scholarly journals Interaction between human tissue thromboplastin and human antithrombin III.

1989 ◽  
Vol 37 (11) ◽  
pp. 2984-2987 ◽  
Author(s):  
Keizo HIRAHARA ◽  
Tetsuro MATSUISHI ◽  
Nobuo SUZUKI ◽  
Munetsugu KURATA
Keyword(s):  
Human Tissue ◽  
Antithrombin Iii ◽  
Tissue Thromboplastin

Tissue Thromboplastin Induced Reversible DIC and Heparin-Enhanced Inhibitors in Dogs

1986 ◽  
Vol 55 (01) ◽  
pp. 078-085 ◽  
Author(s):  
German A Marbet ◽  
Michael J Griffith
Keyword(s):  
Antithrombin Iii ◽  
Ex Vivo ◽  
Order Rate Constant ◽  
Thrombin Inhibitors ◽  
Heparin Cofactor Ii ◽  
First Order ◽  
Tissue Thromboplastin ◽  
Pseudo First Order ◽  
Homologous Tissue

SummaryReversible acute disseminated intravascular coagulation (DIC) has been induced in dogs by intravenous injection of homologous tissue thromboplastin. There was no measurable consumption of antithrombin III and heparin cofactor II even if fibrinogen was reduced during DIC by more than 80% of its baseline. The prothrombin level remained practically constant. These data correspond to the generation of a few nanomoles of thrombin in vivo with subsequent pseudo-first order inactivation by the major thrombin inhibitors. An ex vivo measure of the pseudo-first order rate constant (dynamic thrombin inhibitory capacity, DTIC) was a sensitive probe of circulating heparin. There was no change of DTIC during DIC in the absence of exogenous heparin suggesting that heparin-like endogenous glycosaminoglycans were not released in substantial amounts. Pretreatment with heparin efficiently inhibited the development of tissue thromboplastin induced DIC. This animal model may serve as a tool for the study of glycosaminoglycan anticoagulants in vivo.

scholarly journals Synergistic effect of antithrombin III, activated protein C and heparin on the inhibition of the tissue thromboplastin-mediated coagulation.

1989 ◽  
Vol 37 (3) ◽  
pp. 692-696 ◽  
Author(s):  
Keizo HIRAHARA ◽  
Yuko ETOH ◽  
Tetsuro MATSUISHI ◽  
Nobuo SUZUKI ◽  
Munetsugu KURATA
Keyword(s):  
Synergistic Effect ◽  
Protein C ◽  
Antithrombin Iii ◽  
Activated Protein C ◽  
Tissue Thromboplastin

Antithrombin III Concentrates

1992 ◽  
Vol 6 (5) ◽  
pp. 1115-1120 ◽  
Author(s):  
Doris Menache
Keyword(s):  
Antithrombin Iii

Unterarmgangrän und Hirninfarkt bei „normaler“ Gerinnung: Homozygoter Antithrombin III – Mangel Typ II (Budapest)

2010 ◽  
Vol 222 (S 01) ◽  
Author(s):  
M Blohm ◽  
K Lehmberg ◽  
G Hillebrand ◽  
A Neu ◽  
I Ridderbusch ◽  
...  
Keyword(s):  
Antithrombin Iii

Molekularbiologische Grundlagen und Diagnostik der hereditären Defekte von Antithrombin III, Protein C und Protein S

2002 ◽  
Vol 22 (02) ◽  
pp. 57-66
Author(s):  
I. Witt
Keyword(s):  
Protein C ◽  
Antithrombin Iii ◽  
Protein S ◽  
Klinische Relevanz ◽  
At Iii

ZusammenfassungDie enormen Fortschritte in der Molekularbiologie in den letzten Jahren ermöglichten sowohl die Aufklärung der Nukleotidsequenzen der Gene für Antithrombin III (AT III), Protein C (PROC) und Protein S (PROS) als auch die Identifizierung zahlreicher Mutationen bei hereditären Defekten dieser wichtigen Inhibitoren des plasmatischen Gerinnungssystems. Da die Gene für AT III (13,8 kb) und PROC (11,2 kb) nicht groß und relativ leicht zu analysieren sind, gibt es bereits umfangreiche »databases« der Mutationen (50, 73). Für AT III sind 79 und für PROC 160 unterschiedliche Mutationen beschrieben.Sowohl beim AT-III-Mangel als auch beim Protein-C-Mangel hat die Mutationsaufklärung neue Erkenntnisse über die Struktur-Funktions-Beziehung der Proteine gebracht. Beim Protein-C-Mangel steht die klinische Relevanz der DNA-Analyse im Vordergrund, da die Diagnostik des Protein-C-Mangels auf der Proteinebene nicht immer zuverlässig möglich ist.Das Protein-S-Gen ist für die Analytik schwer zugänglich, da es groß ist (80 kb) und außerdem ein Pseudogen existiert. Es sind schon zahlreiche Mutationen bei Patienten mit Protein-S-Mangel identifiziert worden. Eine Database ist bisher nicht publiziert. Die klinische Notwendigkeit zur Mutationsaufklärung besteht ebenso wie beim Protein-C-Mangel. Es ist zu erwarten, dass zukünftig die Identifizierung von Mutationen auch beim Protein-S-Mangel beschleunigt vorangeht.

The Frequency of Type I Heterozygous Protein S and Protein C Deficiency in 141 Unrelated Young Patients with Venous Thrombosis

1988 ◽  
Vol 59 (01) ◽  
pp. 018-022 ◽  
Author(s):  
C L Gladson ◽  
I Scharrer ◽  
V Hach ◽  
K H Beck ◽  
J H Griffin
Keyword(s):  
Venous Thrombosis ◽  
Protein C ◽  
Antithrombin Iii ◽  
Young Patients ◽  
Protein S ◽  
Type I ◽  
Protein S Deficiency ◽  
Protein C Deficiency ◽  
Low Protein ◽  
S Deficiency

SummaryThe frequency of heterozygous protein C and protein S deficiency, detected by measuring total plasma antigen, in a group (n = 141) of young unrelated patients (<45 years old) with venous thrombotic disease was studied and compared to that of antithrombin III, fibrinogen, and plasminogen deficiencies. Among 91 patients not receiving oral anticoagulants, six had low protein S antigen levels and one had a low protein C antigen level. Among 50 patients receiving oral anticoagulant therapy, abnormally low ratios of protein S or C to other vitamin K-dependent factors were presented by one patient for protein S and five for protein C. Thus, heterozygous Type I protein S deficiency appeared in seven of 141 patients (5%) and heterozygous Type I protein C deficiency in six of 141 patients (4%). Eleven of thirteen deficient patients had recurrent venous thrombosis. In this group of 141 patients, 1% had an identifiable fibrinogen abnormality, 2% a plasminogen abnormality, and 3% an antithrombin III deficiency. Thus, among the known plasma protein deficiencies associated with venous thrombosis, protein S and protein C. deficiencies (9%) emerge as the leading identifiable associated abnormalities.

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