lewis-x-antigen and Leukemia--Erythroblastic--Acute

lewis-x-antigen has been researched along with Leukemia--Erythroblastic--Acute* in 2 studies

Other Studies

2 other study(ies) available for lewis-x-antigen and Leukemia--Erythroblastic--Acute

Article	Year
A carbohydrate structure associated with CD15 (Lewis x) on myeloid cells is a novel ligand for human CD2. Journal of immunology (Baltimore, Md. : 1950), 1996, Apr-15, Volume: 156, Issue:8 The T cell and NK cell adhesion molecule CD2 interacts with different ligands, viz, CD58, CD48, and CD59. Using a fluorescent multimeric construct of rCD2, we previously identified an additional CD2 ligand (CD2L) on the erythroleukemic cell line K562. CD2L bound to a different region of CD2 than known ligands and was N-glycosylation dependent. In this study we show that mAbs specific for the carbohydrate Ag Lewis x (CD15, Gal-beta 1-4 GlcNAc alpha 1-3Fuc) inhibit multimeric rCD2 binding to CD2L. CD2L is restricted in expression to myeloid cells, where it is co-expressed with CD58 on monocytes and is the dominant, if not sole, CD2 ligand on neutrophils. Sugar specificity studies show that CD2L is not CD15. Thus, whereas soluble Lewis x inhibits binding of CD15 mAb to K562 and neutrophils, binding of multimeric rCD2 is unaffected. Furthermore, multimeric rCD2 binding to K562 is inhibited by L-fucose and following treatment of K562 with an alpha 1-6 fucosidase, whereas these treatments do not inhibit the binding of CD15 mAb. Thus, it is likely that CD2L is a carbohydrate structure closely associated with, yet distinct from, CD15, which can be sterically blocked by CD15 mAb. Functional studies revealed that CD2L is probably an important CD2 ligand in the non-MHC-restricted NK cell killing of K562 target cells, since this activity was strongly inhibited by CD15 mAb. Collectively, this study indicates that a CD15 (Lewis x)-associated carbohydrate structure(s), which has previously been shown to be a selectin ligand, also may function as an important CD2 ligand on myeloid cells. Topics: Antibodies, Monoclonal; Antigen-Antibody Reactions; B-Lymphocytes; Binding, Competitive; Carbohydrate Sequence; CD2 Antigens; Epitopes; Hematopoietic Stem Cells; Humans; Leukemia, Erythroblastic, Acute; Lewis Blood Group Antigens; Lewis X Antigen; Ligands; Melanoma; Molecular Sequence Data; Structure-Activity Relationship; Tumor Cells, Cultured	1996
Studies on the susceptibility to NK-mediated lysis and the simultaneous expression of various surface molecules in anthracyclin-treated K562 cells and in four K562 cell clones. Immunology letters, 1992, Volume: 34, Issue:1 Target molecules for NK cells are unknown. Numerous studies have proposed putative target molecules, but have examined their role in the modulation of sensitivity to NK-mediated lysis one independently of each other. We examined the simultaneous expression of various surface molecules and the susceptibility of K562 cells to NK attack. We have previously shown that adriamycin (40 nM) and aclacinomycin (15 nM) can induce, in vitro, an increase of glycophorin A (GPA) on K562 cells, a modulation of transferrin receptor (TfR) and CD15 antigen expression and a significant resistance of cells to NK-mediated lysis. In the present work, Fc gamma receptor II (CD32) expression at the K562 cell membrane was clearly decreased after aclacinomycin-treatment but was unaltered by adriamycin-treatment. Four K562 cell clones were studied. Two clones (F and G) expressed a higher level of CD32 at the membrane (62% and 70% of erythrocyte antibody (EA) rosettes respectively) and two clones (9 and 19) expressed lower a level (18% and 7% EA rosettes respectively) than the original population (43%). The sensitivity to lysis by NK cells was increased in clones F, G and 9 but decreased in clone 19 (without alteration in the binding capacity). Relationships between the sensitivity to NK attack and the levels of simultaneous expression of CD32, TfR, CD15, glycophorin A (GPA) and MHC class I monomorphic antigens were studied. In addition, the presence at the membrane of some cellular adhesion molecules (CD54, CD58, CD29, CD18, CD56) was examined in anthracyclin-treated cells and in the four clones. The difference in the sensitivity of target cells to NK attack is not strictly related to variation of one or other of these molecules. Our previous and present data suggest that the resistance of K562 cells to NK cells may correlate with the level of erythroid maturation at the cell membrane, involving simultaneous variations in expression of several molecules such as a decrease of TfR, CD15 and CD32 and an increase of GPA. Topics: Aclarubicin; Antibiotics, Antineoplastic; Antigens, CD; Antigens, Surface; Cell Adhesion Molecules; Clone Cells; Cytotoxicity, Immunologic; Flow Cytometry; Glycophorins; Histocompatibility Antigens Class I; Humans; Killer Cells, Natural; Leukemia, Erythroblastic, Acute; Lewis X Antigen; Receptors, IgG; Receptors, Transferrin; Rosette Formation; Tumor Cells, Cultured	1992

Article

Year

A carbohydrate structure associated with CD15 (Lewis x) on myeloid cells is a novel ligand for human CD2.

Journal of immunology (Baltimore, Md. : 1950), 1996, Apr-15, Volume: 156, Issue:8

The T cell and NK cell adhesion molecule CD2 interacts with different ligands, viz, CD58, CD48, and CD59. Using a fluorescent multimeric construct of rCD2, we previously identified an additional CD2 ligand (CD2L) on the erythroleukemic cell line K562. CD2L bound to a different region of CD2 than known ligands and was N-glycosylation dependent. In this study we show that mAbs specific for the carbohydrate Ag Lewis x (CD15, Gal-beta 1-4 GlcNAc alpha 1-3Fuc) inhibit multimeric rCD2 binding to CD2L. CD2L is restricted in expression to myeloid cells, where it is co-expressed with CD58 on monocytes and is the dominant, if not sole, CD2 ligand on neutrophils. Sugar specificity studies show that CD2L is not CD15. Thus, whereas soluble Lewis x inhibits binding of CD15 mAb to K562 and neutrophils, binding of multimeric rCD2 is unaffected. Furthermore, multimeric rCD2 binding to K562 is inhibited by L-fucose and following treatment of K562 with an alpha 1-6 fucosidase, whereas these treatments do not inhibit the binding of CD15 mAb. Thus, it is likely that CD2L is a carbohydrate structure closely associated with, yet distinct from, CD15, which can be sterically blocked by CD15 mAb. Functional studies revealed that CD2L is probably an important CD2 ligand in the non-MHC-restricted NK cell killing of K562 target cells, since this activity was strongly inhibited by CD15 mAb. Collectively, this study indicates that a CD15 (Lewis x)-associated carbohydrate structure(s), which has previously been shown to be a selectin ligand, also may function as an important CD2 ligand on myeloid cells.

Topics: Antibodies, Monoclonal; Antigen-Antibody Reactions; B-Lymphocytes; Binding, Competitive; Carbohydrate Sequence; CD2 Antigens; Epitopes; Hematopoietic Stem Cells; Humans; Leukemia, Erythroblastic, Acute; Lewis Blood Group Antigens; Lewis X Antigen; Ligands; Melanoma; Molecular Sequence Data; Structure-Activity Relationship; Tumor Cells, Cultured

1996

Studies on the susceptibility to NK-mediated lysis and the simultaneous expression of various surface molecules in anthracyclin-treated K562 cells and in four K562 cell clones.

Immunology letters, 1992, Volume: 34, Issue:1

Target molecules for NK cells are unknown. Numerous studies have proposed putative target molecules, but have examined their role in the modulation of sensitivity to NK-mediated lysis one independently of each other. We examined the simultaneous expression of various surface molecules and the susceptibility of K562 cells to NK attack. We have previously shown that adriamycin (40 nM) and aclacinomycin (15 nM) can induce, in vitro, an increase of glycophorin A (GPA) on K562 cells, a modulation of transferrin receptor (TfR) and CD15 antigen expression and a significant resistance of cells to NK-mediated lysis. In the present work, Fc gamma receptor II (CD32) expression at the K562 cell membrane was clearly decreased after aclacinomycin-treatment but was unaltered by adriamycin-treatment. Four K562 cell clones were studied. Two clones (F and G) expressed a higher level of CD32 at the membrane (62% and 70% of erythrocyte antibody (EA) rosettes respectively) and two clones (9 and 19) expressed lower a level (18% and 7% EA rosettes respectively) than the original population (43%). The sensitivity to lysis by NK cells was increased in clones F, G and 9 but decreased in clone 19 (without alteration in the binding capacity). Relationships between the sensitivity to NK attack and the levels of simultaneous expression of CD32, TfR, CD15, glycophorin A (GPA) and MHC class I monomorphic antigens were studied. In addition, the presence at the membrane of some cellular adhesion molecules (CD54, CD58, CD29, CD18, CD56) was examined in anthracyclin-treated cells and in the four clones. The difference in the sensitivity of target cells to NK attack is not strictly related to variation of one or other of these molecules. Our previous and present data suggest that the resistance of K562 cells to NK cells may correlate with the level of erythroid maturation at the cell membrane, involving simultaneous variations in expression of several molecules such as a decrease of TfR, CD15 and CD32 and an increase of GPA.

Topics: Aclarubicin; Antibiotics, Antineoplastic; Antigens, CD; Antigens, Surface; Cell Adhesion Molecules; Clone Cells; Cytotoxicity, Immunologic; Flow Cytometry; Glycophorins; Histocompatibility Antigens Class I; Humans; Killer Cells, Natural; Leukemia, Erythroblastic, Acute; Lewis X Antigen; Receptors, IgG; Receptors, Transferrin; Rosette Formation; Tumor Cells, Cultured

1992