Hyaline vascular Castleman disease relapsing as T cell rich B cell lymphoma with paraneoplastic pemphigus
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Abstract:
Our recent review 1 on a cohort of fine needle aspiration of the breast reported an atypical rate of about 7%, and of these, about 2% had a histological follow-up.A further analysis was carried out on these cases with excision, yielding a benign rate of about 67%.Cases without histological excision were excluded from the calculation, as a significant number of cases were lost to follow-up, and while a proportion may not have been subjected to surgery because of radiological benignity, we cannot assume that these represent the majority.This figure was actually in concordance with that reported in the literature that ranges from 48% to 68%.2e5 Nevertheless, we concede that our reported benign rate of 67% taking into account only those with histological excision will represent a lower end of the range of benign outcomes of atypical aspirates.The aim of our review was to evaluate cytological parameters predictive of excision outcome in a cohort of atypical aspirates.We did not set out to assess the accuracy of how an atypical diagnosis was made in cytology, and hence did not reclassify these atypical FNACs in this cohort.We agree that reclassification of specific criteria for diagnosis of atypia in breast aspirates will be a worthwhile exercise in further understanding and promoting precision in this category.Keywords:
Ristocetin
Bernard–Soulier syndrome
Agglutination (biology)
Blood Platelet Disorders
Mean platelet volume
Ristocetin
GPVI
Agglutination (biology)
Bernard–Soulier syndrome
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The antibiotic ristocetin only aggregates platelets in the presence of plasma von Willebrand factor. Platelets from patients with Bernard-Soulier syndrome do not aggregate upon addition of ristocetin although, in contrast to von Willebrand's disease, plasma levels of factor VIII complex (factor VIII clotting activity, von Willebrand factor activity, and von Willebrand antigen) are normal. The membrane surface of normal platelets was modified and compared to the surface of platelets from a patient with Bernard-Soulier syndrome in an attempt to identify the receptor involved in von Willebrand factor-ristocetin-induced aggregation. After the incubation of washed normal platelets with a preparation of ristocetin previously shown to contain a proteolytic contaminant, the aggregation response is significantly decreased on addition or normal plasma. Analaysis by gel electrophoresis of such platelets when stained for carbohydrate revealed a decrease in the relative amounts of membrane glycopro-eins. Chymotrypsin-treated normal platelets had less membrane glycoproteins in addition to giving a reduced aggregation response in ristocetin-induced aggregation. Staining of gels for protein and carbohydrate indicated that there was an extensive change in the surface of Bernard-Soulier platelets, whereas those from patients with von Willebrand's disease appeared the same as normal. Platelets from patients were labeled by the lactoperoxidase iodination technique. Not only was the relative intensity of staining of platelet-specific proteins and glycoproteins changed in Bernard-Soulier platelets, but the iodination of the glycoproteins on the membrane surface relative to other membrane constituents was lower. In contrast, platelets from patients with von Willebrand's disease showed a normal exposure of membrane components. These data suggest therefore that membrane glycoproteins may play a functional role in ristocetin-induced aggregation.
Ristocetin
Bernard–Soulier syndrome
Glycoprotein Ib
von Willebrand Disease
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Abstract Botrocetin, a protein isolated from the venom of the snake Bothrops jararaca, induces platelet aggregation/agglutination by von Willebrand factor (vWF) binding to the membrane glycoprotein (GP) Ib, an action resembling that of ristocetin. However, some differences in the interaction between vWF and platelet GPIb induced by these two substances have been reported. We have recently shown that the GPIb binding domain on the vWF molecule, in both instances, resides in the tryptic 52/48 kDa fragment extending from amino acid residue 449 to 728 of the constituent subunit. In the present report, we demonstrate that botrocetin does not induce agglutination of formalin‐fixed platelets from a patient with Bernard‐Soulier syndrome congenitally lacking GPIb and GPIX as well as GPV, a finding similar to that shown with ristocetin. A monoclonal antibody against GPIb (AP‐1) inhibits either ristocetin‐ or botrocetin‐dependent vWF binding to formalin‐fixed platelets from normal individuals. Therefore, botrocetin‐induced vWF binding to formalin‐fixed platelets may reflect the interaction between vWF and platelet GPIb. To strengthen this concept, we have now found that heightened botrocetin‐induced type IIB vWF binding to platelet GPIb causes hyperagglutination of normal platelets.
Ristocetin
Agglutination (biology)
Glycoprotein Ib
Bernard–Soulier syndrome
von Willebrand Disease
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Mean platelet volume
Bernard–Soulier syndrome
Ristocetin
Hematology
Platelet disorder
Blood Platelet Disorders
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Bernard–Soulier syndrome
Ristocetin
Glycoprotein Ib
von Willebrand Disease
Polyclonal antibodies
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Seven patients with Bernard-Soulier syndrome (BSS) and 15 presumed heterozygotes of BSS from four families are presented. Evaluation of their platelet membranes was performed by an enzyme-linked radioimmunosorbent assay (ELISA) technique including monoclonal antibodies specific for glycoprotein (GP) lb and GPIIb/IIIa. Analyses of platelets from the patients revealed 6–33% of the normal GPIb concentration; siblings showed nearly equal amounts of this component. One of the relatives had 44% of the normal level, while 85–98% (mean 92%) of the normal GPIb content was observed in the remaining relatives. Normal or slightly elevated levels of GPIIb/IIIa were detected in the patients as well as in the relatives. All relatives had normal platelet count, size distribution, bleeding time, and ristocetin-induced platelet aggregation. The patients and their relatives may account for a biological variation in GPIb expression or may represent a variant type of BSS.
Bernard–Soulier syndrome
Ristocetin
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Bernard–Soulier syndrome
Ristocetin
Glycoprotein Ib
Polyclonal antibodies
von Willebrand Disease
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Glanzmann's thrombasthenia and the Bernard-Soulier syndrome are inherited blood disorders characterized by abnormalities in different aspects of platelet function during haemostasis. Platelets from patients with thrombasthenia do not aggregate in response to the normal physiological platelet aggregation inducing stimuli, while Bernard-Soulier platelet have a reduced capacity to adhere to exposed subendothelium. Deficiencies of different membrane glycoproteins have been located in the platelets of both disorders and suggest specific roles for membrane glycoproteins in different aspects of platelet function.
Bernard–Soulier syndrome
Blood Platelet Disorders
Glanzmann's thrombasthenia
Membrane glycoproteins
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To investigate the abnormality in platelet function in two patients with type I Gaucher's disease causing a chronic bleeding tendency despite normalisation of the platelet count after spleen removal.Routine laboratory methods were used to assess baseline coagulation. Platelet aggregometry was used to assess platelet responses to a range of agonists, and abnormalities were further assessed in mixing experiments using washed platelets and patients' plasma.Platelets from both patients with Gaucher's disease failed to agglutinate to ristocetin, despite normal platelet surface glycoprotein (GP) Ib and plasma von Willebrand factor activity. The agglutination of normal washed platelets was abolished by incubation in patient plasma. The inhibitory activity did not lie in the IgG fraction of patient plasma, and was found to be loosely associated with the patient platelet surface.The inhibition of ristocetin induced platelet agglutination in patients with Gaucher's disease causes a prolonged skin bleeding time. This could be due to the accumulated glucocerebroside in the plasma coating the platelet membrane. It is suggested that the term pseudo-pseudo Bernard-Soulier syndrome would be appropriate, as on initial screening, the abnormality has the features of Bernard-Soulier syndrome, but further investigation shows normal plasma von Willebrand activity and platelet surface GP Ib concentrations. The inhibitory activity is not due to a platelet specific antibody as is the case in pseudo-Bernard Soulier syndrome.
Bernard–Soulier syndrome
Ristocetin
Blood Platelet Disorders
Agglutination (biology)
von Willebrand Disease
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Summary Giant platelets in the blood smear, absent in vitro platelet agglutination in response to ristocetin, and normal aggregation, ATP secretion and thromboxane B2 formation were found in a young patient with a life-long bleeding tendency. Ristocetin-induced von Willebrand factor binding to her platelets was less than 10% of normal. Flow cytometric analysis with monoclonal antibodies LJ-Ib-1, LJ-Ib-10, and LJ-P3 was consistent with the latter finding. SDS-PAGE analysis of solubilized platelets showed a marked reduction of the platelet glycoprotein (GP) Ibα. Genetic characterisation demonstrated that the patient and her father were heterozygous for a deletion of 36 nucleotides (positions 554-589) leading to a mutant GPIbμ (deletion of aminoacids from residue 169 to 180 and a Glu → Lys substitution at residue 181). In addition, a C → T transition at nucleotide 515 in the other allele of the GPIbα gene was found in the patient and in her mother that results in the substitution of alanine for valine in codon 156 (Bernard-Soulier type Bolzano). These variations occurred within the VI and VII leucine-rich repeats. The novel variant of Bernard-Soulier syndrome identified further suggests that the integrity of leucine-rich repeats is important for normal function of the GP Ib-IX-V receptor complex.
Ristocetin
Bernard–Soulier syndrome
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