Studies on the Antithrombin and Heparin Co-factor Activities of a Fraction Adsorbed from Plasma by Aluminum Hydroxide

Monkhouse, Frank C.; Seegers, Walter H.

doi:10.1161/01.res.3.4.397

Cited by 92 publications

(25 citation statements)

References 4 publications

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“…The observation that thrombin splits the methylester linkage of p-toluensulphonyl-arginin-methylester (TAMe) (15) was first utilized in an At-III assay by Monkhouse et al (16) in 1955. TAMe has a relatively low thrombin suscepti bility, and was not well-suited for routine use.…”

Section: Assay Methods With Synthetic Substratesmentioning

confidence: 99%

Antithrombin III: Critical Review of Assay Methods

Ödegård¹,

Abildgaard²

1978

Pathophysiol Haemos Thromb

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Thrombin or factor Xa added to plasma are inactivated by antithrombin III (At-III). The inactivation is accelerated by heparin, permitting assay systems which rapidly measure the At-III content of diluted plasma. Without heparin, the slow inactivation rates may be measured. Existing activity assays (fibrinogen or chromogenic substrates) and immunoassays of At-III have been reviewed. Correlation studies show a close correlation between the results of immunoassay and the results of most activity assays. In health, a narrow range of At-III has been found. The level is low in infancy. Fertile women have on the average somewhat lower levels than men. In old age, the level tends to drop. In clinical material studied with amidolytic assays, subnormal At-III levels were found in hereditary deficiency, liver disease, disseminated intravascular coagulation and in some cases with acute thrombosis. The amidolytic assays are rapid to perform, do not require experience in clotting technique and seem preferable in clinical routine work.

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Section: Assay Methods With Synthetic Substratesmentioning

confidence: 99%

Antithrombin III: Critical Review of Assay Methods

Ödegård¹,

Abildgaard²

1978

Pathophysiol Haemos Thromb

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“…[52][53][54] The recognition that heparin required a plasma cofactor for its full anticoagulant effect led to the identification of what was later called antithrombin III, and now just antithrombin. 50,55 The lysis of blood clots was recognized in antiquity, and in 1893 Dastre in France gave the term "fibrinolysis" to the effect of serum in lysing fibrin. 56 In 1933, Tillett and Garner in Baltimore identified a fibrinolysin in streptococcal lysates, and studies of the plasma cofactor required for this "streptokinase" activity led to its identification by Kaplan in North Carolina as plasminogen in 1944.…”

Section: Brief Histories Of Select Topics In Hematologymentioning

confidence: 99%

Blood at 70: its roots in the history of hematology and its birth

Coller

2015

Blood

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This year we celebrate Blood's 70th year of publication. Created from the partnership of the book publisher Henry M. Stratton and the prominent hematologist Dr William Dameshek of Tufts School of Medicine, Blood has published many papers describing major advances in the science and clinical practice of hematology. Blood's founding antedated that of the American Society of Hematology (ASH) by more than 11 years and Stratton and Dameshek helped galvanize support for the creation of ASH. In this review, I place the birth of Blood in the context of the history of hematology before 1946, emphasizing the American experience from which it emerged, and focusing on research conducted during World War II. I also provide a few milestones along Blood's 70 years of publication, including: the growth in Blood's publications, the evolution of its appearance, the countries of submission of Blood papers, current subscriptions to Blood, and the evolution of topics reported in Blood's papers. The latter provides a snapshot of the evolution of hematology as a scientific and clinical discipline and the introduction of new technology to study blood and bone marrow. Detailed descriptions of the landmark discoveries reported in Blood will appear in later papers celebrating Blood's birthday authored by past Editors-in-Chief.

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“…Work by several investigators in the 1950's [29,32,51] suggested the similarity of plasma antithrombin activity and plasma heparin cofactor activity. It was shown that heparin acted to accelerate the interaction between antithrombin and thrombin 50-100 fold.…”

Section: Intrinsic Coagulation Pathwaymentioning

confidence: 99%

Plasma Inhibitors of The Hageman Factor Dependent Pathways

Schreiber¹

2008

Semin Thromb Hemost

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Activation of Hageman factor is initiated by negatively charged surfaces which may be provided by several biologic substances [20,28,35,53]. Activation of Hageman factor results in the initiation of three plasma protein systems: the kinin generation system [30,52], the fibrinolytic sequence [21,36], and the intrinsic pathway of coagulation [41]. Bradykinin generation results from the action of activated Hageman factor or its fragments on prekallikrein, generating kallikrein [23] which cleaves the active peptide bradykinin from kininogen, an alpha-glycoprotein. Bradykinin both enhances vascular permeability and produces peripheral vasodilation and, therefore, is important in the inflammatory response. Similarly, Hageman factor or its fragments activate the fibrinolytic sequence by converting the plasminogen proactivator to the plasminogen activator [24,26]. This active molecule then converts plasminogen to plasmin, the active fibrinolytic enzyme in man. The third plasma protein system initiated by the activation of Hageman factor is the intrinsic pathway of coagulation. Activated Hageman factor converts pre-plasma thromboplastin antecedent (pre-PTA) to its active form PTA (the 11th clotting factor) [41], which then activates factor IX in the coagulation sequence. Thus, the contribution of Hageman factor activation to tissue injury is not merely limited to the initiation of coagulation by activation of factor XI, but includes activation of prekallikrein to achieve bradykinin generation and activation of plasminogen proactivator in order to form plasmin. In addition, two enzymes activated in these sequences, kallikrein and plasminogen activator, also function in neutrophil chemotaxis [25,27]. Subsequent interactions may also generate biologically active products from the complement system, as well, primarily via the action of plasmin on C1, the first component of complement [42], and on C3, the third component of complement [33]. Thus, the activation of Hageman factor by immunologic or nonimmunologic events introduces coagulation and fibrinolysis, augments leukocyte chemotaxis and results in enhanced vascular permeability. Therefore, regulation and control of these biologically active products resulting from Hageman factor activation are critical to modulating the effects of tissue injury. In this section we will discuss the circulating plasma factors which appear operative in regulating the biologic activity of these pathways. We will discuss each of the Hageman factor dependent systems in sequence.

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Studies on the Antithrombin and Heparin Co-factor Activities of a Fraction Adsorbed from Plasma by Aluminum Hydroxide

Cited by 92 publications

References 4 publications

Antithrombin III: Critical Review of Assay Methods

Antithrombin III: Critical Review of Assay Methods

Blood at 70: its roots in the history of hematology and its birth

Plasma Inhibitors of The Hageman Factor Dependent Pathways

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