scholarly journals Monoclonal antibody YB5.B8 identifies the human c-kit protein product

Blood ◽  
1991 ◽  
Vol 77 (9) ◽  
pp. 1876-1883 ◽  
Author(s):  
NB Lerner ◽  
KH Nocka ◽  
SR Cole ◽  
FH Qiu ◽  
A Strife ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Mast Cells ◽  
Cell Surface ◽  
Bone Marrow Cells ◽  
Protein Product ◽  
Surface Glycoprotein ◽  
Leukemic Cells ◽  
Acute Myelocytic Leukemia ◽  
Erythroid Progenitors ◽  
Cell Surface Glycoprotein

Abstract The c-kit proto-oncogene encodes a 145- to 160-Kd transmembrane tyrosine kinase, which is a member of the platelet-derived growth factor receptor family and is allelic with the murine white spotting locus (W). W mutations affect several aspects of hematopoiesis, most notably erythroid progenitors and mast cells. A monoclonal antibody, YB5.B8, had been raised against the leukemic blasts of a patient with M1-type acute myelocytic leukemia (AML) and it precipitates a 150-Kd cell surface glycoprotein from leukemic cells. The YB5.B8 epitope is expressed on mast cells, on up to 3% of normal mononuclear bone marrow cells, and it identifies a sub-group of AML patients with a poor prognosis. In view of similarities noted between the cell surface antigen identified by YB5.B8 and the c-kit protein product, we performed experiments to determine whether they are identical. c-kit RNA expression in the cell lines HEL (human erythroleukemia) and A172 (glioblastoma) was shown to parallel the expression of the YB5.B8 epitope in these lines as measured by flow cytometry. Immunoprecipitation analysis with anti-kit serum and YB5.B8 antibody indicated that the two antibodies identified proteins of identical size in HEL (155 Kd) and A172 (145 Kd) cells, and sequential immunoprecipitations with the kit and the YB5.B8 antibodies demonstrated that the two antibodies recognize the same molecule. The proteins identified by both the anti-kit and YB5.B8 antibodies displayed in vitro autophosphorylation activity in immune complex kinase assays. In addition, YB5.B8 was able to inhibit the binding of the kit ligand to HEL cells. These studies provide evidence that the YB5.B8 antigen and the c-kit protein product are identical and raise certain hypotheses regarding the role of c-kit in AML.

scholarly journals Monoclonal antibody YB5.B8 identifies the human c-kit protein product

Blood ◽  
1991 ◽  
Vol 77 (9) ◽  
pp. 1876-1883 ◽  
Author(s):  
NB Lerner ◽  
KH Nocka ◽  
SR Cole ◽  
FH Qiu ◽  
A Strife ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Mast Cells ◽  
Cell Surface ◽  
Bone Marrow Cells ◽  
Protein Product ◽  
Surface Glycoprotein ◽  
Leukemic Cells ◽  
Acute Myelocytic Leukemia ◽  
Erythroid Progenitors ◽  
Cell Surface Glycoprotein

The c-kit proto-oncogene encodes a 145- to 160-Kd transmembrane tyrosine kinase, which is a member of the platelet-derived growth factor receptor family and is allelic with the murine white spotting locus (W). W mutations affect several aspects of hematopoiesis, most notably erythroid progenitors and mast cells. A monoclonal antibody, YB5.B8, had been raised against the leukemic blasts of a patient with M1-type acute myelocytic leukemia (AML) and it precipitates a 150-Kd cell surface glycoprotein from leukemic cells. The YB5.B8 epitope is expressed on mast cells, on up to 3% of normal mononuclear bone marrow cells, and it identifies a sub-group of AML patients with a poor prognosis. In view of similarities noted between the cell surface antigen identified by YB5.B8 and the c-kit protein product, we performed experiments to determine whether they are identical. c-kit RNA expression in the cell lines HEL (human erythroleukemia) and A172 (glioblastoma) was shown to parallel the expression of the YB5.B8 epitope in these lines as measured by flow cytometry. Immunoprecipitation analysis with anti-kit serum and YB5.B8 antibody indicated that the two antibodies identified proteins of identical size in HEL (155 Kd) and A172 (145 Kd) cells, and sequential immunoprecipitations with the kit and the YB5.B8 antibodies demonstrated that the two antibodies recognize the same molecule. The proteins identified by both the anti-kit and YB5.B8 antibodies displayed in vitro autophosphorylation activity in immune complex kinase assays. In addition, YB5.B8 was able to inhibit the binding of the kit ligand to HEL cells. These studies provide evidence that the YB5.B8 antigen and the c-kit protein product are identical and raise certain hypotheses regarding the role of c-kit in AML.

A new brain cell surface glycoprotein identified by monoclonal antibody

Neuroscience ◽  
1982 ◽  
Vol 7 (1) ◽  
pp. 239-250 ◽  
Author(s):  
M. Hirn ◽  
M. Pierres ◽  
H. Deagostini-Bazin ◽  
M.R. Hirsch ◽  
C. Goridis ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Brain Cell ◽  
Surface Glycoprotein ◽  
Cell Surface Glycoprotein

scholarly journals Production of a monoclonal antibody against cell-surface glycoprotein of guinea pig adrenocortical cells.

1993 ◽  
Vol 41 (2) ◽  
pp. 235-243 ◽  
Author(s):  
Y Kameda ◽  
C Hirota
Keyword(s):  
Monoclonal Antibody ◽  
Sialic Acid ◽  
Cell Surface ◽  
Guinea Pig ◽  
Plasma Membranes ◽  
Surface Glycoprotein ◽  
Zona Fasciculata ◽  
Cell Surface Antigens ◽  
Adrenocortical Cells ◽  
Cell Surface Glycoprotein

A monoclonal antibody (MAb) that reacted with the cell-surface antigens of adrenocortical cells was generated against cell suspensions from guinea pig adrenal glands. Cell-surface membranes of the adrenocortical cells in all zones, i.e., zona glomerulosa, zona fasciculata, and zona reticularis, were labeled with the antibody. Adrenal medulla remained unlabeled. Immunoelectron microscopy showed that entire plasma membranes, i.e., plasma membranes between adjacent cells and free cell-surface membranes, including sinusoidal microvilli, were immunoreactive to the antibody. Immunoblot analysis demonstrated that the antibody bound to two prominent bands at molecular weights of approximately 62,000 and 110,000. Two bands were stained with lectin-digoxigenin conjugates. The 110 KD band reacted with Datura stramonium (DSA) and Maackia amurensis (MAA) agglutinins, indicating the presence of N-acetyl-glucosamine and sialic acid-linked alpha (2-3) to galactose; the 62 KD band reacted with SNA, indicating the presence of sialic acid-linked alpha (2-6) to galactose. In adrenocortical cells, the reaction pattern of Sambucus nigra (SNA) agglutinin was similar to that of the (MAb), whereas reaction patterns of DSA and MAA were different. Both neuraminidase digestion and prior absorption of the antibody with N-acetyl-neuraminic acid completely prevented the immunolabeling of adrenocortical cells. These results indicate that the MAb mainly recognizes the 2-6 sialylated cell-surface antigen of adrenocortical cells.

scholarly journals Identification of Fc epsilon RIneg mast cells in mouse bone marrow cell cultures. Use of a monoclonal anti-p161 antibody.

1995 ◽  
Vol 182 (2) ◽  
pp. 575-579 ◽  
Author(s):  
C A Kinzer ◽  
A D Keegan ◽  
W E Paul
Keyword(s):  
Bone Marrow ◽  
Mast Cell ◽  
Mast Cells ◽  
Bone Marrow Cells ◽  
Marrow Cell ◽  
Surface Glycoprotein ◽  
Mouse Bone Marrow ◽  
Short Term ◽  
Mouse Bone Marrow Cell ◽  
Cell Surface Glycoprotein

A monoclonal hamster antibody (K-1) specific for a 161-kD mast cell surface glycoprotein was derived. p161 is expressed on normal and cultured mast cells and on some macrophages, but not on basophils or other hematopoietic cells. A population of Fc epsilon Rneg cells expressing p161 was found in short term cultures of bone marrow cells grown in interleukin (IL)-3. These cells were purified and propagated for extended periods in IL-3. They express c-kit and Fc gamma RII/III, contain alcian blue-positive granules and histamine, and secrete IL-3 in response to ionomycin treatment. Their morphology is consistent with that of mast cells. We propose that they represent Fc epsilon RIneg mast cells that can be detected and purified because of their p161 expression.

Monoclonal antibody against cell surface glycoprotein of neurons

1981 ◽  
Vol 214 (2) ◽  
pp. 433-439 ◽  
Author(s):  
M. Hirn ◽  
M. Pierres ◽  
H. Deagostini-Bazin ◽  
M. Hirsch ◽  
C. Goridis
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Surface Glycoprotein ◽  
Cell Surface Glycoprotein
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