Glycophorin a as a cell surface marker of early erythroid differentiation in acute leukemia

Andersson, Leif C.; Gahmberg, Carl G.; Teerenhovi, Lasse; Vuopio, P

doi:10.1002/ijc.2910240603

Cited by 72 publications

(21 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Normal morphologically distinguishable erythroid cells, similar to megaloblasts in pernicious anemia and AEL cells, were clearly positive, however. This is in contrast to the observations made by Anderson et a1 [3,4]. When studying the expression of GpA on leukemic blast cells with a rabbit anti-GpA antiserum, they found positive reactions in 3 of 15 cases [3] and later in 6 of 51 cases 141.…”

Section: Discussioncontrasting

confidence: 83%

See 1 more Smart Citation

Glycophorin a expression in malignant hematopoiesis

et al. 1983

View full text Add to dashboard Cite

Two hundred twenty-nine patients with hematopoietic malignancies were tested for reactivity with a monoclonal anti-human glycophorin A antibody. One hundred twenty-three of these cases were classified as acute leukemias of either the myeloid, lymphoid, erythroid, or undifferentiated type. The monoclonal antibody we used (VIE-G4) was obtained after immunization with a human thymocyte suspension. It selectively reacts with glycophorin A (GpA) and strongly binds to 40% of K-562 cells and all morphologically recognizable erythroid precursor cells. Apart from two cases with acute erythroid leukemia, this antibody reacted with none of the malignant cells in the 229 tested hematopoietic malignancies, including the 121 nonerythroid acute leukemias. This finding seems to contradict the earlier observations by L. Andersson and colleagues that a considerable proportion of acute leukemias express GpA on their surface. One reason for this discrepancy might be the fact that VIE-G4 detects only complete glycosylated GpA. If this is the sole explanation, this would mean that the poorly differentiated cells in these cases express incompletely glycosylated GpA.

show abstract

Section: Discussioncontrasting

confidence: 83%

“…It was therefore suggested [3] that GpA may provide a useful marker for the red cell lineage. The potential importance of such a marker has been further substantiated by the observation of Andersson et a1 that a large proportion of leukemic blast cells from 6 of 51 patients with acute leukemia reacted with a rabbit anti-GpA antiserum [4].…”

Section: Introductionmentioning

confidence: 99%

Glycophorin a expression in malignant hematopoiesis

et al. 1983

View full text Add to dashboard Cite

show abstract

“…We have earlier reported that the malignant blasts in a significant proportion (610%) of undifferentiated acute leukemias carry surface structures that react with rabbit anti-GPA antiserum (41). Using monoclonal antibodies to GPA for the phenotyping of leukemic cells, only occasional reactivity is found (22,42).…”

Section: Discussionmentioning

confidence: 99%

Differentiation of human erythroid cells is associated with increased O-glycosylation of the major sialoglycoprotein, glycophorin A.

Gahmberg¹,

Ekblom²,

Andersson³

1984

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Glycophorin A, the major human erythrocyte sialoglycoprotein, is found exclusively on cells of the erythroid lineage. The amino acid sequence is known, and glycophorin A isolated from mature erythrocytes contains a single N-glycosidic and 15 O-glycosidic oligosaecharides. Monoclonal antibodies against erythrocyte glycophorin A reacted weakly with erythroid precursors while a monospecific rabbit antiserum reacted strongly with immature and mature red cells.Glycophorin A was isolated from cells representing various stAges of erythropoiesis in normal bone miarirow, from blood cells of neonates with erythroblastosis fetalis, and from the erythroleukemic cell lines K562 and HEL before and after induced differentiation. Analysis of the oligosaccharides showed less O-glycosylation of glycophorin A in erythroid precursors.The degree of glycosylation increased concomitantly with differentiation.The major sialoglycoprotein of human erythrocytes, glycophorin A (GPA), consists of 131 amino acids distributed in three separate domains: at the cell surface, within the lipid bilayer, and in the cytoplasm (1). The external NH2-terminal portion is highly glycosylated, containing one N-glycosidic oligosaccharide at Asn-26 and 15 O-glycosidic oligosaccharides. The structure of the N-glycosidic oligosaccharide has been determined (2). Most O-glycosidic oligosaccharides have the structure Neu5Aca2-3Gall31-3(Neu5Aca2-6)GalNAc (ref. It was shown that GPA is confined to the erythroid cell lineage and appears at the basophilic normoblast stage of erythropoiesis (5, 6). GPA is also found on the erythroleukemia cell lines K562 (7) and HEL (8,9). The biosynthesis of the protein has been extensively studied in K562 cells and its N-and O-glycosylations have been elucidated (10-12).We have now isolated GPA from normal bone marrow precursor cells and from the K562 and HEL cell lines before and after induction of differentiation, and we have studied its oligosaccharides. Our

show abstract

“…Incubation with dimethyl sulfoxide (Me2SO) induces HL-60 to maturate into myelocytes and granulocytes (9) which have acquired functional properties characteristic of these cells (10). In contrast, the phorbol ester 12-0-tetradecanoylphorbol 13-acetate (TPA) induces differentiation ofHL-60 along the monocyte/macrophage pathway, with a concomitant increase in phagocytic capacity and adherence to plastic surfaces (11).…”

mentioning

confidence: 99%

“…Other cell lines of putative myeloid origin include K562 (12) which, by both immunological (13) and biochemical (14) criteria, is an erythroleukemic cell line, and the early myeloid cell line KG-1, which expresses the HLA-DR antigen (15,16). The relatively mature character of HL-60 is further evidenced by its lack of HLA-DR antigen normally present on myeloblasts (17).…”

mentioning

confidence: 99%

Characterization, by immunoprecipitation, of myeloid- and monocyte-specific antigens present on the human promyelocytic cell line (HL-60) in three stages of differentiation.

Mulder¹,

Alexander²,

Engelfriet³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The human promyelocytic leukemia cell line HL-60 is reactive with an antiserum raised against normal human granulocytes (AGS). Immunoprecipitation with AGS on [ S]methioninelabeled HL-60 cell lysates with subsequent analysis by NaDodSO4/polyacrylamide slab gel electrophoresis shows a major antigenic doublet with molecular weights-of 88,000 and 86,000, together with some minor antigens of lower molecular weight. Upon stimulation with dimethyl sulfoxide or 12-O-tetradecanoylphorbol 13-acetate, which induces HL-60 to differentiate to mature granulocytes or monocytes/macrophages, respectively, this antigenic doublet disappears. 12-O-Tetradecanoylphorbol 13-acetate induces the synthesis of an antigen, molecular weight 83,000, reactive with an antimonocyte serum. Neutrophil-specific alloantigens were not detected on HL-60 or its differentiated derivatives.With the aid of the appropriate human antisera in leukoagglutination or indirect immunofluorescence assays, several neutrophil-specific alloantigen systems have been detected on human granulocytes (1-4). In addition, neutrophil-specific xenogeneic antisera have been produced (5-7).Recently, a human leukemic cell line (HL-60) has been established from the peripheral blood of a patient with acute promyelocytic leukemia, which shows myeloid characteristics (8). Morphologically, the cultured HL-60 cells are predominantly promyelocytes, although some mature myelocytic cells are also present. Furthermore, cells of this cell line can be induced to differentiate in culture. Incubation with dimethyl sulfoxide (Me2SO) induces HL-60 to maturate into myelocytes and granulocytes (9) which have acquired functional properties characteristic of these cells (10). In contrast, the phorbol ester 12-0-tetradecanoylphorbol 13-acetate (TPA) induces differentiation ofHL-60 along the monocyte/macrophage pathway, with a concomitant increase in phagocytic capacity and adherence to plastic surfaces (11).Other cell lines of putative myeloid origin include K562 (12) which, by both immunological (13) and biochemical (14) criteria, is an erythroleukemic cell line, and the early myeloid cell line KG-1, which expresses the HLA-DR antigen (15, 16). The relatively mature character of HL-60 is further evidenced by its lack of HLA-DR antigen normally present on myeloblasts (17).In this study, antigens present on HL-60 at its various stages of differentiation were detected by immunofluorescence with a set of reagents that included xenogeneic-antisera with specificity for granulocytes and monocytes, respectively. We further analyzed these antigens by immunoprecipitation on radioactively labeled cell lysates, followed by NaDodSOjpolyacrylamide gel electrophoresis. This study has potentially important consequences for analysis of antigens on leukemic cells present in patients with chronic myeloid leukemia and acute myeloblastic leukemia. MATERIALS AND METHODS Cell Lines and Conditions for Growth and Differentiation.The continuous suspension cell lines used in this study were HL-60 (8), K562 (12), ...

show abstract

Glycophorin a as a cell surface marker of early erythroid differentiation in acute leukemia

Cited by 72 publications

References 18 publications

Glycophorin a expression in malignant hematopoiesis

Glycophorin a expression in malignant hematopoiesis

Differentiation of human erythroid cells is associated with increased O-glycosylation of the major sialoglycoprotein, glycophorin A.

Characterization, by immunoprecipitation, of myeloid- and monocyte-specific antigens present on the human promyelocytic cell line (HL-60) in three stages of differentiation.

Contact Info

Product

Resources

About