Seminars in thrombosis and hemostasis最新文献_第9页

Thrombosis in Antiphospholipid Syndrome: Current Perspectives and Challenges in Laboratory Testing for Antiphospholipid Antibodies. 抗磷脂综合征的血栓形成：抗磷脂抗体实验室检测的当前视角与挑战》（Current Perspectives and Challenges in Laboratory Testing for Antiphospholipid Antibodies）。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-07 DOI: 10.1055/s-0044-1791699

Katrien M J Devreese

{"title":"Thrombosis in Antiphospholipid Syndrome: Current Perspectives and Challenges in Laboratory Testing for Antiphospholipid Antibodies.","authors":"Katrien M J Devreese","doi":"10.1055/s-0044-1791699","DOIUrl":"https://doi.org/10.1055/s-0044-1791699","url":null,"abstract":"Antiphospholipid syndrome (APS) diagnosis hinges on identifying antiphospholipid antibodies (aPL). Currently, laboratory testing encompasses lupus anticoagulant (LA), anticardiolipin (aCL), and anti-β2-glycoprotein I antibodies (aβ2GPI) IgG or IgM, which are included in the APS classification criteria. All the assays needed to detect aPL antibodies have methodological concerns. LA testing remains challenging due to its complexity and susceptibility to interference from anticoagulant therapy. Solid phase assays for aCL and aβ2GPI exhibit discrepancies between different assays. Antibody profiles aid in identifying the patients at risk for thrombosis through integrated interpretation of all positive aPL tests. Antibodies targeting domain I of β2-glycoprotein and antiphosphatidylserine-prothrombin antibodies have been evaluated for their role in thrombotic APS but are not yet included in the APS criteria. Detecting these antibodies may help patients with incomplete antibody profiles and stratify the risk of APS patients. The added diagnostic value of other methodologies and measurements of other APS-associated antibodies are inconsistent. This manuscript describes laboratory parameters useful in the diagnosis of thrombotic APS and will concentrate on the laboratory aspects, clinical significance of assays, and interpretation of aPL results in the diagnosis of thrombotic APS.","PeriodicalId":21673,"journal":{"name":"Seminars in thrombosis and hemostasis","volume":" ","pages":""},"PeriodicalIF":3.6,"publicationDate":"2024-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142393077","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Inhibitors of Polyphosphate and Neutrophil Extracellular Traps. 多磷酸盐和中性粒细胞胞外陷阱抑制剂。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2023-05-16 DOI: 10.1055/s-0043-1768936

Sreeparna Vappala, Stephanie A Smith, Jayachandran N Kizhakkedathu, James H Morrissey

{"title":"Inhibitors of Polyphosphate and Neutrophil Extracellular Traps.","authors":"Sreeparna Vappala, Stephanie A Smith, Jayachandran N Kizhakkedathu, James H Morrissey","doi":"10.1055/s-0043-1768936","DOIUrl":"10.1055/s-0043-1768936","url":null,"abstract":"The contact pathway of blood clotting has received intense interest in recent years as studies have linked it to thrombosis, inflammation, and innate immunity. Because the contact pathway plays little to no role in normal hemostasis, it has emerged as a potential target for safer thromboprotection, relative to currently approved antithrombotic drugs which all target the final common pathway of blood clotting. Research since the mid-2000s has identified polyphosphate, DNA, and RNA as important triggers of the contact pathway with roles in thrombosis, although these molecules also modulate blood clotting and inflammation via mechanisms other than the contact pathway of the clotting cascade. The most significant source of extracellular DNA in many disease settings is in the form of neutrophil extracellular traps (NETs), which have been shown to contribute to incidence and severity of thrombosis. This review summarizes known roles of extracellular polyphosphate and nucleic acids in thrombosis, with an emphasis on novel agents under current development that target the prothrombotic activities of polyphosphate and NETs.","PeriodicalId":21673,"journal":{"name":"Seminars in thrombosis and hemostasis","volume":" ","pages":"970-977"},"PeriodicalIF":3.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10651799/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9477797","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Prone Position and the Risk of Venous Thrombosis in COVID-19 Patients with Respiratory Failure. 俯卧位与 COVID-19 呼吸衰竭患者静脉血栓形成的风险。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2024-05-11 DOI: 10.1055/s-0044-1786735

Giuseppe Lippi, Camilla Mattiuzzi, Emmanuel J Favaloro

引用次数: 0

Contact Activation: Where Thrombosis and Hemostasis Meet on a Foreign Surface, Plus a Mini-editorial Compilation ("Part XVI"). 接触活化：血栓与止血在异物表面相遇，外加小型编辑汇编（"第 XVI 部分"）。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2024-05-17 DOI: 10.1055/s-0044-1786751

Helen H Vu, Owen J T McCarty, Emmanuel J Favaloro

引用次数: 0

Heparins May Not Be the Optimal Anticoagulants for Sepsis and Sepsis-Associated Disseminated Intravascular Coagulation. 肝素可能不是败血症和败血症相关弥散性血管内凝血的最佳抗凝剂。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2024-05-11 DOI: 10.1055/s-0044-1786754

Toshiaki Iba, Julie Helms, Takaaki Totoki, Jerrold H Levy

{"title":"Heparins May Not Be the Optimal Anticoagulants for Sepsis and Sepsis-Associated Disseminated Intravascular Coagulation.","authors":"Toshiaki Iba, Julie Helms, Takaaki Totoki, Jerrold H Levy","doi":"10.1055/s-0044-1786754","DOIUrl":"10.1055/s-0044-1786754","url":null,"abstract":"Historically, heparin has had the longest historical use as an anticoagulant and continues this day to be the primary therapeutic option for preventing thrombosis and thromboembolism in critically ill hospitalized patients. Heparin is also used to treat sepsis and sepsis-associated disseminated intravascular coagulation (DIC) in various countries. However, the efficacy and safety of heparin for this indication remains controversial, as adequately powered randomized clinical studies have not demonstrated as yet a survival benefit in sepsis and sepsis-associated DIC, despite meta-analyses and propensity analyses reporting improved outcomes without increasing bleeding risk. Further, activated protein C and recombinant thrombomodulin showed greater improvements in outcomes compared with heparin, although these effects were inconclusive. In summary, further research is warranted, despite the ongoing clinical use of heparin for sepsis and sepsis-associated DIC. Based on Japanese guidelines, antithrombin or recombinant thrombomodulin may be a preferable choice if they are accessible.","PeriodicalId":21673,"journal":{"name":"Seminars in thrombosis and hemostasis","volume":" ","pages":"1012-1018"},"PeriodicalIF":3.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140909365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Factor XII Structure-Function Relationships. 因素十二结构-功能关系。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2023-06-05 DOI: 10.1055/s-0043-1769509

Aleksandr Shamanaev, Maxim Litvak, Ivan Ivanov, Priyanka Srivastava, Mao-Fu Sun, S Kent Dickeson, Sunil Kumar, Tracey Z He, David Gailani

{"title":"Factor XII Structure-Function Relationships.","authors":"Aleksandr Shamanaev, Maxim Litvak, Ivan Ivanov, Priyanka Srivastava, Mao-Fu Sun, S Kent Dickeson, Sunil Kumar, Tracey Z He, David Gailani","doi":"10.1055/s-0043-1769509","DOIUrl":"10.1055/s-0043-1769509","url":null,"abstract":"Factor XII (FXII), the zymogen of the protease FXIIa, contributes to pathologic processes such as bradykinin-dependent angioedema and thrombosis through its capacity to convert the homologs prekallikrein and factor XI to the proteases plasma kallikrein and factor XIa. FXII activation and FXIIa activity are enhanced when the protein binds to a surface. Here, we review recent work on the structure and enzymology of FXII with an emphasis on how they relate to pathology. FXII is a homolog of pro-hepatocyte growth factor activator (pro-HGFA). We prepared a panel of FXII molecules in which individual domains were replaced with corresponding pro-HGFA domains and tested them in FXII activation and activity assays. When in fluid phase (not surface bound), FXII and prekallikrein undergo reciprocal activation. The FXII heavy chain restricts reciprocal activation, setting limits on the rate of this process. Pro-HGFA replacements for the FXII fibronectin type 2 or kringle domains markedly accelerate reciprocal activation, indicating disruption of the normal regulatory function of the heavy chain. Surface binding also enhances FXII activation and activity. This effect is lost if the FXII first epidermal growth factor (EGF1) domain is replaced with pro-HGFA EGF1. These results suggest that FXII circulates in blood in a \"closed\" form that is resistant to activation. Intramolecular interactions involving the fibronectin type 2 and kringle domains maintain the closed form. FXII binding to a surface through the EGF1 domain disrupts these interactions, resulting in an open conformation that facilitates FXII activation. These observations have implications for understanding FXII contributions to diseases such as hereditary angioedema and surface-triggered thrombosis, and for developing treatments for thrombo-inflammatory disorders.","PeriodicalId":21673,"journal":{"name":"Seminars in thrombosis and hemostasis","volume":" ","pages":"937-952"},"PeriodicalIF":3.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10696136/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9577462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

2024 Eberhard F. Mammen Award Announcements: Part I-Most Popular Articles. 2024 年埃伯哈德-F-马门奖公告：第一部分-最受欢迎的文章。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2024-03-08 DOI: 10.1055/s-0044-1782197

Emmanuel J Favaloro

引用次数: 0

Plasma Kallikrein as a Forgotten Clotting Factor. 血浆 Kallikrein 是一种被遗忘的凝血因子。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2023-04-18 DOI: 10.1055/s-0043-57034

Katherine J Kearney, Henri M H Spronk, Jonas Emsley, Nigel S Key, Helen Philippou

{"title":"Plasma Kallikrein as a Forgotten Clotting Factor.","authors":"Katherine J Kearney, Henri M H Spronk, Jonas Emsley, Nigel S Key, Helen Philippou","doi":"10.1055/s-0043-57034","DOIUrl":"10.1055/s-0043-57034","url":null,"abstract":"For decades, it was considered that plasma kallikrein's (PKa) sole function within the coagulation cascade is the activation of factor (F)XII. Until recently, the two key known activators of FIX within the coagulation cascade were activated FXI(a) and the tissue factor-FVII(a) complex. Simultaneously, and using independent experimental approaches, three groups identified a new branch of the coagulation cascade, whereby PKa can directly activate FIX. These key studies identified that (1) FIX or FIXa can bind with high affinity to either prekallikrein (PK) or PKa; (2) in human plasma, PKa can dose dependently trigger thrombin generation and clot formation independent of FXI; (3) in FXI knockout murine models treated with intrinsic pathway agonists, PKa activity results in increased formation of FIXa:AT complexes, indicating direct activation of FIX by PKa in vivo. These findings suggest that there is both a canonical (FXIa-dependent) and non-canonical (PKa-dependent) pathway of FIX activation. These three recent studies are described within this review, alongside historical data that hinted at the existence of this novel role of PKa as a coagulation clotting factor. The implications of direct PKa cleavage of FIX remain to be determined physiologically, pathophysiologically, and in the context of next-generation anticoagulants in development.","PeriodicalId":21673,"journal":{"name":"Seminars in thrombosis and hemostasis","volume":" ","pages":"953-961"},"PeriodicalIF":3.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10000934","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Substrates, Cofactors, and Cellular Targets of Coagulation Factor XIa. 凝血因子 XIa 的底物、辅因子和细胞靶标

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2023-03-20 DOI: 10.1055/s-0043-1764469

André L Lira, Tia C L Kohs, Samantha A Moellmer, Joseph J Shatzel, Owen J T McCarty, Cristina Puy

{"title":"Substrates, Cofactors, and Cellular Targets of Coagulation Factor XIa.","authors":"André L Lira, Tia C L Kohs, Samantha A Moellmer, Joseph J Shatzel, Owen J T McCarty, Cristina Puy","doi":"10.1055/s-0043-1764469","DOIUrl":"10.1055/s-0043-1764469","url":null,"abstract":"Coagulation factor XI (FXI) has increasingly been shown to play an integral role in several physiologic and pathological processes. FXI is among several zymogens within the blood coagulation cascade that are activated by proteolytic cleavage, with FXI converting to the active serine protease form (FXIa). The evolutionary origins of FXI trace back to duplication of the gene that transcribes plasma prekallikrein, a key factor in the plasma kallikrein-kinin system, before further genetic divergence led to FXI playing a unique role in blood coagulation. While FXIa is canonically known for activating the intrinsic pathway of coagulation by catalyzing the conversion of FIX into FIXa, it is promiscuous in nature and has been shown to contribute to thrombin generation independent of FIX. In addition to its role in the intrinsic pathway of coagulation, FXI also interacts with platelets, endothelial cells, and mediates the inflammatory response through activation of FXII and cleavage of high-molecular-weight kininogen to generate bradykinin. In this manuscript, we critically review the current body of knowledge surrounding how FXI navigates the interplay of hemostasis, inflammatory processes, and the immune response and highlight future avenues for research. As FXI continues to be clinically explored as a druggable therapeutic target, understanding how this coagulation factor fits into physiological and disease mechanisms becomes increasingly important.","PeriodicalId":21673,"journal":{"name":"Seminars in thrombosis and hemostasis","volume":" ","pages":"962-969"},"PeriodicalIF":3.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11069399/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9342316","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Targeting the Contact Pathway of Coagulation for the Prevention and Management of Medical Device-Associated Thrombosis. 以凝血接触途径为目标，预防和处理医疗器械相关血栓。

IF 3.6 2区医学

Seminars in thrombosis and hemostasis Pub Date : 2024-10-01 Epub Date: 2023-04-12 DOI: 10.1055/s-0043-57011

Abhishek Goel, Harsha Tathireddy, Si-Han Wang, Helen H Vu, Cristina Puy, Monica T Hinds, David Zonies, Owen J T McCarty, Joseph J Shatzel

{"title":"Targeting the Contact Pathway of Coagulation for the Prevention and Management of Medical Device-Associated Thrombosis.","authors":"Abhishek Goel, Harsha Tathireddy, Si-Han Wang, Helen H Vu, Cristina Puy, Monica T Hinds, David Zonies, Owen J T McCarty, Joseph J Shatzel","doi":"10.1055/s-0043-57011","DOIUrl":"10.1055/s-0043-57011","url":null,"abstract":"Hemorrhage remains a major complication of anticoagulants, with bleeding leading to serious and even life-threatening outcomes in rare settings. Currently available anticoagulants target either multiple coagulation factors or specifically coagulation factor (F) Xa or thrombin; however, inhibiting these pathways universally impairs hemostasis. Bleeding complications are especially salient in the medically complex population who benefit from medical devices. Extracorporeal devices-such as extracorporeal membrane oxygenation, hemodialysis, and cardiac bypass-require anticoagulation for optimal use. Nonetheless, bleeding complications are common, and with certain devices, highly morbid. Likewise, pharmacologic prophylaxis to prevent thrombosis is not commonly used with many medical devices like central venous catheters due to high rates of bleeding. The contact pathway members FXI, FXII, and prekallikrein serve as a nexus, connecting biomaterial surface-mediated thrombin generation and inflammation, and may represent safe, druggable targets to improve medical device hemocompatibility and thrombogenicity. Recent in vivo and clinical data suggest that selectively targeting the contact pathway of coagulation through the inhibition of FXI and FXII can reduce the incidence of medical device-associated thrombotic events, and potentially systemic inflammation, without impairing hemostasis. In the following review, we will outline the current in vivo and clinical data encompassing the mechanism of action of drugs targeting the contact pathway. This new class of inhibitors has the potential to herald a new era of effective and low-risk anticoagulation for the management of patients requiring the use of medical devices.","PeriodicalId":21673,"journal":{"name":"Seminars in thrombosis and hemostasis","volume":" ","pages":"989-997"},"PeriodicalIF":3.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11069398/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9295467","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0