Spinal Cord Stimulator Placement in a Patient with Type 2 von Willebrand’s Disease

Von Willebrand ◽

Willebrand Factor ◽

We present a case of a 76-year-old female with a history of lumbar post-laminectomy pain syndrome and Type II von Willebrand’s disease who underwent successful implantation of a spinal cord stimulator. A consultation with the patient’s hematologist was obtained, and antihemophilic factor/von Willebrand factor complex was administered immediately prior to insertion and removal of trial leads. After reporting greater than 90% pain relief, the patient then underwent permanent implantation with administration of antihemophilic factor/von Willebrand factor complex prior to placement. The epidural space was entered atraumatically, and lead placement was uneventful with minimal resistance met. Leads were tunneled to her right gluteal region, where a pocket was created for her generator. She continues to report good relief without neurological signs of epidural hematoma nearly 6 months post-procedure. Key words: von Willebrand disease, high-frequency spinal cord stimulator, post-laminectomy pain syndrome

The In Vitro Association of Antihemophilic Factor and von Willebrand Factor

10.1055/s-0038-1657311 ◽

1983 ◽

Vol 49 (01) ◽

pp. 037-041 ◽

Cited By ~ 23

Author(s):

M B Zucker ◽

M E Soberano ◽

A J Johnson ◽

A J Fulton ◽

S Kowalski ◽

...

Keyword(s):

Von Willebrand Factor ◽

Ion Concentration ◽

Void Volume ◽

Gel Chromatography ◽

Clotting Factors ◽

Von Willebrand ◽

Willebrand Factor ◽

SummaryConsiderable evidence, including results of gel chromatography, indicates that antihemophilic factor (AHF; factor VIII: C) is associated with von Willebrand factor (vWF; factor VIIIR: RC or VTIIR: Ag) in citrated plasma. The present study was undertaken to determine whether these factors are also associated in plasma with a physiologic calcium ion concentration, or in an artificial medium using purified antihemophilic factor and plasma as a source of vWF. When fresh BaS04-treated native normal plasma was passed through a column of Sepharose CL-4B that was equilibrated and eluted with fresh BaS04-treated plasma from a patient with severe von Willebrand’s disease, the AHF and vWF activities were found in the void volume. Thus, AHF remains associated with vWF on gel chromatography in the presence of physiological concentrations of all plasma constituents except the vitamin-K-dependent clotting factors. On the other hand, when to 200,000 X purified “vWF-free” AHF was chromatographed in buffered 4% albumin with 2 mM CaCl2, virtually all of it appeared in the included volume of the column with an apparent molecular weight between that of fibrinogen or factor V (340,000) and gamma globulin (160,000). The combination of the “vWF-free” AHF with the vWF in plasma was studied by adding the AHF to BaS04-treated plasma from normal subjects or patients with severe hemophilia or von Willebrand’s disease and chromatographing the mixture. The AHF activity appeared in the void volume in an amount that was inversely related to the ratio of the AHF to vWF activity. Thus, with 1-12 U of AHF per unit of vWF, virtually all of the AHF eluted in the void volume, with 30 and 500 units of AHF per unit of vWF, only about 50% and 10% of the AHF, respectively, eluted in the void volume, and in the absence of vWF, none of the AHF activity eluted in the void volume.

Stabilization of the Antihemophilic Factor (VIII :AHF) by the Von Willebrand Factor (VIII :VWF): A Possible Model for Von Willebrand’s Disease

10.1055/s-0039-1680356 ◽

1977 ◽

Author(s):

H. J. Weiss ◽

I. I. Sussman ◽

L. W. Hoyer

Keyword(s):

Factor Viii ◽

Von Willebrand Factor ◽

Crossed Immunoelectrophoresis ◽

Factor Viii Antigen ◽

Von Willebrand ◽

Willebrand Factor ◽

When compared with VIII:AHF in normal citrated plasmas, VIII:AHF activity showed increased lability at 37°C in the ‘late’ post-transfusion plasmas (VIII:AHF≫VIII:VWF) of a patient with von Willebrand’s disease, but not in the ‘early’ post-transfusion plasmas in which VIII:AHF~VIII:VWF. VIII:AHF was also labile in the baseline plasmas of 3 patients with von Willebrand’s disease in whom VIII:AHF≫VIII:VWF. In two of these patients the mobility of Factor VIII antigen (on crossed Immunoelectrophoresis) was increased. (VIII:AHF was not excessively labile in 4 other patients in whom VIII :AHF~VIII:VWF). In all of the above cases, VIII:AHF was stabilized by the addition of either purified von Willebrand factor or plasmas of patients with hemophilia, but not by plasmas of patients with severe von Willebrand’s disease. Thus, VIII:VWF may serve to stabilize VIII:AHF and this might explain the post-transfusion findings in von Willebrand’s disease.

Ins405AsnPro Mutation in the von Willebrand Factor Propeptide in Recessive Type 2A (IIC) von Willebrand’s Disease

10.1055/s-0037-1615051 ◽

1998 ◽

Vol 79 (04) ◽

pp. 718-722 ◽

Cited By ~ 23

Author(s):

D. Karpman ◽

C. Isaksson ◽

A. C. Kristoffersson ◽

S. Lethagen ◽

R. Schneppenheim ◽

...

Keyword(s):

Von Willebrand Factor ◽

De Novo ◽

Duplication Event ◽

Von Willebrand Disease ◽

In Vitro Mutagenesis ◽

Von Willebrand ◽

SummaryThe molecular defects of the von Willebrand factor (vWF) have been studied in the patient in whom the von Willebrand disease phenotype IIC was originally described. A six nucleotide insert, AATCCC, was found in exon 11 of the vWF gene, predicting the insertion of the amino acids asparagine and proline between phenylala-nine 404 and threonine 405 of the vWF propeptide. The mutation was present in one allele. Analysis of amplification products derived from platelet vWF mRNA showed the other allele to be silent. The patient is thus a compound heterozygote for a null allele and the IIC allele, in accord with the recessive mode of inheritance of the IIC phenotype. Family studies indicated the IIC mutation to have occurred de novo, possibly as a result of a duplication event. In vitro mutagenesis and expression in COS-7 cells confirmed the detrimental effect of the mutation on vWF multimer assembly. Taken together with those of earlier studies the present findings suggest that the IIC phenotype may well be exclusively caused by mutations which result in changes of the amino acid sequence in certain regions of the vWF propeptide. Although in the recently revised classification of von Willebrand’s disease variants, the IIC type is included in the 2A category, obviously it constitutes a very distinct subtype.

Properties of the Platelet Retention (von Willebrand) Factor and Its Similarity to the Antihemophilic Factor (AHF)

Blood ◽

10.1182/blood.v41.6.809.809 ◽

1973 ◽

Vol 41 (6) ◽

pp. 809-815 ◽

Cited By ~ 29

Author(s):

Harvey J. Weiss ◽

John Rogers ◽

Harvey Brand

Keyword(s):

Molecular Weight ◽

Von Willebrand Factor ◽

Apparent Molecular Weight ◽

Retention Factor ◽

Void Volume ◽

Von Willebrand ◽

Willebrand Factor ◽

Abstract The abnormal retention of platelets in glass-bead filters in von Willebrand’s disease was corrected by a fraction of normal cryoprecipitate that eluted, along with antihemophilic factor (AHF), in the void volume after chromatography on Bio-Gel 5 M. This platelet retention factor had an apparent molecular weight in excess of 5 x 106, was also present in hemophilic cryoprecipitate, but was not detectable in the void volume fractions of cryoprecipitate prepared from the plasma of a patient with von Willebrand’s disease. The adsorptive and thermal stability properties of the retention (von Willebrand) factor were similar to those of AHF. Platelet retention is the result of a complex interaction between red cells, platelets, and the von Willebrand factor, and it is suggested that the activity of the latter factor may be associated with the same high molecular weight protein that possesses coagulant (AHF) activity in normal subjects but that lacks this activity in hemophiliacs. The deficiency of this protein in von Willebrand’s disease may account for the hemostatic defect in this disorder.

Further Studies on Aggregation of Platelet-Type von Willebrand’s Disease Platelets by Human von Willebrand Factor

10.1055/s-0038-1661559 ◽

1986 ◽

Vol 55 (03) ◽

pp. 338-341 ◽

Cited By ~ 7

Author(s):

H Takahashi ◽

W Tatewaki ◽

M Hanano ◽

R Nagayama ◽

A Shibata

Keyword(s):

Von Willebrand Factor ◽

Ricinus Communis ◽

Divalent Cations ◽

Peanut Agglutinin ◽

Ricinus Communis Agglutinin ◽

Von Willebrand ◽

Induced Aggregation ◽

SummaryPlatelet-type von Willebrand’s disease (vWD) is a bleeding disorder characterized by a heightened interaction between platelets and von Willebrand factor (vWF) as the result of an intrinsic platelet abnormality (probably in GPIb). Platelet aggregability was nearly normal in response to thrombin, wheat germ agglutinin and Ricinus communis agglutinin in this disorder. Unmodified platelets showed no aggregation upon the addition of peanut agglutinin. Partially purified human vWF induced little aggregation of washed patient platelets, but the aggregation was greatly enhanced in the presence of plasma devoid of vWF. Monoclonal antibodies directed against GPIb and GPIIb/IIIa as well as EDTA completely inhibited vWF-induced aggregation. These results indicate that human vWF induces aggregation of platelet-type vWD platelets in the presence of divalent cations and some plasma cofactor(s), and that both GPIb and GPIIb/IIIa are involved in this aggregation.

A de novo mutation in exon 28 of the von Willebrand factor gene in a patient with type IIA von Willebrand's disease coincides with an Mbol polymorphism in the von Willebrand factor pseudogene

Human Molecular Genetics ◽

10.1093/hmg/2.12.2159 ◽

1993 ◽

Vol 2 (12) ◽

pp. 2159-2161 ◽

Cited By ~ 2

Author(s):

Margarita Pérez-Casal ◽

Martina Daly ◽

an Peake

Keyword(s):

Von Willebrand Factor ◽

De Novo ◽

De Novo Mutation ◽

Factor Gene ◽

Von Willebrand ◽

Hyper-responsiveness to DDAVP for patients with type I von Willebrand's disease and normal intra-platelet von Willebrand factor

European Journal Of Haematology ◽

10.1111/j.1600-0609.1988.tb00815.x ◽

2009 ◽

Vol 40 (2) ◽

pp. 163-167 ◽

Cited By ~ 28

Author(s):

F. Rodeghiero ◽

G. Castaman ◽

E. Bona ◽

M. Ruggeri ◽

R. Lombardi ◽

...

Keyword(s):

Von Willebrand Factor ◽

Type I ◽

Von Willebrand ◽

Von Willebrand’s Disease caused by Compound Heterozygosity for a Substitution Mutation (T1156M) in the D3 Domain of the Von Willebrand Factor and a Stop Mutation (Q2470X)

10.1055/s-0037-1613232 ◽

2002 ◽

Vol 88 (09) ◽

pp. 421-426 ◽

Cited By ~ 13

Author(s):

Stefan Lethagen ◽

Christina Isaksson ◽

Charlotta Schaedel ◽

Lars Holmberg

Keyword(s):

Von Willebrand Factor ◽

Null Allele ◽

Dependent Manner ◽

Stop Mutation ◽

Von Willebrand ◽

SummaryHereditary defects of the von Willebrand factor (VWF) gene cause von Willebrand’s disease (VWD) which shows great variability dependent on the nature and location of the mutation. We here describe the characteristics of a substitution of methionine for threonine 1156 in the D3 domain of the VWF, i.e. the domain involved in the intracellular multimerization of pro-VWF dimers. A VWD patient with severe symptoms was a compound heterozygote for the T1156M mutation and a null allele (Q2470X) on the other chromosome. This led to marked reduction of plasma VWF concentration to about 0.05 U/ml and an abnormality of VWF multimers as in type 2A VWD. Expression in vitro of the mutation demonstrated that 1156M-VWF is secreted from COS-7 cells in a much reduced amount and lacking large multimers. When coexpressed with normal VWF 1156M-VWF decreased the secretion of normal VWF in a dose-dependent manner, the secreted VWF showing all the multimers. Two relatives of the propositus were single heterozygotes for the T1156M mutation and were either asymptomatic or had the manifestations of mild type 1 VWD. The expression data and studies of platelet VWF indicate that the T1156M mutation results in intracellular retention of VWF rather than impaired synthesis. Three other members of the family were heterozygotes for the Q2470X mutation and demonstrated the variable expressivity of a null allele.

Characterization of the defect of the factor VIII/von Willebrand factor protein in von Willebrand's disease

Blood ◽

10.1182/blood.v59.3.542.542 ◽

1982 ◽

Vol 59 (3) ◽

pp. 542-548 ◽

Cited By ~ 14

Author(s):

HR Gralnick ◽

MC Cregger ◽

SB Williams

Keyword(s):

Sialic Acid ◽

Factor Viii ◽

Von Willebrand Factor ◽

Platelet Rich Plasma ◽

Molecular Forms ◽

Platelet Receptor ◽

Von Willebrand ◽

Abstract The factor VIII/von Willebrand factor (f.VIII/vWf) protein was purified from the plasma of a patient with von Willebrand's disease (vWd). The patient had all of the classic laboratory findings of vWd except for the ristocetin-induced platelet aggregation of his own platelet-rich plasma. The disease has been documented in three generations. Comparison of the purified normal and vWd f.VIIi/vWf protein revealed several abnormalities, including decreased concentration of f.VIII/vWf antigen; decreased specific vWf activity; absence of the larger molecular forms of the f.VIII/vWf protein; carbohydrate deficiencies affecting the sialic acid, penultimate galactose and N- acetylglucosamine moieties; and decreased binding of the f.VIII/vWf protein to its platelet receptor. These studies indicate the multiplicity of biochemical and functional abnormalities associated with the f.VIII/vWf protein in vWd. f.VIII/vWf protein to normal f.VIII/vWf protein that had been treated with 2-mercaptoethanol (2-ME) to reduce the multimer size and then treated with specific exoglycosidases to remove the sialic acid and penultimate galactose residues revealed similar biologic properties.