TAPA-1, the target of an antiproliferative antibody, is associated on the cell surface with the Leu-13 antigen.
A murine mAb, 5A6 (IgG1), has been isolated by immunization with a human B lymphoma cell line and screening for growth inhibition. The antibody immunoprecipitated a single chain protein of 26 kDa from cell lysates made with Triton X-100 but additional proteins were precipitated when cell lysates were made with ... the milder detergent CHAPS (3-[3-cholamidopropyl)dimethylammonio)-1-propane sulfate). We have identified one of these coprecipitated molecules as the 16-kDa Leu-13 Ag. 5A6 and anti-Leu-13 showed similar, although not identical, reactivity, growth inhibition and temperature-dependent aggregation effects among hematolymphoid cell lines. The aggregation induced by 5A6 and anti-Leu-13 was not dependent on LFA-1 (lymphocyte function-associated Ag-1). The cell-surface expression of both TAPA-1 (target of an antiproliferative antibody-1) and Leu-13 could be down-modulated by binding to their respective antibodies and they could be reciprocally comodulated. These results suggest that TAPA-1 and Leu-13 form a complex on the cell surface and play a role in growth control through a common pathway.
Mesh Terms:
Antibodies, Monoclonal, Antigens, CD, Antigens, Differentiation, Antigens, Surface, Cell Aggregation, Cell Division, Endocytosis, Humans, Lymphocytes, Macromolecular Substances, Membrane Proteins, Precipitin Tests, Receptor Aggregation, Signal Transduction, Temperature
Antibodies, Monoclonal, Antigens, CD, Antigens, Differentiation, Antigens, Surface, Cell Aggregation, Cell Division, Endocytosis, Humans, Lymphocytes, Macromolecular Substances, Membrane Proteins, Precipitin Tests, Receptor Aggregation, Signal Transduction, Temperature
J. Immunol.
Date: Oct. 01, 1990
PubMed ID: 2398277
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