Progress in hemostasis and thrombosis最新文献

{"title":"The platelet glycoprotein Ib-IX complex.","authors":"Z M Ruggeri","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"10 ","pages":"35-68"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13009959","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Platelet IgG: measurement, interpretation, and clinical significance.","authors":"J N George","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Platelet IgG has been studied primarily to develop an aid for clinical diagnosis--a search that has proven elusive (48). However, studies of the interaction of IgG and other plasma proteins with platelets have provided new insight into the intracellular pathways for the acquisition of proteins into regulated secretory granules. From a clinical perspective, it is important not to make the assumption that all platelet IgG is antiplatelet antibody. Data on platelet IgG must be distinguished between measurements of alpha-granule IgG, which comprises almost all of the total platelet IgG content, and platelet surface IgG, representing less than 1 percent of total platelet IgG. alpha-granule IgG does not appear to be antiplatelet antibody; platelet surface IgG is likely to be at least partly antiplatelet antibody. The total platelet (alpha-granule) content of IgG mirrors the concentration and composition of plasma IgG. It is increased in patients with hypergammaglobulinemia of any cause and absent in agammaglobulinemia. The platelet alpha-granule content of IgG, IgA, and albumin is proportional to their concentrations in plasma, and the platelet content of IgG, IgA and albumin also reflects their plasma concentration over a wide range of plasma abnormalities. These observations suggest that platelets acquire IgG, IgA, and albumin by fluid phase endocytosis. Total platelet IgG is consistently increased in patients with ITP and is also commonly increased in patients with thrombocytopenia due to increased platelet destruction of apparently nonimmune mechanisms. The total platelet IgG content does not appear to be increased in patients who have thrombocytopenia due to marrow failure. Therefore, the measurement of total platelet IgG may be analogous to the reticulocyte count, which is increased in patients who have accelerated erythropoiesis caused by either immune or nonimmune hemolytic anemia. The increased concentration of total platelet IgG in patients with ITP is parallel to the appearance of larger platelets produced during the stress of increased thrombopoietic stimulation. Therefore, determinations of mean platelet volume may yield clinical information equivalent to the measurement of total platelet IgG. The concentration of platelet surface IgG is greatly increased in patients with ITP, and concentrations are highest in patients with the most acute ITP. Platelet surface IgG may represent antiplatelet antibody in these patients. However, for unknown reasons, modest elevations of platelet surface IgG are found in many patients with nonimmune thrombocytopenia.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"10 ","pages":"97-126"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13166521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fibrinogen and factor VII as risk factors in vascular disease.","authors":"M B Hultin","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"10 ","pages":"215-41"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13166515","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The lipoprotein-associated coagulation inhibitor.","authors":"G J Broze,&nbsp;T J Girard,&nbsp;W F Novotny","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>TF mediated initiation of coagulation appears to play a critical role in normal hemostasis and probably pathologic thrombosis as well. Although teleological considerations would seem to suggest that a specific regulator of this process should exist, and although the presence in plasma of such an inhibitor was documented many years ago, it was not until the past five years that the inhibitor was characterized and its mechanism of action defined. LACI produces factor Xa-dependent feedback initiation of the VIIa/TF catalytic complex. The mechanism of this feedback inhibition is novel. First, LACI, a multi-headed protease inhibitor, binds factor Xa, a product of VIIa/TF catalysis, at one of its inhibitory domains. The Xa-LACI complex, possibly acting as a pseudosubstrate, then is able to bind to VIIa/TF in an appropriate conformation such that a second inhibitory domain of LACI is positioned to interact with factor VIIa in the VIIa/TF complex. Whether such a unique means of eliciting feedback inhibition in a protease cascade is repeated in nature is unknown. The existence of LACI appears to help explain the clinical need for both \"extrinsic\" and \"intrinsic\" coagulation pathways. In addition, data to the present are consistent with the notion that, in normal hemostasis at least, TF is responsible for an initial burst of factor Xa generation which provides sufficient thrombin to induce the aggregation of platelets and the activation of the critical coagulation cofactors factor V and factor VIII. Ultimate and persistent hemostasis, however, appears to require the continued production of additional factor Xa through the action of factor IXa and factor VIII. The fact that patients with factor XI deficiency suffers a variable but usually mild bleeding diathesis suggests that under certain conditions the initial burst of factor IXa formed through the action of VIIa/TF is insufficient and supplemental factor IXa generated by factor XIa is needed for normal hemostasis. The mechanism by which this factor XIa is generated in vivo, however, has not been determined. We stress that the predicted in vivo role of LACI is simply that--a prediction based on its known in vitro properties. Documentation of its physiologic importance remains to be provided and is an area of active research. Further, although significant progress has been made over the past few years in the characterization of LACI, many questions remain unanswered. For example: What is the mechanism for LACI's association with lipoproteins in plasma? What function, if any, does the third Kunitz-type protease inhibitor domain in LACI serve? (ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"10 ","pages":"243-68"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13166517","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular and cellular biology of von Willebrand factor.","authors":"R I Handin,&nbsp;D D Wagner","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"9 ","pages":"233-59"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13785018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cellular adhesion: GPIIb-IIIa as a prototypic adhesion receptor.","authors":"E F Plow,&nbsp;M H Ginsberg","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"9 ","pages":"117-56"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13785015","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anticoagulant therapy for venous thromboembolism.","authors":"G E Raskob,&nbsp;C J Carter,&nbsp;R D Hull","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"9 ","pages":"1-27"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13785014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Type 1 plasminogen activator inhibitor.","authors":"D J Loskutoff,&nbsp;M Sawdey,&nbsp;J Mimuro","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"9 ","pages":"87-115"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13636481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The alloimmune thrombocytopenias: neonatal alloimmune thrombocytopenic purpura and post-transfusion purpura.","authors":"T J Kunicki,&nbsp;D S Beardsley","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"9 ","pages":"203-32"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13785017","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Thrombospondin: phenomenology to function.","authors":"A S Asch,&nbsp;R L Nachman","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Since the initial description of thrombospondin in 1971, our knowledge of the protein has reached a point where some understanding of its physiologic and pathologic roles has accrued. Thrombospondin is a multifunctional glycoprotein whose demonstrated affinities for multiple ligands make it a versatile molecule that can participate in mediating or modulating cell adhesion, fibrin polymerization, fibrinolysis, and development. The recently defined primary structure will make an understanding of the functional aspects of this molecule more accessible, and the next several years promises to define the role of thrombospondin in human biology.</p>","PeriodicalId":76372,"journal":{"name":"Progress in hemostasis and thrombosis","volume":"9 ","pages":"157-76"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13611958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}