Experimental in vitro organogenesis and its modification by antibody directed to a cell surface antigen

1975 ◽  
Vol 43 (1) ◽  
pp. 101-108 ◽  
Author(s):  
Aron E. Szulman
Keyword(s):  
Cell Surface ◽  
Surface Antigen ◽  
Cell Surface Antigen ◽  
In Vitro Organogenesis ◽  
A Cell

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.

A cell surface antigen expressed by astrocytes and their precursors

Glia ◽  
1993 ◽  
Vol 8 (1) ◽  
pp. 20-32 ◽  
Author(s):  
Vilma Szigeti ◽  
Robert H. Miller
Keyword(s):  
Cell Surface ◽  
Surface Antigen ◽  
Cell Surface Antigen ◽  
A 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.

scholarly journals G(AKSL2): a new cell surface antigen of the mouse related to the dualtropic mink cell focus-inducing class of murine leukemia virus detected by naturally occurring antibody.

1979 ◽  
Vol 149 (1) ◽  
pp. 200-215 ◽  
Author(s):  
E Stockert ◽  
A B DeLeo ◽  
P V O'Donnell ◽  
Y Obata ◽  
L J Old
Keyword(s):  
Cell Surface ◽  
Surface Antigen ◽  
Leukemia Virus ◽  
Natural Antibody ◽  
Cell Surface Antigen ◽  
Cytotoxic Action ◽  
Naturally Occurring ◽  
Infected Cells ◽  
Akr Mice

Normal mouse sera were tested for cytotoxic antibody to surface antigens of cultured monolayer cells infected with AKR-derived ecotropic MuLV, xentropic MuLV, or dualtropic MCF 247 MuLV. Antibody to ecotropic MuLV-infected cells was found in a proportion of C57BL/6, C3Hf/Bi, AKR-Fv-1b, and (C3Hf/Bi X AKR)F1 mice, but not AKR or (AKR X C3Hf/Bi)F1 mice. Antibody to xenotropic MuLV-infected cells was virtually restricted to C57BL/6 mice. Antibody to MCF 247-infected cells was found in all strains tested, including AKR mice. Absorption analysis of (C3Hf/Bi x akr)f1 and AKR-Fv-1b sera with selective reactivity for MCF 247-infected cells showed that these sera recognize distinctive antigens on MCF 247-infected cells that are not present on ecotropic or xenotropic MuLV-infected cells. The transplantable AKR spontaneous leukemia AKSL2 was found to be uniquely sensitive to the cytotoxic action of naturally occurring antibody to MCF 247-related antigens and absorption tests with AKSL2 as the target cell and sera from a single AKR-Fv-1b mouse have permitted the definition of a new MuLV-related cell surface antigen, which has been designated G(AKSL2). Thymocytes from young mice of high leukemia-incidence strains (AKR, C58, and PL) express G(AKSL2), whereas thymocytes from 12 other strains do not. In AKR mice, the antigen is expressed in higher amounts on cells from thymus and bone marrow than on spleen cells. All AKR spontaneous leukemias tested express G(AKSL2), as did three MuLV-induced leukemias arising in G(AKSL2)- strains. Five X-ray-induced leukemias of G(AKSL2)- strains were G(AKSL2)-, as were MuLV+ and MuLV- chemically induced sarcomas. In the limited survey conducted to date, natural antibody to G(AKSL2) has been restricted to strains expressing G(AKSL2) in their normal tissues: AKR, AKR congenic mice AKR-Fv-1b and AKR hybrid mice (C3Hf/Bi x akr)f1 and (C57BL/6 X AKR)F1. In vitro G(AKSL2) induction tests involving MuLV infection of cultured monolayer cells showed that 8 of 12 newly isolated dualtropic MuLV shared the property of G(AKSL2) induction with the prototype MCF MuLV, MCF 247. Of the 12 ecotropic MuLV tested, only the N-tropic MuLV isolated from a leukemia originally induced by Passage A Gross virus induced G(AKSL2). The xenotropic and amphotropic MuLV isolates tested lacked G(AKSL2) inducing activity. Recognition of the g(aksl2) system provides a way to trace the origin and natural history of a class of dualtropic MCF MuLV in the mouse and to determine whether natural antibody to G(AKSL2) plays a role in AKR leukemogenesis.

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