scholarly journals Cell Antigens and Cell Specialization. IV. On the H Blood Group Antigen of Human Platelets and Nucleated Cells of the Human Bone Marrow

Blood ◽  
1964 ◽  
Vol 24 (5) ◽  
pp. 531-541 ◽  
Author(s):  
EDMOND J. YUNIS ◽  
JORGE J. YUNIS

Abstract This article describes the specific agglutination of normoblasts, recitulocytes, megakaryocytes and platelets of human bone marrow with anti-H sera. It also describes the erythrocyte-platelet mixed agglutination reactions demonstrating H antigen receptors on all human platelets regardless of the ABO group of the donor with the exception of the Bombay blood.

Blood ◽  
1981 ◽  
Vol 57 (1) ◽  
pp. 147-151 ◽  
Author(s):  
KK Karhi ◽  
LC Andersson ◽  
P Vuopio ◽  
CG Gahmberg

Abstract We have studied the appearance of blood group A-activity during hematopoiesis in human bone marrow cells by the use of the blood group A-specific lectin from Vicia cracca. Cells that bound the lectin were identified using antiserum against the lectin followed by rosetting with protein A-containing Staphylococcus aureus cells. Only cells of the erythroid lineage from blood group A individuals formed staphylococcal rosettes. A-activity occurred in basophilic normoblasts and later stages of erythropoiesis, whereas pronormoblasts were negative. The appearance of blood group A-activity coincided roughly with the onset of hemoglobin synthesis and slightly later than the expression of the major sialoglycoprotein of erythrocytes, glycophorin A. Glycophorin A did not, however, contain blood group A-activity when analyzed by immunoprecipitation and gel electrophoresis.


Blood ◽  
2004 ◽  
Vol 104 (5) ◽  
pp. 1361-1368 ◽  
Author(s):  
Filiz Akbiyik ◽  
Denise M. Ray ◽  
Kelly F. Gettings ◽  
Neil Blumberg ◽  
Charles W. Francis ◽  
...  

Abstract Peroxisome proliferator-activated receptor γ (PPARγ) is a ligand-activated transcription factor important in lipid metabolism, diabetes, and inflammation. We evaluated whether human platelets and megakaryocytes express PPARγ and whether PPARγ agonists influence platelet release of bioactive mediators. Although PPARγ is mainly considered a nuclear receptor, we show that enucleate platelets highly express PPARγ protein as shown by Western blotting, flow cytometry, and immunocytochemistry. Meg-01 megakaryocyte cells and human bone marrow megakaryocytes also express PPARγ. Platelet and Meg-01 PPARγ bound the PPARγ DNA consensus sequence, and this was enhanced by PPARγ agonists. Platelets are essential not only for clotting, but have an emerging role in inflammation in part due to their release or production of the proinflammatory and proatherogenic mediators CD40 ligand (CD40L) and thromboxanes (TXs). Platelet incubation with a natural PPARγ agonist, 15d-PGJ2, or with a potent synthetic PPARγ ligand, rosiglitazone, prevented thrombin-induced CD40L surface expression and release of CD40L and thromboxane B2 (TXB2). 15d-PGJ2 also inhibited platelet aggregation and adenosine triphosphate (ATP) release. Our results show that human platelets express PPARγ and that PPARγ agonists such as the thiazolidinedione class of antidiabetic drugs have a new target cell, the platelet. This may represent a novel mechanism for treatment of inflammation, thrombosis, and vascular disease in high-risk patients.


Blood ◽  
1981 ◽  
Vol 57 (1) ◽  
pp. 147-151
Author(s):  
KK Karhi ◽  
LC Andersson ◽  
P Vuopio ◽  
CG Gahmberg

We have studied the appearance of blood group A-activity during hematopoiesis in human bone marrow cells by the use of the blood group A-specific lectin from Vicia cracca. Cells that bound the lectin were identified using antiserum against the lectin followed by rosetting with protein A-containing Staphylococcus aureus cells. Only cells of the erythroid lineage from blood group A individuals formed staphylococcal rosettes. A-activity occurred in basophilic normoblasts and later stages of erythropoiesis, whereas pronormoblasts were negative. The appearance of blood group A-activity coincided roughly with the onset of hemoglobin synthesis and slightly later than the expression of the major sialoglycoprotein of erythrocytes, glycophorin A. Glycophorin A did not, however, contain blood group A-activity when analyzed by immunoprecipitation and gel electrophoresis.


2017 ◽  
Author(s):  
D Pal ◽  
H Blair ◽  
S Boyd ◽  
P Bakelis ◽  
A Elder ◽  
...  

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