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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 / 7334 MEDLINE  
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[PMID]:28791829
[Au] Autor:Mec-Slomska AE; Adamiec-Mroczek J; Kuzmicz E; Misiuk-Hojlo M
[Ad] Endereço:Provincial Hospital Center, Jelenia Góra, Poland.
[Ti] Título:Intravitreal ocriplasmin: A breakthrough in the treatment of vitreomacular traction?
[So] Source:Adv Clin Exp Med;26(3):527-531, 2017 May-Jun.
[Is] ISSN:1899-5276
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Vitreoretinal interface pathologies, such as vitreomacular traction syndrome, epiretinal membranes and macular holes are sight-threatening conditions and one of the important causes of vision defects and vision loss. To this date, vigilance with observation of how the vitreomacular traction resolves, or vitreoretinal surgery in more severe cases, were the only treatment options. Recent rapid progress in ophthalmology, especially in diagnostic and visualization techniques, provided better insight into the mechanisms taking place on the vitreoretinal surface, which enabled a more accurate selection of treatment options. Development of ophthalmic pharmacological procedures, such as treatment of vitreomacular traction syndrome with ocriplasmin, constitutes an innovative breakthrough in ophthalmology. The enzyme is a genetically engineered form of human plasmin, a component of blood coagulation cascade that has been envisioned for human therapy since 1950s. It has never been used for vitreolysis in ophthalmology before. The aim of this review is to analyze and compare therapeutic options for symptomatic vitreomacular adhesion and vitreoretinal traction, with particular emphasis on microplasmin. We reviewed the results of recent studies comparing ocriplasmin to other widespread treatment options, such as pars plana vitrectomy.
[Mh] Termos MeSH primário: Fibrinolisina/uso terapêutico
Fragmentos de Peptídeos/uso terapêutico
Doenças Retinianas/tratamento farmacológico
Perfurações Retinianas/tratamento farmacológico
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Aderências Teciduais/tratamento farmacológico
Tração/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Peptide Fragments); 7V6HE3DM5A (microplasmin); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.17219/acem/62122


  3 / 7334 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


  4 / 7334 MEDLINE  
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[PMID]:28700732
[Au] Autor:Zhao XJ; Larkin TM; Lauver MA; Ahmad S; Ducruet AF
[Ad] Endereço:Department of Neurological Surgery, University of Pittsburgh, Pittsburgh, PA, United States of America.
[Ti] Título:Tissue plasminogen activator mediates deleterious complement cascade activation in stroke.
[So] Source:PLoS One;12(7):e0180822, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The use of intravenous tissue plasminogen activator (tPA) in the treatment of ischemic stroke is limited by its propensity to exacerbate brain edema and hemorrhage. The mechanisms underlying these deleterious effects of tPA remain incompletely understood. The purpose of this study was to delineate a pathway of tPA-mediated complement cascade activation in stroke and to determine whether complement inhibition ameliorates the adverse effects of post-ischemic tPA administration. We found that tPA promotes C3 cleavage both in vitro and in ischemic brain through a plasmin-mediated extrinsic pathway. Using cell culture models, we then showed that the C3a-receptor is strongly expressed on ischemic endothelium and that exogenous C3a dramatically enhances endothelial cell permeability. Next, we assessed the effect of tPA administration on brain edema and hemorrhage in a transient model of focal cerebral ischemia in C57BL/6 mice. We found that intravenous tPA exacerbates brain edema and hemorrhage in stroke, and that these effects are abrogated by a small-molecule antagonist of the C3a receptor. These findings establish for the first time that intravenous tPA dramatically upregulates complement cascade activation in ischemic brain and that pharmacologic complement inhibition protects against the adverse effects of tPA-mediated thrombolysis in stroke.
[Mh] Termos MeSH primário: Acidente Vascular Cerebral/metabolismo
Ativador de Plasminogênio Tecidual/farmacologia
[Mh] Termos MeSH secundário: Animais
Arginina/análogos & derivados
Arginina/farmacologia
Compostos Benzidrílicos/farmacologia
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Edema Encefálico/metabolismo
Morte Celular/efeitos dos fármacos
Células Cultivadas
Complemento C3/metabolismo
Células Endoteliais/efeitos dos fármacos
Células Endoteliais/metabolismo
Fibrinolisina/farmacologia
Hemoglobinas/metabolismo
Hemorragia/metabolismo
Seres Humanos
Imuno-Histoquímica
Infarto da Artéria Cerebral Média/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzhydryl Compounds); 0 (Complement C3); 0 (Hemoglobins); 0 (SB 290157); 94ZLA3W45F (Arginine); EC 3.4.21.68 (Tissue Plasminogen Activator); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180822


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[PMID]:28686706
[Au] Autor:Tashima Y; Banno F; Kita T; Matsuda Y; Yanamoto H; Miyata T
[Ad] Endereço:Department of Molecular Pathogenesis, National Cerebral and Cardiovascular Center, Suita, Osaka, Japan.
[Ti] Título:Plasminogen Tochigi mice exhibit phenotypes similar to wild-type mice under experimental thrombotic conditions.
[So] Source:PLoS One;12(7):e0180981, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plasminogen (Plg) is a precursor of plasmin that degrades fibrin. A race-specific A620T mutation in Plg, also known as Plg-Tochigi, originally identified in a patient with recurrent venous thromboembolism, causes dysplasminogenemia with reduced plasmin activity. The Plg-A620T mutation is present in 3-4% of individuals in East Asian populations, and as many as 50,000 Japanese are estimated to be homozygous for the mutant 620T allele. In the present study, to understand the changes of thrombotic phenotypes in individuals with the mutant 620T allele, we generated knock-in mice carrying the homozygous Plg-A622T mutation (PlgT/T), an equivalent to the A620T mutation in human Plg. PlgT/T mice grew normally but showed severely reduced plasmin activity activated by urokinase, equivalent to ~8% of that in wild-type mice. In vitro fibrin clot lysis in plasma was significantly slower in PlgT/T mice than in wild-type mice. However, all experimental models of electrolytic deep vein thrombosis, tissue factor-induced pulmonary embolism, transient focal brain ischaemic stroke, or skin-wound healing showed largely similar phenotypes between PlgT/T mice and wild-type mice. Protein S-K196E mutation (Pros1E/E) is a race-specific genetic risk factor for venous thromboembolism. Coexistence in mice of PlgT/T and Pros1E/E did not affect pulmonary embolism symptoms, compared with those in Pros1E/E mice. Hence, the present study showed that the Plg-A622T mutation, which confers ~8% plasmin activity, does not increase the risk of thrombotic diseases in mice under experimental thrombotic conditions and does not modify the thrombotic phenotype observed in Pros1E/E mice. PlgT/T mice can be used to investigate the potential pathophysiological impact of the Plg-A620T mutation.
[Mh] Termos MeSH primário: Conjuntivite/genética
Técnicas de Introdução de Genes
Mutação
Fenótipo
Plasminogênio/deficiência
Plasminogênio/genética
Dermatopatias Genéticas/genética
Tromboembolia Venosa/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Isquemia Encefálica/sangue
Isquemia Encefálica/genética
Isquemia Encefálica/patologia
Conjuntivite/sangue
Conjuntivite/patologia
Modelos Animais de Doenças
Feminino
Fibrina/genética
Fibrina/metabolismo
Fibrinolisina/genética
Fibrinolisina/metabolismo
Expressão Gênica
Seres Humanos
Masculino
Camundongos
Camundongos Transgênicos
Plasminogênio/metabolismo
Proteína S/genética
Proteína S/metabolismo
Embolia Pulmonar/sangue
Embolia Pulmonar/genética
Embolia Pulmonar/patologia
Dermatopatias Genéticas/sangue
Dermatopatias Genéticas/patologia
Acidente Vascular Cerebral/sangue
Acidente Vascular Cerebral/genética
Acidente Vascular Cerebral/patologia
Tromboembolia Venosa/sangue
Tromboembolia Venosa/patologia
Trombose Venosa/sangue
Trombose Venosa/genética
Trombose Venosa/patologia
Cicatrização/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein S); 9001-31-4 (Fibrin); 9001-91-6 (Plasminogen); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180981


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[PMID]:28653850
[Au] Autor:Schmidt TC; Eriksson PO; Gustafsson D; Cosgrove D; Frølund B; Boström J
[Ad] Endereço:Cardiovascular and Metabolic Diseases, Innovative Medicines and Early Development, AstraZeneca , Pepparedsleden 1, SE 43183 Mölndal, Sweden.
[Ti] Título:Discovery and Evaluation of Anti-Fibrinolytic Plasmin Inhibitors Derived from 5-(4-Piperidyl)isoxazol-3-ol (4-PIOL).
[So] Source:J Chem Inf Model;57(7):1703-1714, 2017 Jul 24.
[Is] ISSN:1549-960X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inhibition of plasmin has been found to effectively reduce fibrinolysis and to avoid hemorrhage. This can be achieved by addressing its kringle 1 domain with the known drug and lysine analogue tranexamic acid. Guided by shape similarities toward a previously discovered lead compound, 5-(4-piperidyl)isoxazol-3-ol, a set of 16 structurally similar compounds was assembled and investigated. Successfully, in vitro measurements revealed one compound, 5-(4-piperidyl)isothiazol-3-ol, superior in potency compared to the initial lead. Furthermore, a strikingly high correlation (R = 0.93) between anti-fibrinolytic activity and kringle 1 binding affinity provided strong support for the hypothesized inhibition mechanism, as well as revealing opportunities to fine-tune biological effects through minor structural modifications. Several different ligand-based (Freeform, shape, and electrostatic-based similarities) and structure-based methods (e.g., Posit, MM/GBSA, FEP+) were used to retrospectively predict the binding affinities. A combined method, molecular alignment using Posit and scoring with T , lead to the highest coefficient of determination (R = 0.6).
[Mh] Termos MeSH primário: Antifibrinolíticos/química
Antifibrinolíticos/farmacologia
Descoberta de Drogas
Fibrinolisina/antagonistas & inibidores
Isoxazóis/química
Isoxazóis/farmacologia
Piperidinas/química
Piperidinas/farmacologia
[Mh] Termos MeSH secundário: Antifibrinolíticos/metabolismo
Fibrinolisina/química
Fibrinolisina/metabolismo
Isoxazóis/metabolismo
Simulação de Acoplamento Molecular
Piperidinas/metabolismo
Domínios Proteicos
Relação Quantitativa Estrutura-Atividade
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifibrinolytic Agents); 0 (Isoxazoles); 0 (Piperidines); 132033-91-1 (5-(4-piperidyl)isoxazol-3-ol); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jcim.7b00255


  7 / 7334 MEDLINE  
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[PMID]:28601310
[Au] Autor:Morton AP; Moore EE; Moore HB; Gonzalez E; Chapman MP; Peltz E; Banerjee A; Silliman C
[Ad] Endereço:Department of Surgery-Trauma Research Center, University of Colorado, Denver, Colorado. Electronic address: alexander.morton@ucdenver.edu.
[Ti] Título:Hemoglobin-based oxygen carriers promote systemic hyperfibrinolysis that is both dependent and independent of plasmin.
[So] Source:J Surg Res;213:166-170, 2017 Jun 01.
[Is] ISSN:1095-8673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hyperfibrinolysis plays an integral role in the genesis of trauma-induced coagulopathy. Recent data demonstrate that red blood cell lysis promotes fibrinolysis; however, the mechanism is unclear. Hemoglobin-based oxygen carriers (HBOCs) have been developed for resuscitation and have been associated with coagulopathy. We hypothesize that replacement of whole blood (WB) using an HBOC results in a coagulopathy because of the presence of free hemoglobin. MATERIALS AND METHODS: WB was sampled from healthy donors (n = 6). The clotting profile of each citrated sample was evaluated using native thromboelastography. Serial titrations were performed using both HBOC (PolyHeme) and normal saline (NS; 5%, 25%, and 50%) and evaluated both with and without a 75-ng/mL tissue plasminogen activator (tPA) challenge. Tranexamic acid (TXA) was added to inhibit plasmin-dependent fibrinolysis. Fibrinolysis was measured and recorded as lysis at 30 min (LY30), the percentage of clot LY30 after maximal clot strength. Dilution of WB with NS or HBOC was correlated using LY30 via Spearman rho coefficients. Groups were also compared using a Friedman test and post hoc analysis with a Bonferroni adjustment. RESULTS: tPA-provoked fibrinolysis was enhanced by both HBOC (median LY30 at 5%, 25%, and 50% titrations: 11%, 21%, and 44%, respectively; Spearman = 0.94; P < 0.001) and NS (11%, 28%, and 58%, respectively; Spearman = 0.790; P < 0.001). However, HBOC also enhanced fibrinolysis without the addition of tPA (1%, 4%, 5%; Spearman = 0.735; P = 0.001) and NS did not (1%, 2%, 1%; r = 0.300; P = 0.186. Moreover, addition of TXA did not alter or inhibit this fibrinolysis (WB versus 50% HBOC: 1.8% versus 5.7%, P = 0.04). There was no significant difference in fibrinolysis of HBOC with or without TXA (50% HBOC versus 50% HBOC + TXA: 5.6% versus 5.7%, P = 0.92). In addition, the increased fibrinolysis seen with NS was reversed when TXA was present (WB versus 50% NS: 1.8% versus 1.7%, P = 1.0). CONCLUSIONS: HBOCs enhance fibrinolysis both with and without addition of tPA; moreover, this mechanism is independent of plasmin as the phenomenon persists in the presence of TXA. Our findings indicate the hemoglobin molecule or its components stimulate fibrinolysis by both tPA-dependent and innate mechanisms.
[Mh] Termos MeSH primário: Substitutos Sanguíneos/efeitos adversos
Fibrinolisina/metabolismo
Fibrinólise/efeitos dos fármacos
Hemoglobinas/efeitos adversos
[Mh] Termos MeSH secundário: Adulto
Biomarcadores/metabolismo
Fibrinólise/fisiologia
Voluntários Saudáveis
Seres Humanos
Masculino
Tromboelastografia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Blood Substitutes); 0 (Hemoglobins); 0 (PolyHeme); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170612
[St] Status:MEDLINE


  8 / 7334 MEDLINE  
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[PMID]:28524014
[Au] Autor:Johansson M; Lundh Å; de Vries R; Sjaunja KS
[Ad] Endereço:Department of Molecular Sciences,Swedish University of Agricultural Sciences,PO Box 7015,SE-750 07 Uppsala,Sweden.
[Ti] Título:Composition and enzymatic activity in bulk milk from dairy farms with conventional or robotic milking systems.
[So] Source:J Dairy Res;84(2):154-158, 2017 May.
[Is] ISSN:1469-7629
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The objective of the studies reported in this research communication was to investigate differences in composition and enzymatic activities in bulk milk samples provided from Swedish dairy farms with different management systems, i.e. automated (AMS) and conventional milking systems (CMS). A bulk milk sample was collected from each of 104 dairy farms, 51 using AMS and 53 using CMS, located in the same geographical region. Sampling took place within two consecutive days during the indoor period (October). Milk samples were analysed for contents of total fat and protein, free fatty acids (FFA), caseins and whey proteins, somatic cell count (SCC), pH, plasmin and plasminogen derived activities, and total proteolysis. Our results showed a lower protein content and higher SCC in bulk milk from AMS herds compared with milk from CMS herds. Plasmin, plasminogen and total plasmin/ plasminogen derived activities were lower in milk from AMS herds but despite this, total casein and the ß-casein fraction as % of total protein were lower in milk from AMS herds than in milk from herds using CMS. Total proteolysis was higher in milk from AMS herds, suggesting that other proteases than plasmin, e.g. cellular and bacterial proteases, contributed to the degradation of casein. This was supported by a positive correlation between SCC and total proteolysis (P < 0·01), as well as a negative correlation between total proteolysis and ß-casein fraction (P < 0·05). In conclusion, comparing the quality of bulk milk from commercial dairy herds using AMS and CMS, respectively, several differences were observed, suggesting a significant effect from management system.
[Mh] Termos MeSH primário: Bovinos
Indústria de Laticínios/instrumentação
Indústria de Laticínios/métodos
Leite/química
Leite/enzimologia
[Mh] Termos MeSH secundário: Animais
Caseínas/análise
Caseínas/metabolismo
Contagem de Células
Gorduras/análise
Ácidos Graxos não Esterificados/análise
Feminino
Fibrinolisina/metabolismo
Concentração de Íons de Hidrogênio
Lactação
Leite/citologia
Proteínas do Leite/análise
Plasminogênio/metabolismo
Proteólise
Suécia
Proteínas do Soro do Leite/análise
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caseins); 0 (Fats); 0 (Fatty Acids, Nonesterified); 0 (Milk Proteins); 0 (Whey Proteins); 9001-91-6 (Plasminogen); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1017/S0022029917000140


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[PMID]:28510599
[Au] Autor:Niego B; Lee N; Larsson P; De Silva TM; Au AE; McCutcheon F; Medcalf RL
[Ad] Endereço:Molecular Neurotrauma and Haemostasis, Australian Centre for Blood Diseases, Monash University, Melbourne, Victoria, Australia.
[Ti] Título:Selective inhibition of brain endothelial Rho-kinase-2 provides optimal protection of an in vitro blood-brain barrier from tissue-type plasminogen activator and plasmin.
[So] Source:PLoS One;12(5):e0177332, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rho-kinase (ROCK) inhibition, broadly utilised in cardiovascular disease, may protect the blood-brain barrier (BBB) during thrombolysis from rt-PA-induced damage. While the use of nonselective ROCK inhibitors like fasudil together with rt-PA may be hindered by possible hypotensive side-effects and inadequate capacity to block detrimental rt-PA activity in brain endothelial cells (BECs), selective ROCK-2 inhibition may overcome these limitations. Here, we examined ROCK-2 expression in major brain cells and compared the ability of fasudil and KD025, a selective ROCK-2 inhibitor, to attenuate rt-PA-induced BBB impairment in an in vitro human model. ROCK-2 was highly expressed relative to ROCK-1 in all human and mouse brain cell types and particularly enriched in rodent brain endothelial cells and astrocytes compared to neurons. KD025 was more potent than fasudil in attenuation of rt-PA- and plasminogen-induced BBB permeation under normoxia, but especially under stroke-like conditions. Importantly, only KD025, but not fasudil, was able to block rt-PA-dependent permeability increases, morphology changes and tight junction degradation in isolated BECs. Selective ROCK-2 inhibition further diminished rt-PA-triggered myosin phosphorylation, shape alterations and matrix metalloprotease activation in astrocytes. These findings highlight ROCK-2 as the key isoform driving BBB impairment and brain endothelial damage by rt-PA and the potential of KD025 to optimally protect the BBB during thrombolysis.
[Mh] Termos MeSH primário: Barreira Hematoencefálica/metabolismo
Encéfalo/metabolismo
Células Endoteliais/metabolismo
Fibrinolisina/metabolismo
Ativador de Plasminogênio Tecidual/metabolismo
Quinases Associadas a rho/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Astrócitos/efeitos dos fármacos
Astrócitos/metabolismo
Linhagem Celular
Expressão Gênica
Compostos Heterocíclicos de 4 ou mais Anéis/farmacologia
Seres Humanos
Camundongos
Permeabilidade
Isoformas de Proteínas
Transdução de Sinais
Ativador de Plasminogênio Tecidual/farmacologia
Quinases Associadas a rho/genética
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterocyclic Compounds, 4 or More Rings); 0 (KD025); 0 (Protein Isoforms); EC 2.7.11.1 (ROCK2 protein, human); EC 2.7.11.1 (rho-Associated Kinases); EC 3.4.21.68 (Tissue Plasminogen Activator); EC 3.4.21.7 (Fibrinolysin)
[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:170517
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177332


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[PMID]:28501622
[Au] Autor:Eiamboonsert S; Salama Y; Watarai H; Dhahri D; Tsuda Y; Okada Y; Hattori K; Heissig B
[Ad] Endereço:Division of Stem Cell Dynamics, Center for Stem Cell Biology and Regenerative Medicine, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
[Ti] Título:The role of plasmin in the pathogenesis of murine multiple myeloma.
[So] Source:Biochem Biophys Res Commun;488(2):387-392, 2017 Jun 24.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aside from a role in clot dissolution, the fibrinolytic factor, plasmin is implicated in tumorigenesis. Although abnormalities of coagulation and fibrinolysis have been reported in multiple myeloma patients, the biological roles of fibrinolytic factors in multiple myeloma (MM) using in vivo models have not been elucidated. In this study, we established a murine model of fulminant MM with bone marrow and extramedullar engraftment after intravenous injection of B53 cells. We found that the fibrinolytic factor expression pattern in murine B53 MM cells is similar to the expression pattern reported in primary human MM cells. Pharmacological targeting of plasmin using the plasmin inhibitors YO-2 did not change disease progression in MM cell bearing mice although systemic plasmin levels was suppressed. Our findings suggest that although plasmin has been suggested to be a driver for disease progression using clinical patient samples in MM using mostly in vitro studies, here we demonstrate that suppression of plasmin generation or inhibition of plasmin cannot alter MM progression in vivo.
[Mh] Termos MeSH primário: Fibrinolisina/metabolismo
Mieloma Múltiplo/metabolismo
Mieloma Múltiplo/patologia
Neoplasias Experimentais/metabolismo
Neoplasias Experimentais/patologia
[Mh] Termos MeSH secundário: Animais
Antifibrinolíticos/química
Antifibrinolíticos/farmacologia
Antineoplásicos/química
Antineoplásicos/farmacologia
Bortezomib/administração & dosagem
Bortezomib/farmacologia
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Dipeptídeos/química
Dipeptídeos/farmacologia
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Doxorrubicina/administração & dosagem
Doxorrubicina/farmacologia
Ensaios de Seleção de Medicamentos Antitumorais
Feminino
Fibrinolisina/antagonistas & inibidores
Seres Humanos
Camundongos
Camundongos Endogâmicos NOD
Camundongos SCID
Mieloma Múltiplo/tratamento farmacológico
Neoplasias Experimentais/tratamento farmacológico
Relação Estrutura-Atividade
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifibrinolytic Agents); 0 (Antineoplastic Agents); 0 (Dipeptides); 0 (YO 2 compound); 69G8BD63PP (Bortezomib); 80168379AG (Doxorubicin); EC 3.4.21.7 (Fibrinolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170515
[St] Status:MEDLINE



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