DDAVP IN DIABETES INSIPIDUS

1987 ◽  
Author(s):  
V Vicente ◽  
J Corrales ◽  
J Miralles ◽  
I Alberca
Keyword(s):  
Factor Viii ◽  
Diabetes Insipidus ◽  
Von Willebrand Factor ◽  
Therapeutic Dose ◽  
Healthy Subjects ◽  
Tissue Plasminogen ◽  
Patients With Diabetes ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Cranial Diabetes Insipidus

In order to investigate whether the response of von Willebrand factor (vWF), Factor VIII (FVIII) and tissue plasminogen activator (t-PA) to DDAVP infusion is governed by the integrity of the hypothaLamo neurohypophyseal axis, we studied the behaviours >of these proteins (FVIII, one stage; vWF antigen by electroimmunoassay and t-PA was measured in the plasma auglobulin fraction with added C-1 inactivator on fibrin plates) after DDAVP infusion (0.3 ug/Kg) in five patients with cranial diabetes insipidus, comparing them with the responses obtained in six healthy subjects.In spite of receiving a daily therapeutic dose of 10-20 ug of DDAVP the patients with diabetes insipidus showed normal basal levels of FVIII, vWF and t-PA. The increase in these parameters following DDAVP infusion were not significantly different in the two groups. These findings suggest that the integrity of the hypothalamo-hypophyseal axis is not neccessary for a response by vWF, FVIII and t-PA to occur after DDAVP infusion.

Factor VIII Inhibitor Antibodies with C2 Domain Specificity Are Less inhibitory to Factor VIII Complexed with von Willebrand Factor

1996 ◽  
Vol 76 (05) ◽  
pp. 749-754 ◽  
Author(s):  
Suzuki Suzuki ◽  
Morio Arai ◽  
Kagehiro Amano ◽  
Kazuhiko Kagawa ◽  
Katsuyuki Fukutake
Keyword(s):  
Complex Formation ◽  
Factor Viii ◽  
Von Willebrand Factor ◽  
Domain Specificity ◽  
Factor Viii Inhibitor ◽  
C2 Domain ◽  
Recombinant Fviii ◽  
Von Willebrand ◽  
A2 Domain ◽  
Willebrand Factor

SummaryIn order to clarify the potential role of von Willebrand factor (vWf) in attenuating the inactivation of factor VIII (fVIII) by those antibodies with C2 domain specificity, we investigated a panel of 14 human antibodies to fVIII. Immunoblotting analysis localized light chain (C2 domain) epitopes for four cases, heavy chain (A2 domain) epitopes in five cases, while the remaining five cases were both light and heavy chains. The inhibitor titer was considerably higher for Kogenate, a recombinant fVIII concentrate, than for Haemate P, a fVIII/vWf complex concentrate, in all inhibitor plasmas that had C2 domain specificity. In five inhibitor plasmas with A2 domain specificity and in five with both A2 and C2 domain specificities, Kogenate gave titers similar to or lower than those with Haemate P. The inhibitory effect of IgG of each inhibitor plasma was then compared with recombinant fVIII and its complex with vWf. When compared to the other 10 inhibitor IgGs, IgG concentration, which inhibited 50% of fVIII activity (IC50), was remarkably higher for the fVIII/vWf complex than for fVIII in all the inhibitor IgGs that had C2 domain reactivity. Competition of inhibitor IgG and vWf for fVIII binding was observed in an ELISA system. In 10 inhibitors that had C2 domain reactivity, the dose dependent inhibition of fVIII-vWf complex formation was observed, while, in the group of inhibitors with A2 domain specificity, there was no inhibition of the complex formation except one case. We conclude that a subset of fVIII inhibitors, those that bind to C2 domain determinants, are less inhibitory to fVIII when it is complexed with vWf that binds to overlapping region in the C2 domain.

Molecular Biology of Factor VIII/von Willebrand Factor

1978 ◽  
Vol 40 (02) ◽  
pp. 245-251 ◽  
Author(s):  
D Meyer ◽  
P A Mc Kee ◽  
L W Hoyer ◽  
T S Zimmerman ◽  
H R Gralnick
Keyword(s):  
Molecular Biology ◽  
Factor Viii ◽  
Von Willebrand Factor ◽  
Von Willebrand ◽  
Willebrand Factor
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