Use of a monoclonal antibody recognizing a cell surface determinant to distinguish prestalk and prespore cells of Dictyostelium discoideum slugs

Development ◽  
1985 ◽  
Vol 88 (1) ◽  
pp. 15-24
Author(s):  
Marianne Krefft ◽  
Ludwig Voet ◽  
James H. Gregg ◽  
Keith L. Williams
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Dictyostelium Discoideum ◽  
Antigenic Determinant ◽  
Developmental Stages ◽  
Double Labelling ◽  
Spore Surface ◽  
Cell Sorter ◽  
A Cell

Double labelling experiments on Dictyostelium discoideum cells at different developmental stages were carried out using monoclonal antibodies MUD1 (prespore specific), MUD9 (strong label on prestalk and anterior-like cells) and a fluorescence-activated cell sorter. The monoclonal antibody MUD9, which recognizes the surface of prestalk and anterior-like cells strongly and prespore cells weakly, is also present on the surface of vegetative amoebae and on mature stalk cells but not on the spore surface. Sharing of an antigenic determinant between vegetative, prestalk and anterior-like cells is consistent with these cells being ‘less differentiated’ than prespore cells.

A scale associated protein of Apedinella radians (Pedinellophyceae) and its possible role in the adhesion of surface components

1993 ◽  
Vol 104 (2) ◽  
pp. 391-398
Author(s):  
A. Koutoulis ◽  
M. Ludwig ◽  
R. Wetherbee
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cell Membrane ◽  
Cell Surface ◽  
Immunofluorescence Microscopy ◽  
Endomembrane System ◽  
Thin Sections ◽  
Specific Location ◽  
Whole Cells

Monoclonal antibodies have been generated against cell surface components of the unicellular phytoflagellate Apedinella radians (Pedinellophyceae). One monoclonal antibody, designated Arg 1E5/1B1, labels a scale associated protein (SAP) of 145 kDa. Immunofluorescence microscopy of whole cells as well as immunoelectron microscopy of whole cell mounts and thin sections using Arg 1E5/1B1 have shown that the SAP is located on the proximal surface of body scales and spine-scales. Its specific location suggests that the SAP may play a role in the adhesion of these surface components to the cell membrane and/or to one another. The potential of monoclonal antibody Arg 1E5/1B1 as a tool to study cell surface morphogenesis and the role of the endomembrane system in A. radians is discussed.

Expression of a surface epitope on cells that link branches in the tracheal network of Manduca sexta

Development ◽  
1990 ◽  
Vol 110 (3) ◽  
pp. 681-688 ◽  
Author(s):  
J.B. Nardi
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Manduca Sexta ◽  
Abdominal Segment ◽  
Western Blots ◽  
Tracheal Epithelial Cells ◽  
A Cell ◽  
Tracheal Epithelial ◽  
Thoracic And Abdominal ◽  
Small Subpopulation

A monoclonal antibody (MAb 2F5) to a cell surface epitope labels a small subpopulation of tracheal epithelial cells in each thoracic and abdominal segment of Manduca. These cells (nodes) represent the sites within the tracheal network at which invaginating tracheal tubes join during embryonic establishment of the tracheal network. Tracheal nodes are also the sites at which tracheal cuticle fractures during each molt. Since tracheal cuticle is shed through each spiracle, a tracheal node lies between each pair of contralateral spiracles within a segment (commissural node) and between each pair of adjacent, ipsilateral spiracles (lateral longitudinal node). MAb 2F5 first labels presumptive nodal cells of tracheal epithelium immediately prior to the linking of epithelial tubes from successive and opposite spiracles. One cell at the tip of each invaginating tracheal branch labels with MAb 2F5. The highly localized expression of the cell surface epitope recognized by MAb 2F5 may be instrumental in the orderly coupling of tracheal branches during embryonic development. On the basis of immunolabeling of Western blots and tissues, MAb 2F5 is believed to recognize Manduca fasciclin II, a member of a class of molecules involved in cell adhesion/recognition.

Immunotherapy of Mouse Leukemia with Monoclonal Antibodies Directed against Type-C Virus Structural Proteins

1984 ◽  
Vol 70 (1) ◽  
pp. 9-16
Author(s):  
Mauro Boiocchi ◽  
Piera Mondellini
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Therapeutic Effect ◽  
Structural Proteins ◽  
Leukemia Cells ◽  
Envelope Glycoproteins ◽  
Mouse Leukemia ◽  
Type C

The monoclonal antibody A6, isolated during a study on the natural immunoresponse of BALB/c mice against leukemia cells (4), reacts with the envelope glycoproteins gp70 of the MuLV and with the cell surface of the SL2 AKR leukemia. In the present paper, we describe the in vivo immunotherapeutic effect exerted by the A6 monoclonal antibody on the growth of the transplanted leukemia SL2. The greater therapeutic effect observed when the A6 was used with exogenous complement cooperation suggests that the immunotherapeutic activity is mediated by C'-dependent cytotoxicity.

scholarly journals A monoclonal antibody identifying a cell surface antigen shared by common acute lymphoblastic leukemias and B lineage cells

Blood ◽  
1980 ◽  
Vol 56 (6) ◽  
pp. 1141-1144 ◽  
Author(s):  
MF Greaves ◽  
W Verbi ◽  
J Kemshead ◽  
R Kennett
Keyword(s):  
Monoclonal Antibody ◽  
B Cells ◽  
Cell Surface ◽  
Lymphoblastic Leukemia ◽  
Blast Crisis ◽  
Fetal Brain ◽  
Lymphocytic Leukemia ◽  
Cell Surface Antigens ◽  
A Cell ◽  
B Lineage

Abstract A monoclonal antibody designated PI153/3, which reacts with neuroblastoma and fetal brain, is shown to identify also a cell surface determinant shared by pre-B and mature B cells and their corresponding leukemias including chronic lymphocytic leukemia, non-Hodgkin's lymphoma, B acute lymphoblastic leukemia, and hairy cell leukemia, but not plasmacytoma. Almost all non-T, non-B acute “lymphoid” leukemias bind PI153/3. The latter includes 71 of 74 common ALL tested, most but not all “unclassified” or “null” ALL and cases of both acute undifferentiated leukemia and Ph1 positive chronic myeloid leukemia in blast crisis with common ALL phenotypes. The antigen is absent or present at very low density on normal and leukemic T lymphocyte, myeloid and erythroid cells. The determinant appears to co-redistribute with cell surface immunoglobulin in B lymphocytes and segregates independently of other cell surface antigens associated with B cells and/or cALL including HLA-DR (Ia-like antigens) and the cALL (gp 100) antigen.

Monoclonal antibody 9C4 recognizes epithelial cellular adhesion molecule, a cell surface antigen expressed in early steps of erythropoiesis

2002 ◽  
Vol 30 (6) ◽  
pp. 537-545 ◽  
Author(s):  
Reiner Lammers ◽  
Christina Giesert ◽  
Frank Grünebach ◽  
Anke Marxer ◽  
Wichard Vogel ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Surface Antigen ◽  
Adhesion Molecule ◽  
Cellular Adhesion ◽  
Cell Surface Antigen ◽  
Cellular Adhesion Molecule ◽  
A Cell

Antibody localization in human renal cell carcinoma: a phase I study of monoclonal antibody G250.

1993 ◽  
Vol 11 (4) ◽  
pp. 738-750 ◽  
Author(s):  
E Oosterwijk ◽  
N H Bander ◽  
C R Divgi ◽  
S Welt ◽  
J C Wakka ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Monoclonal Antibody ◽  
Cell Surface ◽  
Cell Carcinoma ◽  
Surface Antigen ◽  
Renal Cell ◽  
Clear Cell ◽  
Cell Surface Antigen ◽  
Human Renal Cell Carcinoma ◽  
A Cell

PURPOSE To define the imaging and biodistribution characteristics of iodine 131-labeled monoclonal antibody (mAb) G250 (131I-mAbG250), which recognizes a cell-surface antigen expressed by human renal cell carcinoma (RCC). PATIENTS AND METHODS G250 is a cell-surface antigen recognized by mAbG250 expressed by RCC but not detected in normal kidney. Clear-cell RCC, the most frequent form of RCC, shows homogeneous expression of G250, whereas non-clear-cell RCC and cancers derived from other organs generally do not express G250. Expression in normal tissues is highly restricted and limited to large bile ducts and gastric epithelium. 131I-mAbG250 was administered intravenously (IV) to 16 patients with RCC 7 to 8 days before surgery at five dose levels, with at least three patients entered at each dose level. RESULTS Clear tumor images were observed in 12 patients with G250-positive tumors and in one of three patients with G250-negative tumors. Imaged lesions in the peritoneal cavity were confirmed at surgery. The smallest lesion visualized was 8 mm in diameter. The specificity of 131I-mAbG250 localization to tumor tissue was established by radioactivity measurements, autoradiography, and immunohistochemistry of biopsied tissues, and technetium 99-human serum albumin blood-flow studies. The fraction of the injected 131I-mAbG250 dose per gram tumor (%ID/g tumor) localized in G250-positive tumors showed a broad range, but reached levels as high as 0.02% to 0.12%. CONCLUSION 131I-mAbG250 localized specifically to G250 antigen-positive RCC and seems to have considerable potential as an imaging agent in RCC patients. 131I-mAbG250 uptake in the tumors, relative as well as absolute, are among the highest reported for tumor biopsies obtained 8 days after IV mAb administration. Based on the specific localization and high accumulation, mAb G250 may have therapeutic potential.

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