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At least 19 recordsLinked to original sources
PubMed1978

Deletion of the platelet-specific alloantigen PlA1 from platelets in Glanzmann's thrombasthenia.

Expression of a Platelet-specific alloantigen (Pl(A1)) was studied in five unrelated patients with Glanzmann's thrombasthenia using immunologic techniques based on release of (51)Cr from tagged platelets by Pl(A1)-specific antibody. Less than 1% of the normal quantity of Pl(A1) could be detected on platelets of patients 1, 2, and 3; platelets from patients 4 and 5 contained 22 and 12% of normal levels, respectively. After treatment with bromelain, platelets from patients 4 and 5, but not those from patients 1, 2, and 3, released (51)Cr as well as normal Pl(A1)-positive platelets when exposed to anti-Pl(A1). Platelets from each of the five patients reacted normally with drug-dependent antibodies and with autoantibodies specific for platelets. Polyacrylamide gel electrophoresis of thrombasthenic platelets showed marked deficiencies of glycoproteins IIbalpha and III (P < 0.0005), confirming recent reports of others. Deficiency of the two proteins as determined by gel scanning was more pronounced in patients 1, 2, and 3 than in patients 4 and 5. Normal levels of glycoproteins IIbalpha and III were found in platelets from normal subjects negative for Pl(A1). These observations are consistent with the possibility that the Pl(A1) antigen is located on one or both of the glycoproteins lacking in Glanzmann's thrombasthenia, although other explanations are possible. They further suggest that patients with thrombasthenia may be heterogeneous in respect to the degree to which these glycoproteins are deleted. The Pl(A1) antigen can be measured with considerable precision and may provide a marker useful for the diagnosis and study of Glanzmann's disease.

Blood Platelets↗
PubMed1977

Platelet membrane defects in Glanzmann's thrombasthenia. Evidence for decreased amounts of two major glycoproteins.

Platelets from patients with Glanzmann's thrombasthenia have a distinct molecular alteration of the plasma membrane surface, namely decreased amounts of a major glycoprotein designated as IIb (apparent mol wt 142,000). To identify other possible surface defects of thrombasthenic platelets, we labeled the membrane polypeptides of normal and thrombasthenic platelets by two different techniques: lactoperoxidase-catalyzed iodination and galactose oxidase oxidation, followed by reduction with tritiated sodium borohydride. Labeling patterns were determined after the polypeptides were separated by two-dimensional polyacrylamide gel electrophoresis. Before the second dimension was run, platelet samples were incubated with a reducing agent, beta-mercapto-ethanol, to cleave the disulfide bonds of certain glycoproteins; the resulting changes in electrophoretic mobility permitted better resolution of individual molecules. Comparison of the labeled polypeptides of normal and thrombasthenic samples after reduction indicated decreased labeling of two major glycoproteins in thrombasthenic platelets: IIb and III (apparent mol wt 114,000). The relative proportions of radioactivity incorporated by these polypeptides were about 60 and 80% less than control values, respectively. With either Coomassie Blue or periodic acid-Schiff's reagent, glycoprotein III stained much less intensely in thrombasthenic compared to normal samples, indicating that the observed labeling deficit was caused by a decreased concentration of the molecule rather than steric inaccessibility on the membrane surface. Analysis of normal plasma membranes by affinity chromatography showed that glycoprotein IIb has receptors for lectin from Lens culinaris, the common lentil, whereas III does not. We conclude that a characteristic feature of Glanzmann's thrombasthenia is a decreased concentration of two discrete glycoproteins in the platelet plasma membrane.

Blood Platelet Disorders↗
PubMed1979

The management of dental extractions in cases of thrombasthenia complicated by the development of isoantibodies to donor platelets.

Two cases of thrombasthenia, a rare hereditary disorder of platelet function, are presented. The oral surgical and dental management of these cases is discussed in the light of the development of isoantibodies to transfused platelets in one of the cases and in another case encountered. The problems of obtaining donor platelets matched for platelet and HL-A antigens are discussed. Emphasis is placed on the use of local hemostatic measures and antifibrinolytic agents in the management of hemorrhage in this disorder and the avoidance of platelet transfusions as far as possible. Conservative dentistry and early preventive dental advice are considered desirable in order to avoid extractions.

Adolescent↗
PubMed1979

[Immunochemical study of protein anomalies in platelets of patients with Glanzmann's thrombasthenia and Bernard-Soulier syndrome].

Crossed immunoelectrophoresis of "Triton X-100" solubilized proteins from (125I) iodinated normal and abnormal (Bernard-Soulier and thrombasthenic) platelets was performed using rabbit antibodies raised against whole, normal platelets. In Bernard-Soulier platelets neither of the two surface oriented forms of GP I, glycocalicin and glycoprotein Ib (band 13) were detected. In two patients with type I thrombasthenia, the most prominent precipitate (No. 16) and platelet fibrinogen (No 24) were not detected whereas in one patient with type II thromblasthenia, fibrinogen was normally detected and the amount of protein 16 was around 15% of the normal level. The alloantibody IgG L..., able to induce a "thrombasthenic-like" reactivity in normal human platelets, has been shown to be directed against protein 16.

Animals↗
PubMed1976

Ultrastructure of platelet aggregation in refractory anemia and myelomonocytic leukemia. II. Individual platelet abnormalities: thrombasthenia-like platelets, surface defects, and dissociation phenomena.

Studies of in vitro platelet aggregation were done in five patients with refractory anemia and two with acute myelomonocytic leukemia. The macroscopic results as well as the general ultrastructural findings were reviewed in a companion paper. Electron microscopic analysis of changes in the individual platelets within aggregates revealed a striking heterogeneity, both in the degree of response of each platelet are in the ultrastructural characteristics of the platelet population. Many of the unaggregated platelets had reacted individually, resembling the platelets of patients with Glanzmann's thrombasthenia. There were other abnormalities suggesting the presence of surface defects, such as the presence of areas of obliteration of the interplatelet space (so-called tight connections). One of the most striking findings was a peculiar dissociation between the different components of the aggregation sequence.

Anemia, Aplastic↗
PubMed1979

alpha-Actinin deficiency in thrombasthenia: possible identity of alpha-actinin and glycoprotein III.

Blood platelets contain a variety of contractile protein species, including the glycoprotein alpha-actinin, which is found at the Z disc in skeletal muscle cells. In the present study, we have considered the possibility that alpha-actinin might be one of several previously described platelet surface glycoproteins. Purified anti-alpha-actinin antibody was found to react strongly with partially purified platelet glycoprotein III, weakly with platelet glycoprotein IIb, and not at all with platelet glycoproteins Ib and IV. Platelets from three siblings with thrombasthenia, a disorder characterized by severe deficiency of platelet glycoproteins IIb and III, were found also to be equally deficient in alpha-actinin. These findings indicate that alpha-actinin and glycoprotein III are identical and suggest that this protein may be an anchor point for actin on the inside of the membrane. Combined with ultrastructural studies of normal and thrombasthenic platelets, the new findings provide a clearer understanding of contraction in single cells and small aggregates.

Actinin↗
PubMed1979

Platelet membrane glycoproteins in thrombasthenia, Bernard-Soulier syndrome, and storage pool disease.

Quantitative polyacrylamide gel electrophoresis has been carried out on patients with Bernard-Soulier syndrome, Glanzmann's thrombasthenia, and storage pool defect in order to clarify the abnormalities in their platelet membrane glycoproteins. Normal individuals had values (expressed as PAS staining units/mg of membrane protein) of 5.11 +/- 0.63 for glycoprotein 1 (Mr 150,000), 2.35 +/- 0.35 for glycoprotein II (Mr 120,000), 0.89 +/- 0.22 for glycoprotein III (Mr 100,000), and 1.34 +/- 0.64 for glycoprotein IV (Mr 85,000). Total PAS staining of these four major bands was 9.70 +/- 1.26 PAS units/mg of membane protein. Patients with Bernard-Soulier syndrome completely lacked glycocalicin and had about one half (1.90 PAS units/mg) of the glycoprotein I of normal controls. These was no significant reduction in glycoproteins II, III, and IV, but total PASstaining was reduced to 4.40 units/mg, reflecting the importance of the contribution of glycoprotein I to this parameter. Thrombasthenic platelets gave values for glycoprotein II of 0.66, which were about 25% of controls, and the values for glycoprotein III (0.34) were about 40% of controls. Patients with storage pool disease gave values within the normal range with the exception of one family which showed, in addition, small platelets and an associated lipid defect. In thic case of glycoprotein (2.71) was significantly elevated.

Blood Platelet Disorders↗
PubMed1979

[Thrombasthenia in a newborn (author's transl)].

Thrombasthenia is an extemely rare hereditary disorder of platelet function characterized by impairment of adhesiveness, ADP-induced aggregation, and clot retraction. Petechiae and ecchymoses in a newborn infant followed by prolonged jaundice facilitated early diagnosis.

Blood Coagulation Factors↗
PubMed1978

[Twin pregnancy in a patient with Glanzmann disease (congenital thrombasthenia) (author's transl)].

Report on a 30-year old primigravida with a family history of bleeding and a personal history of nasopharyngeal bleeding since age four. Severe menorrhagia since her menarche. First seen at 20 weeks gestation with naso-pharyngeal bleeding and a twin pregnancy. The patient was found to have Glanzmann's disease (congenital thrombasthenia) with an excessive lack of factor XIII. Ambulatory treatment with packed cell transfusions until 35 weeks gestation. The thrombelastogram did not improve with transfusions of platelet concentrates. In-patient treatment from 35 to 37 weeks gestation, no vaginal bleeding throughout the pregnancy. Elective Caesarean hysterectomy at 37 weeks gestation with lo units fresh blood, 3 units platelet concentrate and 10 ampules factor XIII concentrate in readiness. Delivery of twin girls 3180 and 3050 g without signs of Glanzmann's disease. Treatment of the maternal bleeding by replacement. Factor XIII 80% of normal 8 weeks postpartum. This appears to be the first case of twin pregnancy in the presence of Glanzmann's disease and the fourth case in the world literature.

Adult↗
PubMed1979

[Obstetrical problems in patients with Glanzmann's thrombasthenia. A casuistic presentation (author's transl)].

Glanzmann's thrombasthenia is a rare, autosomal recessive disorder of bleeding arrest. The differential diagnosis of this platelet defect with respect to recently gained knowledge is presented in the case of a pregnant woman. Because of pelvic presentation a cesarean section was performed after adequate platelet substitution, which did not involve excessive blood loss. A severe puerperal infection necessitated an abdominal hysterectomy after appropriate platelet transfusion. The difficulties in testing platelet function in the newborn are discussed. The effectiveness of a commercially available homologous phospholipide complex (Fibraccel) was tested on the patient in a noncritical phase. The results appear important for general procedure when pregnancy and platelet dysfunction concur.

Adult↗
PubMed1979

Glanzmann's thrombasthenia. Report of two oral surgical cases using a new microfibrillar collagen preparation and EACA for hemostasis.

Glanzmann's thromboasthenia is a rare congenital platelet disorder characterized by a prolonged bleeding time, a qualitative platelet defect, and severe hemorrhagic episodes. Patients with this disorder have been managed by administration of blood and blood components (most recently, platelet-rich plasma and platelet concentrates) to control hemorrhage resulting from trauma or surgical procedures. The two case reports presented here illustrate the use of a local hemostatic agent (microfibrillar bovine collagen, Avitene) and a systemic fibrinolytic inhibitor (epsilon aminocaproic acid, Amicar) to control postoperative hemorrhage secondary to elective extraction of teeth. The clinical results demonstrate excellent postoperative hemostasis and support recent in vitro observation of platelet adherence to the collagen preparation. This provides an alternate therapeutic modality in the management of patients with Glanzmann's disease and possibly other disorders of platelet function.

Abscess↗