Shedding a little light on posttransfusion purpura

Transfusion ◽  
2015 ◽  
Vol 55 (2) ◽  
pp. 232-234 ◽  
Author(s):  
Nareg H. Roubinian ◽  
Andrew D. Leavitt
Keyword(s):  
Posttransfusion Purpura

scholarly journals Spectrum of Ig classes, specificities, and titers of serum antiglycoproteins in chronic idiopathic thrombocytopenic purpura

Blood ◽  
1994 ◽  
Vol 83 (4) ◽  
pp. 1024-1032 ◽  
Author(s):  
R He ◽  
DM Reid ◽  
CE Jones ◽  
NR Shulman
Keyword(s):  
Idiopathic Thrombocytopenic Purpura ◽  
Cytoplasmic Domain ◽  
Platelet Glycoprotein ◽  
Chronic Idiopathic Thrombocytopenic Purpura ◽  
Platelet Destruction ◽  
Thrombocytopenic Purpura ◽  
Secondary Phenomenon ◽  
Almost All ◽  
Posttransfusion Purpura ◽  
Detectable Serum

Abstract The characteristic decreased recovery and survival of transfused platelets in nonalloimmunized patients with idiopathic thrombocytopenic purpura (ITP) suggest that plasma antiplatelet autoantibodies (autoAbs) are present in almost all cases. Studies emphasizing reactions of IgG autoAbs with platelet glycoprotein (GP) IIb/IIIa indicate that less than 50% of ITP patients have detectable serum Abs, and that many of these Abs may not be pathogenic because they are directed against epitopes in the cytoplasmic domain of GPIIIa (Fujisawa et al, Blood 77:2207, 1991 and 79:1441, 1992). We evaluated the contribution of Ig classes other than IgG to the overall incidence of serum Abs in 47 patients with chronic ITP and the frequency of reactions with GPs IIb/IIIa, Ib/IX, IV, and Ia/IIa. Abs were further characterized by their reactions with cytosolic or exosolic GP epitopes and their titers and apparent affinities. Using immunobead techniques we found (1) anti- GPs in 85% of sera; (2) IgA and IgG Abs each in 68%, together in 51%; (3) IgM agglutinins in 15%, always with another Ab class; (4) GP Ib/IX, IIb/IIIa, IV, and Ia/IIa targets in 83%, 81%, 38%, and 28% of cases, respectively; (5) 93% of positive sera reactive with more than one GP; but GP IV or Ia/IIa never the sole target; (6) Abs against cytosolic epitopes on one or more of GPs IIIa, Ib alpha, and IIb beta in 66% of sera, always accompanied by Abs against exosolic epitopes of the same or a different GP; (7) autoAbs against cytosolic GP epitopes in 38% of 16 patients recovered from posttransfusion purpura and drug purpura; and (8) evidence that serum ITP Abs, often high-titered, saturate platelets less than alloAbs against the same GPs. Whereas Abs against external GP epitopes are a distinctive marker for ITP in 80% of patients, Abs against internal GP epitopes are likely a secondary phenomenon of platelet destruction and not pathogenic. Anti-GPs against exosolic epitopes were also found in eluates of patients platelets', suggesting that they have pathogenic significance.

scholarly journals Posttransfusion purpura associated with an autoantibody directed against a previously undefined platelet antigen

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1458-1463
Author(s):  
RB Stricker ◽  
BH Lewis ◽  
L Corash ◽  
MA Shuman
Keyword(s):  
Acute Phase ◽  
Platelet Destruction ◽  
Autoantibody Production ◽  
Antiplatelet Antibodies ◽  
Platelet Protein ◽  
Gp 120 ◽  
Platelet Antigen ◽  
Immunoblot Technique ◽  
Posttransfusion Purpura ◽  
Acute Phase Serum

Although alloantibody against the PLA1 platelet antigen is usually found in patients with posttransfusion purpura (PTP), the mechanism of destruction of the patient's own PLA1-negative platelets is unexplained. We used a sensitive immunoblot technique to detect antiplatelet antibodies in a patient with classic PTP. The patient's acute-phase serum contained antibodies against three proteins present in control (PLA1-positive) platelets: an antibody that bound to a previously unrecognized platelet protein of mol wt 120,000 [glycoprotein (GP) 120], antibodies that bound to PLA1 (mol wt 90,000), and an epitope of GP IIb (mol wt 140,000). The antibodies against PLA1 and GP IIb did not react with the patient's own PLA1-negative platelets, control PLA1-negative platelets, or thrombasthenic platelets. In contrast, the antibody against GP 120 recognized this protein in all three platelet preparations, but not in Bernard-Soulier or Leka (Baka)-negative platelets. Antibody against GP 120 was not detected in the patient's recovery serum, although the antibodies against PLA1 and GP IIb persisted. F(ab)2 prepared from the patient's acute-phase serum also bound to GP 120. These results suggest that in PTP, transient autoantibody production may be responsible for autologous (PLA1-negative) platelet destruction. In addition, alloantibodies against more than one platelet alloantigen may be found in this disease. The nature of the GP 120 autoantigen and the GP IIb- related alloantigen defined by our patient's serum remains to be determined.

scholarly journals A practical approach to evaluating postoperative thrombocytopenia

2020 ◽  
Vol 4 (4) ◽  
pp. 776-783 ◽  
Author(s):  
Leslie Skeith ◽  
Lisa Baumann Kreuziger ◽  
Mark A. Crowther ◽  
Theodore E. Warkentin
Keyword(s):  
Platelet Count ◽  
Late Onset ◽  
Practical Approach ◽  
Drug Induced ◽  
Heparin Induced Thrombocytopenia ◽  
Replacement Surgery ◽  
Device Implantation ◽  
Increased Risk ◽  
Posttransfusion Purpura ◽  
Heparin Exposure

Abstract Identifying the cause(s) of postoperative thrombocytopenia is challenging. The postoperative period includes numerous interventions, including fluid administration and transfusion of blood products, medication use (including heparin), and increased risk of organ dysfunction and infection. Understanding normal thrombopoietin physiology and the associated expected postoperative platelet count changes is the crucial first step in evaluation. Timing of thrombocytopenia is the most important feature when differentiating causes of postoperative thrombocytopenia. Thrombocytopenia within 4 days of surgery is commonly caused by hemodilution and increased perioperative platelet consumption prior to thrombopoietin-induced platelet count recovery and transient platelet count overshoot. A much broader list of possible conditions that can cause late-onset thrombocytopenia (postoperative day 5 [POD5] or later) is generally divided into consumptive and destructive causes. The former includes common (eg, infection-associated disseminated intravascular coagulation) and rare (eg, postoperative thrombotic thrombocytopenic purpura) conditions, whereas the latter includes such entities as drug-induced immune thrombocytopenia or posttransfusion purpura. Heparin-induced thrombocytopenia is a unique entity associated with thrombosis that is typically related to intraoperative/perioperative heparin exposure, although it can develop following knee replacement surgery even in the absence of heparin exposure. Very late onset (POD10 or later) of thrombocytopenia can indicate bacterial or fungal infection. Lastly, thrombocytopenia after mechanical device implantation requires unique considerations. Understanding the timing and severity of postoperative thrombocytopenia provides a practical approach to a common and challenging consultation.

scholarly journals Posttransfusion purpura associated with an autoantibody directed against a previously undefined platelet antigen

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1458-1463 ◽  
Author(s):  
RB Stricker ◽  
BH Lewis ◽  
L Corash ◽  
MA Shuman
Keyword(s):  
Acute Phase ◽  
Platelet Destruction ◽  
Autoantibody Production ◽  
Antiplatelet Antibodies ◽  
Platelet Protein ◽  
Gp 120 ◽  
Platelet Antigen ◽  
Immunoblot Technique ◽  
Posttransfusion Purpura ◽  
Acute Phase Serum

Abstract Although alloantibody against the PLA1 platelet antigen is usually found in patients with posttransfusion purpura (PTP), the mechanism of destruction of the patient's own PLA1-negative platelets is unexplained. We used a sensitive immunoblot technique to detect antiplatelet antibodies in a patient with classic PTP. The patient's acute-phase serum contained antibodies against three proteins present in control (PLA1-positive) platelets: an antibody that bound to a previously unrecognized platelet protein of mol wt 120,000 [glycoprotein (GP) 120], antibodies that bound to PLA1 (mol wt 90,000), and an epitope of GP IIb (mol wt 140,000). The antibodies against PLA1 and GP IIb did not react with the patient's own PLA1-negative platelets, control PLA1-negative platelets, or thrombasthenic platelets. In contrast, the antibody against GP 120 recognized this protein in all three platelet preparations, but not in Bernard-Soulier or Leka (Baka)-negative platelets. Antibody against GP 120 was not detected in the patient's recovery serum, although the antibodies against PLA1 and GP IIb persisted. F(ab)2 prepared from the patient's acute-phase serum also bound to GP 120. These results suggest that in PTP, transient autoantibody production may be responsible for autologous (PLA1-negative) platelet destruction. In addition, alloantibodies against more than one platelet alloantigen may be found in this disease. The nature of the GP 120 autoantigen and the GP IIb- related alloantigen defined by our patient's serum remains to be determined.

scholarly journals Expression and purification of functional recombinant epitopes for the platelet antigens, PlA1 and PlA2

Blood ◽  
1994 ◽  
Vol 84 (4) ◽  
pp. 1157-1163 ◽  
Author(s):  
EA Barron-Casella ◽  
TS Kickler ◽  
OC Rogers ◽  
JF Casella
Keyword(s):  
Amino Acids ◽  
Fusion Protein ◽  
Fusion Proteins ◽  
Disulfide Bonds ◽  
Affinity Purification ◽  
Platelet Glycoprotein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Glutathione S Transferase ◽  
Amino Terminal ◽  
Posttransfusion Purpura

Abstract The platelet antigens, PlA1 and PlA2, are responsible for most cases of posttransfusion purpura (PTP) and neonatal alloimmune thrombocytopenia (NAIT) in the caucasian population and are determined by two allelic forms of the platelet glycoprotein GPIIIa gene. To study the interaction between these antigens and their respective antibodies, we inserted the sequence that encodes the signal peptide and the N- terminal 66 amino acids of the PlA1 form of GPIIIa into the expression vector pGEX1. To express the PlA2 antigen, nucleotide 196 of the PlA1 coding sequence was mutated to the PlA2 allelic form. When transformed and induced in Escherichia coli, the two constructs produce glutathione S-transferase (GST)/N-terminal GPIIIa fusion proteins, one containing leucine at position 33 (PlA1), the other proline (PlA2). These proteins are easily purified in milligram quantities using glutathione-Sepharose and react specifically with their respective antibodies by immunoblot and enzyme-linked immunosorbent assay. Antigenicity of the PlA1 fusion protein in reduced glutathione increases with time; moreover, the addition of oxidized glutathione accelerates this process, presumably because of formation of the native disulfide bonds. Neutralization assays indicate that the PlA1 fusion protein competes for all of the anti-PlA1 antibody in the serum of patients with PTP and NAIT that is capable of interacting with the surface of intact platelets. This study shows that the GST/N-terminal GPIIIa fusion proteins contain conformational epitopes that mimic those involved in alloimmunization, and that regions other than the amino terminal 66 amino acids of GPIIIa are not likely to contain or be required for the development of functional PlA1 epitopes. Furthermore, these recombinant proteins can be used for the affinity-purification of clinical anti-PlA1 antibodies and specific antibody identification by western blotting, making them useful in the diagnosis of patients alloimmunized to PlA1 alloantigens.

Posttransfusion Purpura in a Dog with Hemophilia A

1997 ◽  
Vol 11 (4) ◽  
pp. 261-263 ◽  
Author(s):  
K. Jane Wardrop ◽  
David Lewis ◽  
Steven Marks ◽  
Michael Buss
Keyword(s):  
Hemophilia A ◽  
Posttransfusion Purpura

scholarly journals Anti-HPA-1b Mediated Posttransfusion Purpura: A Case Report

2013 ◽  
Vol 2013 ◽  
pp. 1-3 ◽  
Author(s):  
O. P. Arewa ◽  
S. Nahirniak ◽  
G. Clarke
Keyword(s):  
African American ◽  
Case Report ◽  
Human Platelet ◽  
Blood Component ◽  
Transfusion Reaction ◽  
Blood Component Transfusion ◽  
Platelet Antigen ◽  
Human Platelet Antigen ◽  
Specific Antigens ◽  
Posttransfusion Purpura

Posttransfusion purpura (PTP) is an uncommon, but potentially fatal, transfusion reaction characterized by profound thrombocytopenia and bleeding. PTP is caused by alloimmunization to human platelet specific antigens following blood component transfusion. Although there is evidence of a wide serological spectrum of culprit antibodies implicated, Anti-human-platelet-antigen- (HPA-) 1a is the most common antibody in cases reported. We report a case of posttransfusion purpura in an African American. The patient was negative for HPA-1a antibodies, but anti-HPA-1b was identified with a platelet phenotype of HPA-1a/HPA-1a. Although less common, HPA-1b antibody may be an important consideration in posttransfusion purpura diagnosed in patients of African descent.

Nomifensine-induced immune hemolytic anemia and posttransfusion purpura in the same patient

Transfusion ◽  
1987 ◽  
Vol 27 (3) ◽  
pp. 250-252 ◽  
Author(s):  
C Mueller-Eckhardt ◽  
B Allolio ◽  
A Salama ◽  
V Kiefel ◽  
U Deuss
Keyword(s):  
Hemolytic Anemia ◽  
Immune Hemolytic Anemia ◽  
Posttransfusion Purpura
Sign in / Sign up

Export Citation Format

Share Document