Monoclonal Antibody H3/5-47 Recognizes an Inducible Cell Surface Antigen Expressed Differently in Endothelium of Normal and Diseased Tissues and in vitro

Pathobiology ◽  
1992 ◽  
Vol 60 (3) ◽  
pp. 122-126
Author(s):  
Hans-Hermann Hagemeier ◽  
Sergij Goerdt ◽  
Clemens Sorg
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Surface Antigen ◽  
Cell Surface Antigen

scholarly journals A monoclonal antibody (8H3) that binds to rat T lineage cells and augments in vitro proliferative responses.

1990 ◽  
Vol 172 (5) ◽  
pp. 1315-1323 ◽  
Author(s):  
Y Torimoto ◽  
M Kinebuchi ◽  
A Matsuura ◽  
K Kikuchi ◽  
T Uede
Keyword(s):  
Monoclonal Antibody ◽  
T Cells ◽  
Cell Surface ◽  
Surface Antigen ◽  
Interleukin 2 ◽  
Cell Surface Antigen ◽  
Double Negative ◽  
Mouse Immunoglobulin ◽  
A Cell

A murine monoclonal antibody, designated 8H3, recognizes a cell surface antigen expressed exclusively on rat T lineage cells. 8H3 antibody immunoprecipitated 180-, 120-, and 90-kD components from rat thymocytes as well as splenic T cells under nonreducing conditions. 8H3 antibody specifically inhibited the binding of thymocytes to fibronectin. Furthermore, binding of rat thymocytes to immobilized synthetic peptide Gly-Arg-Gly-Asp-Ser-Pro-Cys-BSA was inhibited by 8H3 antibody as was Gly-Arg-Gly-Asp-Ser-Pro-Cys, but not by Gly-Arg-Ala-Asp-Ser-Pro-Lys or Gly-Arg-Gly-Glu-Ser-Pro. Crosslinking of 8H3 antigen on double-negative thymocytes and adult thymocytes, as well as splenic T lymphocytes by 8H3 antibody and F(ab')2 fragments of goat antibodies to mouse immunoglobulin, led to an increase in the concentration of cytoplasmic free Ca2+ due to the release of Ca2+ from intracellular stores as well as the influx of Ca2+ from extracellular sources. Expression of interleukin 2 receptor and subsequently cell proliferation was observed upon incubation of thymocytes and splenic T cells with 8H3 antibody. Furthermore, 8H3 antibody induced the proliferation of double-negative thymocytes. These data collectively indicated that a cell surface antigen, 8H3, is involved in not only cell adhesion but also involved in the expression of immature as well as mature thymocytes.

In vivo and in vitro cultured mouse preimplantation embryos differ in their display of a teratocarcinoma cell surface antigen: possible binding of an oviduct factor

Development ◽  
1985 ◽  
Vol 88 (1) ◽  
pp. 55-69
Author(s):  
Stephen J. Gaunt
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Surface Antigen ◽  
Antigenic Site ◽  
Cell Surface Antigen ◽  
Preimplantation Embryos ◽  
Cell Stage ◽  
Teratocarcinoma Cell

By use of a monoclonal antibody, 2B5, in indirect immunofluorescence experiments, it was found that both fertilized and unfertilized mouse eggs obtained directly from the oviduct commenced expression of a cell surface antigen at about 5h after ovulation. Surface labelling became intense by 16 h after ovulation and persisted over all blastomeres throughout preimplantation development. In contrast, embryos cultured in vitro did not show appearance of 2B5 antigen until about 48 h after ovulation, at which time they were at the 2- to 4-cell stage. Antigen expression in vitro commonly began on a single blastomere and did not appear consistently over all blastomeres until the 8-cell stage (72h after ovulation). Unfertilized eggs maintained for 72 h in culture did not acquire 2B5 antigen. It is postulated that the absence of 2B5 antigen on 1-cell eggs cultured in vitro may be due either to a failure of normal synthesis by eggs as a result of a deficiency in the culture medium, or alternatively, to absence of a soluble oviduct factor which carries the 2B5 antigen, and which normally becomes bound to the surface of eggs after ovulation. The second of these two possibilities was supported by egg transfer experiments which showed that unfertilized eggs within the oviduct became 2B5 antigenpositive even after their prior fixation in glutaraldehyde. By the 2- to 4-cell stage, however, embryos developed their own capacity for synthesis of 2B5 antigen-positive cell surface molecules. This synthesis was inhibited by tunicamycin, suggesting that the antigenic site involved the sugar component of glycoprotein. The range of tissues within the postimplantation embryo and adult reproductive tracts which labelled with 2B5 antibody was found to be very similar to that known for SSEA-1 monoclonal antibody (Solter & Knowles, 1978; Fox et al. 1981; Fox, Damjanov, Knowles & Solter, 1982), and as further evidence of a relationship between 2B5 and SSEA-1 antigens it was found that 125I SSEA-1 antibody could be blocked in its binding to teratocarcinoma cells by preincubation in 2B5 monoclonal antibody.

A new mouse cell-surface antigen (Ly-m18) defined by a monoclonal antibody

1981 ◽  
Vol 13 (6) ◽  
pp. 547-554 ◽  
Author(s):  
Shoji Kimura ◽  
Nobuhiko Tada ◽  
Yen Liu ◽  
Ulrich H�mmerling
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Surface Antigen ◽  
Mouse Cell ◽  
Cell Surface Antigen

scholarly journals A monoclonal antibody to cell surface antigen of human thymic epithelial cell

1994 ◽  
Vol 9 (1) ◽  
pp. 47 ◽  
Author(s):  
Doo Hyun Chung ◽  
Young Mee Bae ◽  
Hee Young Shin ◽  
Hyo Seop Ahn ◽  
Hyung Geun Song ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Epithelial Cell ◽  
Cell Surface ◽  
Surface Antigen ◽  
Cell Surface Antigen ◽  
Thymic Epithelial Cell

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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