Low von Willebrand Factor in Children and Adolescents

Author(s):  
Lakshmi Srivaths ◽  
Peter A. Kouides
2021 ◽  
Vol 100 (3) ◽  
pp. 47-53
Author(s):  
M.M. Tсvetkova ◽  
◽  
L.M. Minkina ◽  
O.E. Aliyeva ◽  
A.A. Kravchuk ◽  
...  

The aim of the study is to identify the features of the anamnesis and laboratory characteristics of children and adolescents with platelet pathology. Materials and methods of research: the features of medical history and laboratory characteristics of children and adolescents aged 1 to 17 years with platelet pathology (thrombocytopenia and thrombocytopathy) were studied based on the analysis of 112 medical records of inpatients. Study design: retrospective, single-center, solid, non-randomized, uncontrolled. Results: when comparing parameters of the indicated nosological groups, a higher viral load was revealed in children with thrombocytopenia (level of antibodies to the herpesvirus group was statistically significantly higher in children with thrombocytopenia than with thrombocytopathy: for HSV1,2 and VEB – p<0,001, CMV – p=0,008). According to hemostasiogram, APTT was statistically significantly higher in the thrombocytopathy group (29,56±2,18 s versus 28,44±1,62 s respectively, p=0,0011), the prothrombin time was higher in thrombocytopenia (12,37±0,72 s and 12,03±0,48 s, respectively, p=0,014). The activity of von Willebrand factor is statistically significantly higher in thrombocytopenia compared with thrombocytopathy (123,78±36,35% versus 79,73±35,21%, respectively, p<0,001). A positive correlation between the relative number of platelets and leukocytes (Rs=0,40, p<0,001) has been established in the group of children with thrombocytopathy. Conclusion: the differences and dependencies identified indicate the inclusion of compensatory mechanisms of hemostasis regulation and immune protection in platelet pathology, which is more pronounced with decrease in their number.


Transfusion ◽  
2010 ◽  
Vol 50 (7) ◽  
pp. 1571-1580 ◽  
Author(s):  
Dieter Klarmann ◽  
Christine Eggert ◽  
Christof Geisen ◽  
Sabine Becker ◽  
Erhard Seifried ◽  
...  

1986 ◽  
Vol 55 (02) ◽  
pp. 276-278 ◽  
Author(s):  
F Brosstad ◽  
Inge Kjønniksen ◽  
B Rønning ◽  
H Stormorken

SummaryA method for visualization of the multimeric forms of von Willebrand Factor (vWF) in plasma and platelets is described. The method is based upon: 1) Separation of the vWF multimers by SDS-agarose electrophoresis, 2) Subsequent blotting of the vWF multimers onto nitrocellulose, 3) Immunolocalization and visualization of the vWF pattern by the sequential incubation of the blot with a) primary vWF antiserum, b) peroxidase- or beta-galactosidase-conjugated secondary antibodies and a relevant chromogenic substrate.


1988 ◽  
Vol 60 (02) ◽  
pp. 182-187 ◽  
Author(s):  
Morio Aihara ◽  
Ken Tamura ◽  
Ryuko Kawarada ◽  
Keizou Okawa ◽  
Yutaka Yoshida

SummaryThe adhesion of human fixed washed platelets (FWP) to collagen was decreased after treatment with Serratia marcescens protease (SP), which removed 95% of the glycocalicin from platelet membrane glycoprotein (GP) lb. However, the diminished adhesion of SP treated FWP to collagen could still be increased in the presence of purified von Willebrand factor (vWF). This ability of vWF to increase FWP adhesion to collagen is defined as collagen cofactor (CCo). The adhesion of FWP to collagen was not affected by a monoclonal antibody (MAb) to GP Ilb/IIIa (10E5), that inhibits ADP and collagen induced platelet aggregation. On the other hand, it was decreased by 50% by a MAb to GP lb (6D1), that inhibits ristocetin induced platelet aggregation. Adhesion of FWP in buffer to collagen was completely inhibited by Ricinus communis agglutinin I or concanavalin A, while Lens culinalis agglutinin and wheat germ agglutinin showed 50% inhibition. The FWP adhesion to collagen in the presence of vWF (normal plasma) was unaffected by MAbs to GP Ilb/IIIa (10E5, P2, HPL1) but was decreased to 32-38% by MAbs to GP lb (6D1, AN51, HPL11). A MAb to vWF (CLB-RAg 35), that inhibits ristocetin induced binding of vWF to platelets, decreased the CCo of normal plasma by 70%. The MAb, CLB-RAg 201, that inhibits the binding of vWF to collagen, completely inhibited the CCo of normal plasma. In conclusion, our data suggest that (1) GP lb has a partial role in FWP adhesion to collagen; (2) the binding of vWF to collagen is required for the expression of CCo; (3) CCo is partly mediated through GP lb; but (4) other platelet membrane protein(s) besides GP lb or GP Ilb/IIIa must also be involved in FWP-vWF-collagen interactions.


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