scholarly journals Expression of the major sialoglycoprotein (glycophorin) on erythroid cells in human bone marrow

Blood ◽  
1978 ◽  
Vol 52 (2) ◽  
pp. 379-387 ◽  
Author(s):  
CG Gahmberg ◽  
M Jokinen ◽  
LC Andersson
Keyword(s):  
Bone Marrow ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Human Erythrocyte ◽  
Bone Marrow Cells ◽  
Protein A ◽  
Human Bone ◽  
Erythrocyte Membranes ◽  
Erythroid Cells ◽  
Human Erythrocyte Membranes

Abstract The major sialoglycoprotein of human erythrocyte membranes (glycophorin) is one of the most-studied membrane proteins. Although the structure is relatively well known, almost nothing is known about its expression in erythroid cells. To study this we raised an antiserum that reacted specifically with this protein. This was accomplished by immunization of rabbits with a preparation of glycophorin followed by absorption with En(a-) erythrocyte membranes, which lack glycophorin. By use of this antiserum and a staphylococcus protein A technique we could establish that only bone marrow cells of erythrocyte lineage express glycophorin at the cell surface. This occurs in basophilic normoblasts and later stages of erythrocyte differentiation, whereas pronormoblasts do not seem to contain glycophorin.

scholarly journals Expression of the major sialoglycoprotein (glycophorin) on erythroid cells in human bone marrow

Blood ◽  
1978 ◽  
Vol 52 (2) ◽  
pp. 379-387 ◽  
Author(s):  
CG Gahmberg ◽  
M Jokinen ◽  
LC Andersson
Keyword(s):  
Bone Marrow ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Human Erythrocyte ◽  
Bone Marrow Cells ◽  
Protein A ◽  
Human Bone ◽  
Erythrocyte Membranes ◽  
Erythroid Cells ◽  
Human Erythrocyte Membranes

The major sialoglycoprotein of human erythrocyte membranes (glycophorin) is one of the most-studied membrane proteins. Although the structure is relatively well known, almost nothing is known about its expression in erythroid cells. To study this we raised an antiserum that reacted specifically with this protein. This was accomplished by immunization of rabbits with a preparation of glycophorin followed by absorption with En(a-) erythrocyte membranes, which lack glycophorin. By use of this antiserum and a staphylococcus protein A technique we could establish that only bone marrow cells of erythrocyte lineage express glycophorin at the cell surface. This occurs in basophilic normoblasts and later stages of erythrocyte differentiation, whereas pronormoblasts do not seem to contain glycophorin.

scholarly journals Effects of Roundup® Pesticide on the Stability of Human Erythrocyte Membranes and Micronuclei Frequency in Bone Marrow Cells of Swiss Mice

2011 ◽  
Vol 4 (1) ◽  
pp. 54-59 ◽  
Author(s):  
Humberto G. Rodrigues ◽  
Nilson G. Rodrigues ◽  
Mariana Ferreira Pereira de Araujo ◽  
Hisao Nishijo ◽  
Tales A. Aversi-Ferreira
Keyword(s):  
Bone Marrow ◽  
Human Erythrocyte ◽  
Bone Marrow Cells ◽  
Erythrocyte Membranes ◽  
Swiss Mice ◽  
Human Erythrocyte Membranes ◽  
The Stability ◽  
Marrow Cells

Ku80 autoantigen as a cellular coreceptor for human parvovirus B19 infection

Blood ◽  
2005 ◽  
Vol 106 (10) ◽  
pp. 3449-3456 ◽  
Author(s):  
Yasuhiko Munakata ◽  
Takako Saito-Ito ◽  
Keiko Kumura-Ishii ◽  
Jie Huang ◽  
Takao Kodera ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Cell Surface ◽  
Cell Lines ◽  
Bone Marrow Cells ◽  
Parvovirus B19 ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Human Parvovirus B19 ◽  
Erythroid Cells ◽  
Interfering Rna

AbstractHuman parvovirus B19 (B19) infects human erythroid cells expressing P antigen. However, some cell lines that were positive for P antigen failed to bind B19, whereas some cell lines had an ability to bind B19 despite undetectable expression of P antigen. We here demonstrate that B19 specifically binds with Ku80 autoantigen on the cell surface. Furthermore, transfection of HeLa cells with the gene of Ku80 enabled the binding of B19 and allowed its entry into cells. Moreover, reduction of cell-surface expression of Ku80 in KU812Ep6 cells, which was a high-sensitive cell line for B19 infection, by short interfering RNA for Ku80 resulted in the marked inhibition of B19 binding in KU812Ep6 cells. Although Ku80 originally has been described as a nuclear protein, human bone marrow erythroid cells with glycophorin A or CD36, B cells with CD20, or T cells with CD3 were all positive for cell-surface expression of Ku80. B19 infection of KU812Ep6 cells and bone marrow cells was inhibited in the presence of anti-Ku80 antibody. Our data suggest that Ku80 functions as a novel coreceptor for B19 infection, and this finding may provide an explanation for the pathologic immunity associated with B19 infection.

scholarly journals Expression of blood group A antigens in human bone marrow cells

Blood ◽  
1981 ◽  
Vol 57 (1) ◽  
pp. 147-151 ◽  
Author(s):  
KK Karhi ◽  
LC Andersson ◽  
P Vuopio ◽  
CG Gahmberg
Keyword(s):  
Bone Marrow ◽  
Blood Group ◽  
Bone Marrow Cells ◽  
Protein A ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Glycophorin A ◽  
Blood Group A ◽  
Group A ◽  
Marrow Cells

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.

scholarly journals Labelling of the intramembranous region of the major sialoglycoprotein of human erythrocytes with a photosensitive hydrophobic probe

1979 ◽  
Vol 179 (2) ◽  
pp. 265-272 ◽  
Author(s):  
E Wells ◽  
J B Findlay
Keyword(s):  
Membrane Proteins ◽  
Human Erythrocyte ◽  
Human Erythrocytes ◽  
Labelling Pattern ◽  
Erythrocyte Membranes ◽  
Transmembrane Region ◽  
Human Erythrocyte Membranes ◽  
Hydrophobic Probe

Human erythrocyte membranes were incubated with the photosensitive hydrophobic reagent 1-azido-r-iodo[3H]benzene and the mixture was irradiated. The major sialoglycoprotein was then isolated and the labelled polypeptide subjected to proteolytic dissection. Characterization of the purified tryptic and chymotryptic peptides show that the probe is covalently attached only to the transmembrane region of the protein. This labelling pattern is discussed in relation to the use of such reagents for the identification of segments of membrane proteins exposed to the hydrophobic millieu of the membrane.

Human erythrocyte membrane proteins of zone 4.5 exist as families of related proteins

1985 ◽  
Vol 248 (1) ◽  
pp. C70-C79 ◽  
Author(s):  
C. F. Whitfield ◽  
D. B. Coleman ◽  
M. M. Kay ◽  
K. A. Shiffer ◽  
J. Miller ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Human Erythrocyte ◽  
Peptide Mapping ◽  
Protein Composition ◽  
Cross Reactivity ◽  
Erythrocyte Membranes ◽  
Two Dimensional ◽  
Coomassie Blue ◽  
Human Erythrocyte Membranes ◽  
Mapping Techniques

An analysis of the polypeptide composition of zone 4.5 of human erythrocyte membranes has been done by immunoautoradiographic and two-dimensional peptide mapping techniques. Results of these studies demonstrated that the Coomassie blue profile was constant, with 14 well-resolved bands present. Zone 4.5 polypeptides existed as at least four families of two or more components with closely related polypeptide backbones. The families could be distinguished on the basis of their extraction characteristics, immunological cross-reactivity, and two-dimensional peptide maps. One family was related to protein 4.1, one family was related to band 3, and two families were independent and not similar to other larger membrane proteins. The data show that all of the visualized bands in zone 4.5 do not have the same protein composition and that several closely related forms of some polypeptides are present.

scholarly journals Simultaneous measurement of DNA content and cell-surface immunofluorescence of human bone marrow cells using a single laser flow cytometer

Cytometry ◽  
1990 ◽  
Vol 11 (7) ◽  
pp. 837-844 ◽  
Author(s):  
Paul P. T. Brons ◽  
Arie H. M. Pennings ◽  
Clemens Haanen ◽  
Hans M. C. Wessels ◽  
Jan B. M. Boezeman
Keyword(s):  
Bone Marrow ◽  
Cell Surface ◽  
Dna Content ◽  
Simultaneous Measurement ◽  
Bone Marrow Cells ◽  
Flow Cytometer ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Single Laser ◽  
Marrow Cells

scholarly journals The 175 antigen expressed on myeloid and erythroid cells during differentiation is associated with serine protease activity

Blood ◽  
1995 ◽  
Vol 85 (5) ◽  
pp. 1215-1219 ◽  
Author(s):  
D Deane ◽  
L Inglis ◽  
D Haig
Keyword(s):  
Monoclonal Antibody ◽  
Bone Marrow ◽  
Cell Surface ◽  
Serine Protease ◽  
Protease Activity ◽  
Bone Marrow Cells ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecylsulfate ◽  
Erythroid Cells ◽  
Serine Protease Activity

Monoclonal antibody 175 recognizes a cell-surface antigen on more than 80% of nucleated ovine bone marrow cells (BMC). The distribution is unusual, as the majority of differentiated myeloid and erythroid cells express the antigen (175 antigen), whereas mast cells, basophils, and the majority of lymphocytes do not. The level of 175 antigen expression has been shown to increase as BMC differentiate during hematopoiesis. Previous attempts to identify the 175 antigen have been unsuccessful. In this study, the 175 antigen was affinity-purified and shown to contain serine protease activity. Immunoblot analysis following sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) of bone marrow cell lysates run under reducing or nonreducing conditions showed two closely adjacent protein bands (a doublet) of 28 to 30 kD molecular weight. N-linked deglycosylation showed that the 30-kD band was a glycosylated form of the 28-kD protein. Both protein bands shared the same N-terminal amino acid sequence over 20 residues, with high homology with serine proteases. Affinity-purified 175 antigen was proteolytic in substrate gels, the activity being inhibited by the 175 monoclonal antibody (Mab) and the serine protease inhibitor phenylmethylsulfonyl fluoride (PMSF), but not by metallo, thiol, or acid protease-specific inhibitors. The 175 antigen is therefore part of a growing family of cell-surface proteases associated with hematopoietic cell differentiation.

scholarly journals Expression of blood group A antigens in human bone marrow cells

Blood ◽  
1981 ◽  
Vol 57 (1) ◽  
pp. 147-151
Author(s):  
KK Karhi ◽  
LC Andersson ◽  
P Vuopio ◽  
CG Gahmberg
Keyword(s):  
Bone Marrow ◽  
Blood Group ◽  
Bone Marrow Cells ◽  
Protein A ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Glycophorin A ◽  
Blood Group A ◽  
Group A ◽  
Marrow Cells

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.

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