High blood levels of α -antiplasmin (a2AP), an ultrafast, covalent inhibitor of plasmin, have been linked in humans to increased risk of ischemic stroke and failure of tissue plasminogen activator (tPA) therapy. Consistent with these observations, a2AP neutralizes the therapeutic benefit of tPA therapy in experimental stroke. In addition, a2AP has deleterious, dose-related effects on ischemic brain injury in the absence of therapy. Experimental therapeutic inactivation of a2AP markedly reduces microvascular thrombosis, ischemic brain injury, brain swelling, brain hemorrhage, and death after thromboembolic stroke. These data provide new insights into the critical importance of a2AP in the pathogenesis of ischemic brain injury and suggest that transiently inactivating a2AP may have therapeutic value in ischemic stroke.
[Mh] Termos MeSH primário: Acidente Vascular Cerebral/tratamento farmacológico
alfa 2-Antiplasmina/uso terapêutico
[Mh] Termos MeSH secundário: Seres Humanos
Acidente Vascular Cerebral/mortalidade
Acidente Vascular Cerebral/patologia
alfa 2-Antiplasmina/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (alpha-2-Antiplasmin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160730
[St] Status:MEDLINE
[do] DOI:10.1055/s-0036-1585077


  6 / 1597 MEDLINE  
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[PMID]:27861608
[Au] Autor:Zakrzewski M; Zakrzewska E; Kicinski P; Przybylska-Kuc S; Dybala A; Myslinski W; Pastryk J; Tomaszewski T; Mosiewicz J
[Ad] Endereço:Department of Internal Diseases, Medical University of Lublin, Lublin, Poland.
[Ti] Título:Evaluation of Fibrinolytic Inhibitors: Alpha-2-Antiplasmin and Plasminogen Activator Inhibitor 1 in Patients with Obstructive Sleep Apnoea.
[So] Source:PLoS One;11(11):e0166725, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Obstructive sleep apnoea (OSA) induces thrombophilia and reduces fibrinolysis. Alpha-2-antiplasmin (a-2-AP) and plasminogen activator inhibitor 1 (PAI-1) are major inhibitors of the fibrinolytic system. Increased concentrations of these factors are associated with a higher risk of cardiovascular diseases. The aim of this study was to assess plasma a-2-AP and PAI-1 in patients with OSA and evaluate correlations with the polysomnographic record and selected risk factors of cardiovascular diseases. The study group comprised 45 patients with OSA, and the control group consisted of 19 patients who did not meet the diagnostic criteria of OSA. Plasma a-2-AP and PAI-1 concentrations were assessed by enzyme-linked immunosorbent assay (ELISA). In the study group, the median value of plasma a-2-AP was higher than that of the control group (157.34 vs. 11.89 pg/ml, respectively, P<0.0001). A-2-AP concentration increased proportionally to the severity of OSA. The concentration of a-2-AP was positively correlated with the apnoea-hypopnoea index (AHI), apnoea index (AI), respiratory disturbances time (RDT), and desaturaion index (DI), and negatively correlated with mean and minimal oxygen saturation (SpO2 mean, SpO2 min, respectively). The median value of PAI-1 was higher in the study group than the control group (12.55 vs. 5.40 ng/ml, respectively, P = 0.006) and increased along with OSA severity. PAI-1 concentration was positively correlated with AHI, AI, RDT, DI, and body mass index (BMI) and negatively correlated with SpO2 mean and SpO2 min. Higher plasma concentrations of a-2-AP and PAI-1 in patients with OSA indicated that these patients had increased prothrombotic activity. OSA increases the risk of cardiovascular complications as it enhances prothrombotic activity.
[Mh] Termos MeSH primário: Inibidor 1 de Ativador de Plasminogênio/sangue
Apneia Obstrutiva do Sono/sangue
alfa 2-Antiplasmina
[Mh] Termos MeSH secundário: Adulto
Biomarcadores
Análise Química do Sangue
Coagulação Sanguínea
Gasometria
Estudos de Casos e Controles
Comorbidade
Feminino
Seres Humanos
Masculino
Meia-Idade
Fenótipo
Polissonografia
Fatores de Risco
Apneia Obstrutiva do Sono/diagnóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Plasminogen Activator Inhibitor 1); 0 (alpha-2-Antiplasmin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0166725


  7 / 1597 MEDLINE  
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[PMID]:27543913
[Au] Autor:Yamanaka A; Kimura F; Yoshida T; Kita N; Takahashi K; Kushima R; Murakmai T
[Ad] Endereço:Department of Obstetrics and Gynecology, Shiga University of Medical Science, Seta-Tsukinowa-cho, Otsu, Shiga 520-2192, Japan. Electronic address: ykiyoshi@belle.shiga-med.ac.jp.
[Ti] Título:Dysfunctional coagulation and fibrinolysis systems due to adenomyosis is a possible cause of thrombosis and menorrhagia.
[So] Source:Eur J Obstet Gynecol Reprod Biol;204:99-103, 2016 Sep.
[Is] ISSN:1872-7654
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To study the effects of adenomyosis on the coagulation and fibrinolysis system during menstruation and the relationship between dysfunction of the coagulation and fibrinolysis system and the symptoms and complications of adenomyosis. STUDY DESIGN: Concentrations of thrombin-antithrombin complex (TAT) and soluble fibrin (SF) as markers of coagulation, D-dimer (DD) as a marker of both coagulation and fibrinolysis, and plasmin-alpha 2-plasmin inhibitor complex (PIC) as a marker of fibrinolysis in the peripheral blood of eight patients with adenomyosis were measured daily from the first to fifth day of menstruation. Associations between levels of these markers during menstruation and patient characteristics, history of thrombotic disorder, and hemoglobin loss during menstruation were investigated. RESULTS: TAT, SF, DD and PIC increased in 5, 2, 3 and 1 of the 8 patients, respectively. TAT increased in 5 of the 6 patients with an adenomyotic uterus ≥100 cubic centimeters. Patients with elevated DD, SF and/or PIC were among patients with elevated TAT. DD was only increased in 3 patients with a past history of small cerebral infarction or pulmonary thromboembolism and/or hemoglobin loss >2.0g/dl during menstruation. SF was increased only in 2 patients with a past history of cerebral infarction or pulmonary thromboembolism. PIC increased in 1 of the 2 patients with hemoglobin loss >2.0g/dl during menstruation. CONCLUSION: Adenomyosis patients with a uterus volume ≥100 cubic centimeters are at risk of having an activated coagulation system. These patients, particularly those with elevated SF and DD, may be at risk of thrombotic disorders. Fibrinolysis is activated in a portion of patients with activated coagulation during menstruation. Activated fibrinolysis during menstruation may contribute to menorrhagia in patients with adenomyosis, as only patients with activated fibrinolysis suffered menorrhagia, even though patients with an adenomyotic uterus ≥100 cubic centimeters without activated fibrinolysis did not. These results suggest extensive adenomyosis confers a potential risk of infarction and thrombosis and exacerbates menorrhagia via activation of coagulation and fibrinolysis during menstruation.
[Mh] Termos MeSH primário: Adenomiose/sangue
Coagulação Sanguínea/fisiologia
Fibrinólise/fisiologia
Menorragia/sangue
Trombose/sangue
[Mh] Termos MeSH secundário: Adulto
Antitrombina III
Feminino
Fibrina/metabolismo
Produtos de Degradação da Fibrina e do Fibrinogênio/metabolismo
Fibrinolisina/metabolismo
Seres Humanos
Peptídeo Hidrolases/sangue
alfa 2-Antiplasmina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibrin Fibrinogen Degradation Products); 0 (alpha-2-Antiplasmin); 0 (antithrombin III-protease complex); 0 (fibrin fragment D); 0 (plasmin-plasmin inhibitor complex); 9000-94-6 (Antithrombin III); 9001-31-4 (Fibrin); EC 3.4.- (Peptide Hydrolases); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160821
[St] Status:MEDLINE


  8 / 1597 MEDLINE  
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[PMID]:27462668
[Au] Autor:Maderal A; Miteva M
[Ti] Título:SnapshotDx Quiz: April 2016.
[So] Source:J Invest Dermatol;136(4):e39, 2016 Apr.
[Is] ISSN:1523-1747
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Dermatologia/métodos
Escleroderma Sistêmico/diagnóstico
[Mh] Termos MeSH secundário: Animais
Dermatologia/educação
Seres Humanos
Camundongos
Camundongos Knockout
Reumatologia/métodos
Fator de Crescimento Transformador beta1/metabolismo
alfa 2-Antiplasmina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (TGFB1 protein, human); 0 (Transforming Growth Factor beta1); 0 (alpha-2-Antiplasmin)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160728
[St] Status:MEDLINE


  9 / 1597 MEDLINE  
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[PMID]:27363989
[Au] Autor:Thomas A; Biswas A; Dodt J; Philippou H; Hethershaw E; Ensikat HJ; Ivaskevicius V; Oldenburg J
[Ad] Endereço:Institute of Experimental Haematology and Transfusion Medicine, University Clinic Bonn, Bonn, Germany.
[Ti] Título:Coagulation Factor XIIIA Subunit Missense Mutations Affect Structure and Function at the Various Steps of Factor XIII Action.
[So] Source:Hum Mutat;37(10):1030-41, 2016 Oct.
[Is] ISSN:1098-1004
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inherited defects of coagulation Factor XIII (FXIII) can be categorized into severe and mild forms based on their genotype and phenotype. Heterozygous mutations occurring in F13A1 and F13B genes causing mild FXIII deficiency have been reported only in the last few years primarily because the mild FXIII deficiency patients are often asymptomatic unless exposed to some kind of a physical trauma. However, unlike mutations causing severe FXIII deficiency, many of these mutations have not been comprehensively characterized based on expression studies. In our current article, we have transiently expressed 16 previously reported missense mutations detected in the F13A1 gene of patients with mild FXIII deficiency and analyzed their respective expression phenotype. Complimentary to expression analysis, we have used in silico analysis to understand and explain some of the in vitro findings. The expression phenotype has been evaluated with a number of expression phenotype determining assays. We observe that the mutations influence different aspects of FXIII function and can be functionally categorized on the basis of their expression phenotype. We identified mutations which even in heterozygous form would have strong impact on the functional status of the protein (namely mutations p.Arg716Gly, p.Arg704Gln, p.Gln602Lys, p.Leu530Pro, p.His343Tyr, p.Pro290Arg, and p.Arg172Gln).
[Mh] Termos MeSH primário: Deficiência do Fator XIII/genética
Fator XIIIa/química
Fator XIIIa/metabolismo
Mutação de Sentido Incorreto
[Mh] Termos MeSH secundário: Sítios de Ligação
Células Cultivadas
Simulação por Computador
Fator XIIIa/genética
Fibrinogênio/metabolismo
Seres Humanos
Modelos Moleculares
Simulação de Acoplamento Molecular
Fenótipo
Ligação Proteica
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Trombina/metabolismo
alfa 2-Antiplasmina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 0 (alpha-2-Antiplasmin); 9001-32-5 (Fibrinogen); EC 2.3.2.13 (Factor XIIIa); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160702
[St] Status:MEDLINE
[do] DOI:10.1002/humu.23041


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[PMID]:27207415
[Au] Autor:Mitchell JL; Mutch NJ
[Ad] Endereço:Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK.
[Ti] Título:Novel aspects of platelet factor XIII function.
[So] Source:Thromb Res;141 Suppl 2:S17-21, 2016 May.
[Is] ISSN:1879-2472
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pools of factor XIII (FXIII) exist in the plasma and within the cytoplasm of hematopoietic cells, including platelets. The functions of the cellular form, FXIII-A, have been assumed to be intracellular in nature, as the protein lacks a signal sequence for its release. Mounting evidence now suggests that platelet FXIII-A modulates hemostasis by several different mechanisms. In this condensed review we discuss recent advances in our understanding of the novel intracellular and extracellular functions of platelet FXIII-A.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Fator XIII/metabolismo
[Mh] Termos MeSH secundário: Animais
Plaquetas/citologia
Fibrina/metabolismo
Fibrinólise
Seres Humanos
Ativação Plaquetária
alfa 2-Antiplasmina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (alpha-2-Antiplasmin); 9001-31-4 (Fibrin); 9013-56-3 (Factor XIII)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160522
[St] Status:MEDLINE



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