scholarly journals Disturbed platelet aggregation to collagen associated with an antibody against an 85- to 90-Kd platelet glycoprotein in a patient with prolonged bleeding time

Blood ◽  
1992 ◽  
Vol 79 (6) ◽  
pp. 1466-1471 ◽  
Author(s):  
H Deckmyn ◽  
E Van Houtte ◽  
J Vermylen
Keyword(s):  
Platelet Aggregation ◽  
Bleeding Time ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Platelet Glycoprotein ◽  
Two Dimensional ◽  
Membrane Glycoproteins ◽  
Prolonged Bleeding ◽  
Prolonged Bleeding Time ◽  
Normal Platelet

Abstract We studied a 5-year-old girl presenting with a markedly prolonged bleeding time. Her platelets were refractory to collagen stimulation, but the response to other agonists was normal. There were no coagulation abnormalities as measured by standard tests. Two- dimensional electrophoresis showed no abnormalities of the patient's platelet membrane glycoproteins. When the patient's plasma or purified plasma IgG was mixed with normal platelets, collagen-induced platelet aggregation was blocked. Western blotting showed the presence of an antibody in the patient's plasma directed against a protein of molecular weight 85 to 90 Kd under both reducing and nonreducing conditions. This protein comigrated with glycoprotein (GP) IV immunoprecipitated by OKM5 from 125I-labeled platelets. Immunoprecipitation of 125I-labeled normal platelet glycoproteins with the patient's IgGs also yielded an 85- to 90-Kd protein that migrated on the diagonal following nonreduced/reduced two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Despite similarities in electrophoretic behavior, the antigen was not demonstrated to be GPIV, since purified GPIV was not recognized by the antibody.

scholarly journals Disturbed platelet aggregation to collagen associated with an antibody against an 85- to 90-Kd platelet glycoprotein in a patient with prolonged bleeding time

Blood ◽  
1992 ◽  
Vol 79 (6) ◽  
pp. 1466-1471 ◽  
Author(s):  
H Deckmyn ◽  
E Van Houtte ◽  
J Vermylen
Keyword(s):  
Platelet Aggregation ◽  
Bleeding Time ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Platelet Glycoprotein ◽  
Two Dimensional ◽  
Membrane Glycoproteins ◽  
Prolonged Bleeding ◽  
Prolonged Bleeding Time ◽  
Normal Platelet

We studied a 5-year-old girl presenting with a markedly prolonged bleeding time. Her platelets were refractory to collagen stimulation, but the response to other agonists was normal. There were no coagulation abnormalities as measured by standard tests. Two- dimensional electrophoresis showed no abnormalities of the patient's platelet membrane glycoproteins. When the patient's plasma or purified plasma IgG was mixed with normal platelets, collagen-induced platelet aggregation was blocked. Western blotting showed the presence of an antibody in the patient's plasma directed against a protein of molecular weight 85 to 90 Kd under both reducing and nonreducing conditions. This protein comigrated with glycoprotein (GP) IV immunoprecipitated by OKM5 from 125I-labeled platelets. Immunoprecipitation of 125I-labeled normal platelet glycoproteins with the patient's IgGs also yielded an 85- to 90-Kd protein that migrated on the diagonal following nonreduced/reduced two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Despite similarities in electrophoretic behavior, the antigen was not demonstrated to be GPIV, since purified GPIV was not recognized by the antibody.

Essential Athrombia

1975 ◽  
Vol 33 (02) ◽  
pp. 278-285 ◽  
Author(s):  
Şeref Inceman ◽  
Yücel Tangün
Keyword(s):  
Platelet Aggregation ◽  
Bleeding Time ◽  
Bleeding Tendency ◽  
Clot Retraction ◽  
Platelet Factor ◽  
Prolonged Bleeding Time ◽  
Normal Platelet ◽  
Aggregation Response ◽  
Platelet Disorder ◽  
Fibrinogen Content

SummaryA constitutional platelet function disorder in a twelve-year-old girl characterized by a lifelong bleeding tendency, prolonged bleeding time, normal platelet count, normal clot retraction, normal platelet factor 3 activity and impaired platelet aggregation was reported.Platelet aggregation, studied turbidimetrically, was absent in the presence of usual doses of ADP (1–4 μM), although a small wave of primary aggregation was obtained by very large ADP concentrations (25–50 μM). The platelets were also unresponsive to epinephrine, thrombin and diluted collagen suspensions. But an almost normal aggregation response occurred with strong collagen suspensions. The platelets responded to Ristocetin. Pelease of platelet ADP was found to be normal by collagen and thrombin, but impaired by kaolin. Platelet fibrinogen content was normal.The present case, investigated with recent methods, confirms the existence of a type of primary functional platelet disorder characterized solely by an aggregation defect, described in 1955 and 1962 under the name of “essential athrombia.”

Acquired Disorder of Platelet Function Associated with Autoantibodies against Membrane Glycoprotein IIb-IIIa Complex - 1. Glycoprotein Analysis

1991 ◽  
Vol 65 (05) ◽  
pp. 491-496 ◽  
Author(s):  
M Meyer ◽  
C M Kirchmaier ◽  
A Schirmer ◽  
P Spangenberg ◽  
Ch Ströhl ◽  
...  
Keyword(s):  
Platelet Count ◽  
Platelet Aggregation ◽  
Platelet Adhesion ◽  
Bleeding Time ◽  
Membrane Glycoprotein ◽  
Membrane Glycoproteins ◽  
Abnormal Behaviour ◽  
Thrombocytopenic Purpura ◽  
Immunoelectrophoretic Analysis ◽  
Prolonged Bleeding Time

SummaryA patient with idiopathic thrombocytopenic purpura developed after splenectomy a thrombasthenia-like severe haemor-rhagic diathesis characterized by a normal or subnormal platelet count, prolonged bleeding time, strongly reduced platelet adhesion to glass and defective platelet aggregation in response to ADP and collagen. In contrast to hereditary thrombasthenia membrane glycoproteins (GP) lib and Ilia were normally present in the patient’s platelets. Immunoelectrophoretic analysis revealed an abnormal behaviour of the patient’s GP IIb-IIIa complex. Autoantibodies against GP IIb-IIIa were detected in Triton-extracted washed platelets. Incubation of normal platelets with plasma from the patient resulted in a similar immunoelectrophoretic abnormality of the GP IIb-IIIa complex indicating that bound autoantibodies (IgG) are responsible for the abnormal immunoelectrophoretic behaviour of the patient’s GP IIb-IIIa complex. Platelet fibrinogen was severely reduced similar to classical thrombasthenia suggesting that the GP IIb-IIIa complex is involved in platelet fibrinogen storage.

Factors which Influence the Bleeding Time

1962 ◽  
Vol 08 (03) ◽  
pp. 511-523
Author(s):  
G. J. H den Ottolander ◽  
A Bleijenberg
Keyword(s):  
Bleeding Time ◽  
Prolonged Bleeding ◽  
Prolonged Bleeding Time ◽  
Normal Platelet

SummaryA prolonged bleeding time can be due to a vascular, plasmatic, or thrombocytic cause. On the basis of investigations in 8 patients with a prolonged bleeding time, these different forms are discussed.There appeared to be at least two plasmatic factors one of which is the bleeding factor of Nilsson. The demonstration of a thrombocytic cause is sometimes only possible with transfusions of normal platelet suspensions. A patient is described with a prolonged bleeding time due to an acquired thrombo-pathia, resulting from excessive haemorrhages and exchange transfusions.

scholarly journals "Impotent" Platelets in Albinos With Prolonged Bleeding Times

Blood ◽  
1972 ◽  
Vol 39 (4) ◽  
pp. 490-499 ◽  
Author(s):  
Harold M. Maurer ◽  
James A. Wolff ◽  
Sue Buckingham ◽  
Arthur R. Spielvogel
Keyword(s):  
Platelet Aggregation ◽  
Adenosine Diphosphate ◽  
Bleeding Tendency ◽  
Prolonged Bleeding ◽  
Prolonged Bleeding Time ◽  
Normal Platelet ◽  
Tryptophan Metabolites ◽  
History Of

Abstract Functional, biochemical, and morphologic platelet abnormalities are reported in four children with the syndrome of albinism, mild bleeding tendency, prolonged bleeding time, and normal platelet count. In these children, primary platelet aggregation with adenosine diphosphate occurred normally, but secondary aggregation was impaired. Collagen and norepinephrine produced almost no platelet aggregation. Platelet content of serotonin (5-HT) was markedly reduced, and uptake and retention of 5-HT by the platelets in vivo and in vitro was poor. In one child who was given a tryptophan load, urinary tryptophan metabolites were normal, suggesting that there was no evidence of a block in the 5-HT synthetic pathway in the gastrointestinal tract. Electron microscopy revealed an absence of densely osmophilic granules in 5-HT poor platelets. Platelets from other albinos with no history of bleeding contained normal amounts of 5-HT and densely osmophilic granules.

Circulating anticoagulant in a family with prolonged bleeding time and factor VIII deficiency

Blood ◽  
1977 ◽  
Vol 49 (5) ◽  
pp. 799-806 ◽  
Author(s):  
M Diez-Ewald ◽  
EC Lian ◽  
R Nunez ◽  
D Deykin ◽  
DR Harkness
Keyword(s):  
Platelet Aggregation ◽  
Factor Viii ◽  
Bleeding Time ◽  
Factor Viii Activity ◽  
Clot Retraction ◽  
Factor Viii Related Antigen ◽  
Factor Viii Deficiency ◽  
Prolonged Bleeding ◽  
Prolonged Bleeding Time ◽  
Aggregation Activity

Abstract A circulating anticoagulant against factor VIII activity was demonstrated in the plasma of a boy from a family with both factor VIII deficiency and prolonged bleeding time. However, the factor VIII- related antigen, ristocetin-induced platelet aggregation activity, platelet retention in glass bead columns, platelet aggregation with adenosine 5′-diphosphate, collagen and epinephrine, and clot retraction among affected members were normal. The electrophoretic mobility of factor VIII-related antigen on crossed immunoelectrophoresis was normal. The inactivation of factor VIII activity by the inhibitor was time dependent and was nonlinear as the concentration of the inhibitor was increased. Immunotyping showed that the inhibitor was IgG with k light chains.

scholarly journals Circulating anticoagulant in a family with prolonged bleeding time and factor VIII deficiency

Blood ◽  
1977 ◽  
Vol 49 (5) ◽  
pp. 799-806
Author(s):  
M Diez-Ewald ◽  
EC Lian ◽  
R Nunez ◽  
D Deykin ◽  
DR Harkness
Keyword(s):  
Platelet Aggregation ◽  
Factor Viii ◽  
Bleeding Time ◽  
Factor Viii Activity ◽  
Clot Retraction ◽  
Factor Viii Related Antigen ◽  
Factor Viii Deficiency ◽  
Prolonged Bleeding ◽  
Prolonged Bleeding Time ◽  
Aggregation Activity

A circulating anticoagulant against factor VIII activity was demonstrated in the plasma of a boy from a family with both factor VIII deficiency and prolonged bleeding time. However, the factor VIII- related antigen, ristocetin-induced platelet aggregation activity, platelet retention in glass bead columns, platelet aggregation with adenosine 5′-diphosphate, collagen and epinephrine, and clot retraction among affected members were normal. The electrophoretic mobility of factor VIII-related antigen on crossed immunoelectrophoresis was normal. The inactivation of factor VIII activity by the inhibitor was time dependent and was nonlinear as the concentration of the inhibitor was increased. Immunotyping showed that the inhibitor was IgG with k light chains.

Sustained Bleeding after a leech Bite in the Apparent Absence of Hirudin

1989 ◽  
Vol 61 (03) ◽  
pp. 366-369 ◽  
Author(s):  
R Munro ◽  
F O P Hechtel ◽  
R T Sawyer
Keyword(s):  
Platelet Aggregation ◽  
Bleeding Time ◽  
Medicinal Leech ◽  
Bite Wound ◽  
Apparent Absence ◽  
Coagulation Parameters ◽  
Prolonged Bleeding ◽  
Prolonged Bleeding Time ◽  
Human Volunteers

SummaryThe bite of the medicinal leech bleeds for many hours. For decades it has been assumed that the remarkably prolonged bleeding time of a leech bite wound is due to hirudin, a specific anti-thrombin secreted by the leech during feeding. By measuring haematological parameters of blood oozing from a leech bite wound on 15 different occasions in 7 human volunteers, we demonstrate that the hirudin-sensitive coagulation parameters, including thrombin-induced platelet aggregation, are prolonged for only 15 min, after which they return to normal. This suggests that excess hirudin secreted by the leech is washed out during this period. However, bleeding from the leech bite wound persists for a mean of 10 h. Platelets in smears of exuding blood show no evidence of spontaneous aggregation, but in vitro platelet aggregation can be induced by exogenous collagen at any time. In view of sustained bleeding in the apparent absence of hirudin, attention is focussed onto an unsuspected factor or factors which may better explain the prolonged bleeding phenomenon.

Isolation and Characterization of jararaca GPIb-BP, a Snake Venom Antagonist Specific to Platelet Glycoprotein lb

1995 ◽  
Vol 74 (02) ◽  
pp. 743-750 ◽  
Author(s):  
Y Fujimura ◽  
Y Ikeda ◽  
S Miura ◽  
E Yoshida ◽  
H Shima ◽  
...  
Keyword(s):  
Shear Stress ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Polyacrylamide Gel Electrophoresis ◽  
Serotonin Release ◽  
Amino Acid Sequences ◽  
Platelet Glycoprotein ◽  
Venom Protein ◽  
Normal Platelet ◽  
Isolation And Characterization

SummaryA platelet glycoprotein lb-binding protein (GPIb-BP) was isolated from the snake venom of Bothrops jararaca. Jararaca GPIb-BP showed a single band with Mr of 30,000, and two distinct bands with Mr. of 17,000/13,000 under non-reducing and reducing conditions, respectively, on SDS-polyacrylamide gel electrophoresis. Jararaca GPIb-BP itself induced neither platelet aggregation nor serotonin release from platelets, but specifically bound to GPIb (40,629 ± 2,521 molecules per normal platelet, with Kd 39.1 ± 2.4 nM at saturation). The purified venom protein completely inhibited ristocetin- or botrocetin-induccd von Willebrand factor (vWF) binding, and blocked the bovine vWF binding to GPIb, with IC50 values ranging from 28 to 42 nM, without affecting the platelet aggregation induced by ADP or α-thrombin. 1251-jararaca GPIb-BP binding to GPIb was not altered by the presence of human α-thrombin. Jararaca GPIb-BP at a final concentration of 104 nM totally abolished vWF-dependent shear- induced platelet aggregation (SIPA) at a high shear stress, but had no effect on SIPA at a low shear stress. Reduced and S-carboxyamidomethylated jararaca GPIb-BP lost its inhibitory activity on SIPA. The NH2-terminal amino acid sequences of the subunits revealed a high degree of homology with those of several Ca2+-dependent lectins, especially to those of two functionally opposite venom proteins, botrocetin (a vWF-modulator) and alboaggregin-B (a GPIb- modulator).

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