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[PMID]:29332224
[Au] Autor:Tong D; Yu M; Guo L; Li T; Li J; Novakovic VA; Dong Z; Tian Y; Kou J; Bi Y; Wang J; Zhou J; Shi J
[Ad] Endereço:Department of Hematology, First Hospital, Harbin Medical University, 23 Youzheng Street, Nangang District, Harbin, 150001, China.
[Ti] Título:Phosphatidylserine-exposing blood and endothelial cells contribute to the hypercoagulable state in essential thrombocythemia patients.
[So] Source:Ann Hematol;97(4):605-616, 2018 Apr.
[Is] ISSN:1432-0584
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The mechanisms of thrombogenicity in essential thrombocythemia (ET) are complex and not well defined. Our objective was to explore whether phosphatidylserine (PS) exposure on blood cells and endothelial cells (ECs) can account for the increased thrombosis and distinct thrombotic risks among mutational subtypes in ET. Using flow cytometry and confocal microscopy, we found that the levels of PS-exposing erythrocytes, platelets, leukocytes, and serum-cultured ECs were significantly higher in each ET group [JAK2, CALR, and triple-negative (TN) (all P < 0.001)] than those in controls. Among ET patients, those with JAK2 mutations showed higher levels of PS-positive erythrocytes, platelets, neutrophils, and serum-cultured ECs than TN patients or those with CALR mutations, which show similar levels. Coagulation function assays showed that higher levels of PS-positive blood cells and serum-cultured ECs led to markedly shortened coagulation time and dramatically increased levels of FXa, thrombin, and fibrin production. This procoagulant activity could be largely blocked by addition of lactadherin (approx. 70% inhibition). Confocal microscopy showed that the FVa/FXa complex and fibrin fibrils colocalized with PS on ET serum-cultured ECs. Additionally, we found a relationship between D-dimer, prothrombin fragment F1 + 2, and PS exposure. Our study reveals a previously unrecognized link between hypercoagulability and exposed PS on cells, which might also be associated with distinct thrombotic risks among mutational subtypes in ET. Thus, blocking PS-binding sites may represent a new therapeutic target for preventing thrombosis in ET.
[Mh] Termos MeSH primário: Plaquetas/patologia
Endotélio Vascular/patologia
Eritrócitos/patologia
Leucócitos/patologia
Fosfatidilserinas/metabolismo
Trombocitemia Essencial/fisiopatologia
Trombose/etiologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Substituição de Aminoácidos
Plaquetas/metabolismo
Calreticulina/genética
Calreticulina/metabolismo
Células Cultivadas
China/epidemiologia
Endotélio Vascular/metabolismo
Eritrócitos/metabolismo
Feminino
Células Endoteliais da Veia Umbilical Humana/citologia
Células Endoteliais da Veia Umbilical Humana/metabolismo
Seres Humanos
Janus Quinase 2/genética
Janus Quinase 2/metabolismo
Leucócitos/metabolismo
Masculino
Meia-Idade
Mutação
Receptores de Trombopoetina/genética
Receptores de Trombopoetina/metabolismo
Risco
Propriedades de Superfície
Trombocitemia Essencial/genética
Trombocitemia Essencial/metabolismo
Trombocitemia Essencial/patologia
Trombose/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calreticulin); 0 (Phosphatidylserines); 0 (Receptors, Thrombopoietin); 0 (calreticulin, human); 143641-95-6 (MPL protein, human); EC 2.7.10.2 (JAK2 protein, human); EC 2.7.10.2 (Janus Kinase 2)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180115
[St] Status:MEDLINE
[do] DOI:10.1007/s00277-018-3228-6


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[PMID]:27778166
[Au] Autor:Fan R; Yuan Y; Zhang Q; Zhou XR; Jia L; Liu Z; Yu C; Luo SZ; Chen L
[Ad] Endereço:Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China.
[Ti] Título:Isoleucine/leucine residues at "a" and "d" positions of a heptad repeat sequence are crucial for the cytolytic activity of a short anticancer lytic peptide.
[So] Source:Amino Acids;49(1):193-202, 2017 01.
[Is] ISSN:1438-2199
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Many lytic peptides contain a heptad sequence with leucine or isoleucine residues at "a" and "d" positions. However, their roles in the peptide-induced cytolytic process remain unclear. We have recently reported an anticancer lytic peptide ZXR-2 (FKIGGFIKKLWRSLLA), which contains a shortened zipper-like sequence with Ile/Leu at "a" and "d" positions. To understand the roles of these Ile/Leu residues, a series of analogs were constructed by sequentially replacing the Ile or Leu residue with alanine (Ala). Significant reduction of the cytolytic activity was observed when the Ile (3rd and 7th) and Leu (10th and 14th) residues at the "a" and "d" positions were substituted, while the replacement of the separate Leu (15th) residue had less effect. Based on the quenching of the intrinsic fluorescence of the peptides and their induced surface pressure changes of lipid monolayer, it was conjectured that the peptide ZXR-2 might insert into cell membranes from the C-terminal and to a depth of the W position. Accordingly, I , I , and L residues which mainly exposed in aqueous solution were more responsible for the peptide self-association on cell membranes, while L , together with L , might help peptide insert and anchor to cell membranes. These results are significant to elucidate the crucial roles of such Ile/Leu residues at "a" and "d" positions in peptide-peptide and peptide-membrane interactions to exert the membrane disruption activity of lytic peptides. With further understanding about the structure-activity relationship of lytic peptides, it would be helpful for designing novel anticancer lytic peptides.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Isoleucina/química
Leucina/química
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: 1,2-Dipalmitoilfosfatidilcolina/análogos & derivados
1,2-Dipalmitoilfosfatidilcolina/química
Alanina/química
Sequência de Aminoácidos
Substituição de Aminoácidos
Antineoplásicos/síntese química
Linhagem Celular Tumoral
Membrana Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Colesterol/química
Células HEK293
Células HeLa
Seres Humanos
L-Lactato Desidrogenase/secreção
Lipossomos/química
Peptídeos/síntese química
Fosfatidilserinas/química
Engenharia de Proteínas
Estrutura Secundária de Proteína
Eletricidade Estática
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Liposomes); 0 (Peptides); 0 (Phosphatidylserines); 04Y7590D77 (Isoleucine); 2644-64-6 (1,2-Dipalmitoylphosphatidylcholine); 3036-82-6 (dipalmitoylphosphatidylserine); 319X2NFW0A (colfosceril palmitate); 97C5T2UQ7J (Cholesterol); EC 1.1.1.27 (L-Lactate Dehydrogenase); GMW67QNF9C (Leucine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE
[do] DOI:10.1007/s00726-016-2350-9


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[PMID]:29254311
[Au] Autor:Jagmag T; Tirant M; Lotti T
[Ad] Endereço:The Dent-All Clinic, Mumbai, India.
[Ti] Título:Link between cutaneous infection, stress and depression.
[So] Source:J Biol Regul Homeost Agents;31(4):1037-1041, 2017 Oct-Dec.
[Is] ISSN:0393-974X
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:Depression and mood disorders often develop after dermatological conditions which could be primary or secondary to dermatological pathology. The oxidative and psychological stress cause physiological changes in the body. Shift in the methylation pathway, elevated cortisol, lowered neurotransmitter levels and lowered immune system allow infection to penetrate the body and lead to anxiety and depression. Here, a case report of a 20 year old male patient is presented to show how infectious skin lesions, unresponsive to the usual treatment plan, were treated after using a multipronged approach of addressing systemic infection of Escherichia coli, elevated cortisol levels and nutritional imbalances.
[Mh] Termos MeSH primário: Ansiedade/psicologia
Depressão/psicologia
Infecções por Escherichia coli/psicologia
Dermatopatias Bacterianas/psicologia
Estresse Psicológico/psicologia
[Mh] Termos MeSH secundário: Antibacterianos/uso terapêutico
Ansiedade/complicações
Ansiedade/tratamento farmacológico
Ansiedade/microbiologia
Cefoperazona/uso terapêutico
Depressão/complicações
Depressão/tratamento farmacológico
Depressão/microbiologia
Infecções por Escherichia coli/complicações
Infecções por Escherichia coli/tratamento farmacológico
Infecções por Escherichia coli/microbiologia
Seres Humanos
Hidrocortisona/sangue
Masculino
Fosfatidilserinas/uso terapêutico
Probióticos/uso terapêutico
Dermatopatias Bacterianas/complicações
Dermatopatias Bacterianas/tratamento farmacológico
Dermatopatias Bacterianas/microbiologia
Estresse Psicológico/complicações
Estresse Psicológico/tratamento farmacológico
Estresse Psicológico/microbiologia
Sulbactam/uso terapêutico
Resultado do Tratamento
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Phosphatidylserines); 7U75I1278D (Cefoperazone); S4TF6I2330 (Sulbactam); WI4X0X7BPJ (Hydrocortisone)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


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[PMID]:29309811
[Au] Autor:Park EJ; Park SJ; Kim S; Lee K; Chang J
[Ad] Endereço:Graduate school of East-West Medical Science, Kyung Hee University, Yongin-si, Gyeonggi-do, 17104, Republic of Korea. Electronic address: pejtoxic@hanmail.net.
[Ti] Título:Lung fibroblasts may play an important role in clearing apoptotic bodies of bronchial epithelial cells generated by exposure to PHMG-P-containing solution.
[So] Source:Toxicol Lett;286:108-119, 2018 Apr.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Polyhexamethylene guanidine (PHMG) has been widely used in the industry owing to its excellent biocidal, anti-corrosive, and anti-biofouling properties. In Korea, consumers exposed to PHMG-phosphate (PHMG-P)-containing humidifier disinfectant have begun to suffer from fibrotic lung injury-related symptoms for unknown reasons. However, no appropriate treatment has yet been found because the detail toxic mechanism has not been identified. Herein, we first studied the toxic mechanism of PHMG-P-containing solution using human normal bronchial epithelial cells (BEAS-2B cells). When exposed for 24 h, PHMG-P-containing solution rapidly decreased cell viability from around 6 h after exposure and significantly increased of the phosphatidylserine exposure and the LDH release. At 6 h of exposure, the material contained in the solution was found to be bound to the cell membrane and the inner wall of vacuoles, and damaged the cell membrane and organelles. In addition, a significant increase of IFN-γ was observed among cytokines, the expression of apoptosis-, autophagy-, and membrane and DNA damage-related proteins was also enhanced. Meanwhile, the level of intracellular ROS and the secretion of IL-8 and CXCL-1, which are chemokines for professional phagocytes, decreased. Thus, we treated dead BEAS-2B cells to lung fibroblasts (HFL-1), non-professional phagocytes, and then we observed that the dead cells rapidly attached to HFL-1 cells and were taken up. Additionally, increased secretion of IL-8 and CXCL-1 was observed in the cells. Based on these results, we suggest that pulmonary exposure to PHMG-P induces apoptosis of bronchial epithelial cells and lung fibroblasts might play an important role in the clearance of the apoptotic debris.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Brônquios/efeitos dos fármacos
Citofagocitose
Desinfetantes/toxicidade
Células Epiteliais/efeitos dos fármacos
Fibroblastos/metabolismo
Guanidinas/toxicidade
[Mh] Termos MeSH secundário: Brônquios/metabolismo
Brônquios/ultraestrutura
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Quimiocina CXCL1/metabolismo
Relação Dose-Resposta a Droga
Células Epiteliais/metabolismo
Células Epiteliais/ultraestrutura
Fibroblastos/ultraestrutura
Seres Humanos
Interferon gama/metabolismo
Interleucina-8/metabolismo
L-Lactato Desidrogenase/metabolismo
Fosfatidilserinas/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CXCL1 protein, human); 0 (Chemokine CXCL1); 0 (Disinfectants); 0 (Guanidines); 0 (IFNG protein, human); 0 (IL8 protein, human); 0 (Interleukin-8); 0 (Phosphatidylserines); 31961-54-3 (polyhexamethyleneguanidine); 82115-62-6 (Interferon-gamma); EC 1.1.1.27 (L-Lactate Dehydrogenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29236391
[Au] Autor:Suleimanova RR; Hudz EA; Melnychuk DO; Kalachniuk LH
[Ti] Título:Age-related changes phospholipids of sterlet in liver and dorsal muscles.
[So] Source:Ukr Biochem J;89(1):71-5, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Study of phospholipids changes peculiarities in the liver and dorsal muscles of sterlet (Acipenser ruthenus Linnaeus) may be important to determine the etiology and pathogenesis of fatty liver. We established that the content of total phospholipids in tissues of the liver and dorsal muscles of three-year-old sterlet was less than for two-year-old fish by 15% and 20% (P ≤ 0.01), respectively. The amount of phosphatidylcholine (P ≤ 0.05), phosphatidylethanolamine, phosphatidylserine (P ≤ 0.01), phosphatidylinositol (P ≤ 0.01) and cardiolipin in the liver of 3-year-old sterlet was lower than for the 2-year-old fish, while quantitative indices for lysophosphatidylcholine and sphingomyelin were slightly increased. Similarly, in the cells of the dorsal muscles, the amount of phospholipid components (except lysophosphatidylcholine) was decreased with age. A decrease in the amount of phosphatidylethanolamine and phosphatidylserine in the dorsal muscles of 3-year-old sterlet was significant. The major phospholipids respective distribution was stable, except for phosphatidylethanolamine and particularly sphingomyelin.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Fígado/metabolismo
Músculos/metabolismo
Fosfolipídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Cardiolipinas/metabolismo
Peixes
Fígado/química
Lisofosfatidilcolinas/metabolismo
Músculos/química
Fosfatidilcolinas/metabolismo
Fosfatidiletanolaminas/metabolismo
Fosfatidilinositóis/metabolismo
Fosfatidilserinas/metabolismo
Esfingomielinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cardiolipins); 0 (Lysophosphatidylcholines); 0 (Phosphatidylcholines); 0 (Phosphatidylethanolamines); 0 (Phosphatidylinositols); 0 (Phosphatidylserines); 0 (Phospholipids); 0 (Sphingomyelins); 39382-08-6 (phosphatidylethanolamine)
[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:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj89.01.071


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[PMID]:28456331
[Au] Autor:Zdanowicz R; Kreutzberger A; Liang B; Kiessling V; Tamm LK; Cafiso DS
[Ad] Endereço:Department of Chemistry, University of Virginia, Charlottesville, Virginia; Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, Virginia.
[Ti] Título:Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.
[So] Source:Biophys J;113(6):1235-1250, 2017 Sep 19.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Complexin-1 is a SNARE effector protein that decreases spontaneous neurotransmitter release and enhances evoked release. Complexin binds to the fully assembled four-helical neuronal SNARE core complex as revealed in competing molecular models derived from x-ray crystallography. Presently, it is unclear how complexin binding to the postfusion complex accounts for its effects upon spontaneous and evoked release in vivo. Using a combination of spectroscopic and imaging methods, we characterize in molecular detail how complexin binds to the 1:1 plasma membrane t-SNARE complex of syntaxin-1a and SNAP-25 while simultaneously binding the lipid bilayer at both its N- and C-terminal ends. These interactions are cooperative, and binding to the prefusion acceptor t-SNARE complex is stronger than to the postfusion core complex. This complexin interaction reduces the affinity of synaptobrevin-2 for the 1:1 complex, thereby retarding SNARE assembly and vesicle docking in vitro. The results provide the basis for molecular models that account for the observed clamping effect of complexin beginning with the acceptor t-SNARE complex and the subsequent activation of the clamped complex by Ca and synaptotagmin.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Bicamadas Lipídicas/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Proteína 25 Associada a Sinaptossoma/metabolismo
Sintaxina 1/metabolismo
Proteína 2 Associada à Membrana da Vesícula/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Adaptadoras de Transporte Vesicular/genética
Animais
Escherichia coli
Bicamadas Lipídicas/química
Lipossomos/química
Lipossomos/metabolismo
Mutação
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Fosfatidilcolinas/química
Fosfatidilserinas/química
Ligação Proteica
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Propriedades de Superfície
Proteína 25 Associada a Sinaptossoma/química
Sintaxina 1/química
Proteína 2 Associada à Membrana da Vesícula/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Lipid Bilayers); 0 (Liposomes); 0 (Nerve Tissue Proteins); 0 (Phosphatidylcholines); 0 (Phosphatidylserines); 0 (Recombinant Proteins); 0 (Snap25 protein, rat); 0 (Synaptosomal-Associated Protein 25); 0 (Syntaxin 1); 0 (Vamp2 protein, rat); 0 (Vesicle-Associated Membrane Protein 2); 0 (complexin I); 40290-44-6 (1-palmitoyl-2-oleoylglycero-3-phosphoserine); TE895536Y5 (1-palmitoyl-2-oleoylphosphatidylcholine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


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[PMID]:28748286
[Au] Autor:Klaihmon P; Vimonpatranon S; Noulsri E; Lertthammakiat S; Anurathapan U; Sirachainan N; Hongeng S; Pattanapanyasat K
[Ad] Endereço:Graduate Program in Immunology, Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand.
[Ti] Título:Normalized levels of red blood cells expressing phosphatidylserine, their microparticles, and activated platelets in young patients with ß-thalassemia following bone marrow transplantation.
[So] Source:Ann Hematol;96(10):1741-1747, 2017 Oct.
[Is] ISSN:1432-0584
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Bone marrow transplantation (BMT) serves as the only curative treatment for patients with ß-thalassemia major; however, hemostatic changes have been observed in these BMT patients. Aggregability of thalassemic red blood cells (RBCs) and increased red blood cell-derived microparticles (RMPs) expressing phosphatidylserine (PS) are thought to participate in thromboembolic events by initially triggering platelet activation. To our knowledge, there has been no report providing quantitation of these circulating PS-expressing RBCs and RMPs in young ß-thalassemia patients after BMT. Whole blood from each subject was fluorescently labeled to detect RBC markers (CD235a) and annexin-V together with the known number TruCount™ beads. PS-expressing RBCs, RMPs, and activated platelets were identified by flow cytometry. In our randomized study, we found the decreased levels of three aforementioned factors compared to levels in patients receiving regular blood transfusion (RT). This study showed that BMT in ß-thalassemia patients decreases the levels of circulating PS-expressing RBCs, their MPs, and procoagulant platelets when compared to patients who received RT. Normalized levels of these coagulation markers may provide the supportive evidence of the effectiveness of BMT for curing thalassemia.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Transplante de Medula Óssea
Micropartículas Derivadas de Células/metabolismo
Eritrócitos/metabolismo
Fosfatidilserinas/sangue
Ativação Plaquetária
Talassemia beta
[Mh] Termos MeSH secundário: Adolescente
Aloenxertos
Anexina A5/sangue
Criança
Feminino
Seres Humanos
Masculino
Talassemia beta/sangue
Talassemia beta/terapia
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A5); 0 (Phosphatidylserines)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171129
[Lr] Data última revisão:
171129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1007/s00277-017-3070-2


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[PMID]:28409836
[Au] Autor:Wang Y; Zhang S; Luo L; Norström E; Braun OÖ; Mörgelin M; Thorlacius H
[Ad] Endereço:Department of Clinical Sciences, Section for Surgery, Lund University, Malmö, Sweden.
[Ti] Título:Platelet-derived microparticles regulates thrombin generation via phophatidylserine in abdominal sepsis.
[So] Source:J Cell Physiol;233(2):1051-1060, 2018 Feb.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sepsis is associated with dysfunctional coagulation. Recent data suggest that platelets play a role in sepsis by promoting neutrophil accumulation. Herein, we show that cecal ligation and puncture (CLP) triggered systemic inflammation, which is characterized by formation of IL-6 and CXC chemokines as well as neutrophil accumulation in the lung. Platelet depletion decreased neutrophil accumulation, IL-6, and CXC chemokines formation in septic lungs. Depletion of platelets increased peak thrombin formation and total thrombin generation (TG) in plasma from septic animals. CLP elevated circulating levels of platelet-derived microparticles (PMPs). In vitro generated PMPs were a potent inducer of TG. Interestingly, in vitro wild-type recombinant annexin V abolished PMP-induced thrombin formation whereas a mutant annexin V protein, which does not bind to phosphatidylserine (PS), had no effect. Administration of wild-type, but not mutant annexin V, significantly inhibited thrombin formation in septic animals. Moreover, CLP-induced formation of thrombin-antithrombin complexes were reduced in platelet-depleted mice and in animals pretreated with annexin V. PMP-induced TG attenuated in FXII- and FVII-deficient plasma. These findings suggest that sepsis-induced TG is dependent on platelets. Moreover, PMPs formed in sepsis are a potent inducer of TG via PS exposure, and activation of both the intrinsic and extrinsic pathway of coagulation. In conclusion, these observations suggest that PMPs and PS play an important role in dysfunctional coagulation in abdominal sepsis.
[Mh] Termos MeSH primário: Coagulação Sanguínea
Plaquetas/metabolismo
Micropartículas Derivadas de Células/metabolismo
Fosfatidilserinas/sangue
Sepse/sangue
Trombina/metabolismo
[Mh] Termos MeSH secundário: Animais
Anexina A5/sangue
Antitrombina III
Plaquetas/imunologia
Plaquetas/microbiologia
Plaquetas/ultraestrutura
Micropartículas Derivadas de Células/imunologia
Micropartículas Derivadas de Células/microbiologia
Micropartículas Derivadas de Células/ultraestrutura
Quimiocinas CXC/metabolismo
Modelos Animais de Doenças
Inflamação/sangue
Inflamação/imunologia
Inflamação/microbiologia
Interleucina-6/metabolismo
Pulmão/imunologia
Pulmão/metabolismo
Pulmão/microbiologia
Masculino
Camundongos Endogâmicos C57BL
Infiltração de Neutrófilos
Peptídeo Hidrolases/sangue
Sepse/imunologia
Sepse/microbiologia
Sepse/patologia
Transdução de Sinais
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A5); 0 (Chemokines, CXC); 0 (Interleukin-6); 0 (Phosphatidylserines); 0 (antithrombin III-protease complex); 0 (interleukin-6, mouse); 9000-94-6 (Antithrombin III); EC 3.4.- (Peptide Hydrolases); EC 3.4.21.5 (Thrombin)
[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:170415
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25959


  9 / 7260 MEDLINE  
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[PMID]:28937994
[Au] Autor:Hakobyan D; Gerke V; Heuer A
[Ad] Endereço:Institute of Physical Chemistry, University of Muenster, Muenster, Germany.
[Ti] Título:Modeling of annexin A2-Membrane interactions by molecular dynamics simulations.
[So] Source:PLoS One;12(9):e0185440, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The annexins are a family of Ca2+-regulated phospholipid binding proteins that are involved in membrane domain organization and membrane trafficking. Although they are widely studied and crystal structures are available for several soluble annexins their mode of membrane association has never been studied at the molecular level. Here we obtained molecular information on the annexin-membrane interaction that could serve as paradigm for the peripheral membrane association of cytosolic proteins by Molecular Dynamics simulations. We analyzed systems containing the monomeric annexin A2 (AnxA2), a membrane with negatively charged phosphatidylserine (POPS) lipids as well as Ca2+ ions. On the atomic level we identify the AnxA2 orientations and the respective residues which display the strongest interaction with Ca2+ ions and the membrane. The simulation results fully agree with earlier experimental findings concerning the positioning of bound Ca2+ ions. Furthermore, we identify for the first time a significant interaction between lysine residues of the protein and POPS lipids that occurs independently of Ca2+ suggesting that AnxA2-membrane interactions can also occur in a low Ca2+ environment. Finally, by varying Ca2+ concentrations and lipid composition in our simulations we observe a calcium-induced negative curvature of the membrane as well as an AnxA2-induced lipid ordering.
[Mh] Termos MeSH primário: Anexina A2/metabolismo
Membranas Artificiais
Simulação de Dinâmica Molecular
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Cátions Bivalentes/metabolismo
Citosol/metabolismo
Dimerização
Fosfatidilserinas/química
Ligação Proteica
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Annexin A2); 0 (Cations, Divalent); 0 (Membranes, Artificial); 0 (Phosphatidylserines); 40290-44-6 (1-palmitoyl-2-oleoylglycero-3-phosphoserine); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185440


  10 / 7260 MEDLINE  
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[PMID]:28930754
[Au] Autor:Al Mamun Bhuyan A; Nüßle S; Cao H; Zhang S; Lang F
[Ad] Endereço:Department of Internal Medicine III, Eberhard-Karls-University of Tuebingen, Tuebingen, Germany.
[Ti] Título:Simvastatin, a Novel Stimulator of Eryptosis, the Suicidal Erythrocyte Death.
[So] Source:Cell Physiol Biochem;43(2):492-506, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: The 3-hydroxy-3-methyl-glutaryl-Coenzyme A (HMG-CoA) reductase inhibitor simvastatin has been shown to trigger apoptosis of several cell types. The substance has thus been proposed as an additional treatment of malignancy. Similar to apoptosis of nucleated cells, erythrocytes may enter eryptosis, the suicidal erythrocyte death. Hallmarks of eryptosis include cell shrinkage and cell membrane scrambling with phosphatidylserine translocation to the extracellular face of the erythrocyte cell membrane. Signaling contributing to stimulation of eryptosis include increase of cytosolic Ca2+ activity ([Ca2+]i), induction of oxidative stress, increase of ceramide abundance, and activation of SB203580-sensitive p38 kinase. The present study explored, whether simvastatin induces eryptosis and aimed to shed light on cellular mechanisms involved. METHODS: Flow cytometry was employed to quantify phosphatidylserine exposure at the cell surface from annexin-V-binding, cell volume from forward scatter, [Ca2+]i from Fluo3-fluorescence, reactive oxygen species (ROS) abundance from DCFDA dependent fluorescence, and ceramide abundance utilizing specific antibodies. Hemolysis was estimated from hemoglobin concentration in the supernatant. RESULTS: A 48 h exposure of human erythrocytes to simvastatin (1 µg/ml) significantly decreased the forward scatter, significantly augmented the percentage of annexin-V-binding cells, significantly increased Fluo3-fluorescence, and significantly enhanced DCFDA fluorescence. Simvastatin tended to increase ceramide abundance, an effect, however, escaping statistical significance. The effect of simvastatin on annexin-V-binding was significantly blunted by removal of extracellular Ca2+ and by addition of SB203580 (2 µM). CONCLUSIONS: Simvastatin stimulates eryptosis, an effect at least in part due to Ca2+ entry, oxidative stress, and p38 kinase.
[Mh] Termos MeSH primário: Eriptose/efeitos dos fármacos
Eritrócitos/efeitos dos fármacos
Inibidores de Hidroximetilglutaril-CoA Redutases/farmacologia
Sinvastatina/farmacologia
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Ceramidas/metabolismo
Eritrócitos/citologia
Eritrócitos/metabolismo
Citometria de Fluxo
Hemólise/efeitos dos fármacos
Seres Humanos
Estresse Oxidativo/efeitos dos fármacos
Fosfatidilserinas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ceramides); 0 (Hydroxymethylglutaryl-CoA Reductase Inhibitors); 0 (Phosphatidylserines); 0 (Reactive Oxygen Species); AGG2FN16EV (Simvastatin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170921
[St] Status:MEDLINE
[do] DOI:10.1159/000480476



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