Platelet Agglutinating Protein P37 From a Thrombotic Thrombocytopenic Purpura Plasma Forms a Complex With Immunoglobulin G

Siddigui, F A; Lian, EC

doi:10.1055/s-0038-1644589

Cited by 6 publications

(5 citation statements)

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“…Agglutination of autologous and homologous platelets by TTP plasma has been demonstrated. A 37 kD protein has been isolated from plasma of some patients with acute TTP, and it has been suggested that this protein, which is not found in all patients with TTP, agglutinates platelets through interaction with CD36 ( Siddiqui & Lian, 1988; Lian et al , 1991 ). It has been previously observed that 23/27 TTP sera showed anti‐CD36 reactivity by at least one method ( Tandon et al , 1994 ).…”

Section: Discussionmentioning

confidence: 99%

Characterization of platelet glycoproteins and platelet/endothelial cell antibodies in patients with thrombotic thrombocytopenic purpura

et al. 1999

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Platelets and sera from 12 patients with thrombotic thrombocytopenic purpura (TTP) and 12 healthy normal control subjects were examined. As determined by quantitative flow cytometry, prior to plasma exchange therapy platelet surface glycoprotein (GP) Ib levels were similar in TTP patients and normal controls (mean 20 188 and 20 226 molecules/platelet, respectively). Platelets from patients with TTP did, however, have significantly reduced levels of GPIIb/IIIa prior to plasmapheresis (mean 36 348 v 52 505 molecules/platelet in controls; P = 0.0004) and of GPIV (mean 13 321 v 26 212 molecules/platelet in controls; P = 0.0002). An increase in activated platelets, as determined by CD62 expression, was observed in 82% of patients. Increased platelet-associated immunoglobulins and/or complement was also seen in approximately 60% of the patients. In general, with return of platelet counts to normal levels following seven plasmaphereses, the above abnormalities were reversed, although often not to normal levels. Western blot analysis indicated the presence of antibodies reactive to platelet GPIV (88 kD) in 70% of pretreatment sera from patients with TTP; a similar band was observed in 80% of patient sera against microvascular endothelial cells. Immunofluorescence microscopic examination indicated the presence of antibody in pretreatment sera from patients with TTP to microvascular (73%) and large vessel (36%) endothelial cells. As measured by an indirect flow cytometric assay, pretreatment sera from 55% of patients with TTP were reactive with large vessel endothelial cells and 100% reacted with microvascular endothelial cells; reactivity was significantly greater against the microvascular endothelial cells (P = 0.0048) and was reduced following plasma exchange therapy. These results indicate abnormalities in platelet glycoprotein expression in TTP and suggest that anti-platelet and anti-endothelial cell antibodies play a role in the thrombocytopenia and vasculitis characteristic of this disorder.

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Section: Discussionmentioning

confidence: 99%

Characterization of platelet glycoproteins and platelet/endothelial cell antibodies in patients with thrombotic thrombocytopenic purpura

et al. 1999

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“…CD36 is an 88-kD glycoprotein expressed in various human cells, including platelets, monocytes, erythroblasts, capillary endothelial cells, and mammary epithelial cells and adipocytes (1)(2)(3)(4)(5). CD36 interacts with a large variety of ligands, including collagen types I (6) and IV (7), thrombospondin (8,9), erythrocytes parasitized with Plasmodium falciparum (10), platelet-agglutinating protein p37 (11,12), oxidized low density lipoprotein (13), and long-chain fatty acids (14). A high prevalence of CD36 deficiency in hereditary hypertrophic cardiomyopathy suggests an important role of this protein in fatty acid metabolism in the heart (15).…”

Section: Introductionmentioning

confidence: 99%

Phenotype-genotype Correlation in CD36 Deficiency Types I and II

Yanai¹,

Chiba²,

Fujiwara³

et al. 2000

Thromb Haemost

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SummaryCD36 deficiency was studied with attention to the phenotypegenotype relationship. The diagnosis of CD36 deficiency was made when CD36 was negative on platelets (type II) or on both platelets and monocytes (type I). Among 827 apparently healthy Japanese volunteers, the type I and II deficiencies were found in 8 (1.0%) and 48 (5.8%), respectively. The T for C substitution at nt478 for Pro90Ser and the insertion of A at nt1159 constituted the major causes of type I and II deficiencies. The dinucleotide deletion at nt539 had a minor role. In two family studies, we found a previously unreported polymorphic site in the 5’-proximal flanking region and the 3’-untranslated region. Including these new polymorphisms, DNA sequence other than the three known mutations affecting CD36 expression was not observed in the CD36 gene, calling into question the previous hypothesis that a platelet-specific silent allele exists near or at the CD36 gene.

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“…Recent findings on the involvement of CD36 in thrombotic thrombocytopenic purpura (TTP) and other disorders of hematopoietic system indicate its pathological implications and yet other critical functions (Byrnes and Moake, 1986;Lian et al, 1991;Siddiqui and Lian, 1992). Now, purified CD36 could be utilized for further characterization of the protein in biochemical as well as clinical aspects.…”

Section: Resultsmentioning

confidence: 99%

Purification of thrombospondin receptor (CD36) from human platelet membrane

Kim

Ho²,

Park³

et al. 1997

Exp Mol Med

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Thrombospondin receptor (CD36) has been recently identified in platelets and various cell lines as the receptor for thrombospondin, an adhesive protein required for irreversible aggregation of platelets as well as other adhesive processes. Thrombospondin receptor, one of major glycosylated platelet membrane proteins, is thought to play an important role as a cell adhesion molecule in blood coagulation system as well as intercellular signaling. In this work, thrombospondin receptor was purified to homogeneity from human platelet by wheat germ agglutinin (WGA)-affinity chromatography and size exclusion chromatography on Ultrogel-AcA44. The molecular weight of the purified thrombospondin receptor was about 88 kDa on SDS-PAGE and its identity was confirmed by immunoblot analysis and immunodiffusion assay.

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Platelet Agglutinating Protein P37 From a Thrombotic Thrombocytopenic Purpura Plasma Forms a Complex With Immunoglobulin G

Cited by 6 publications

References 0 publications

Characterization of platelet glycoproteins and platelet/endothelial cell antibodies in patients with thrombotic thrombocytopenic purpura

Characterization of platelet glycoproteins and platelet/endothelial cell antibodies in patients with thrombotic thrombocytopenic purpura

Phenotype-genotype Correlation in CD36 Deficiency Types I and II

Purification of thrombospondin receptor (CD36) from human platelet membrane

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