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Published August 1, 1976 | Published
Journal Article Open

Terminal deoxynucleotidyl transferase is found in prothymocytes

Abstract

Terminal deoxynucleotidyl transferase is an enzyme which has the unique property of polymerizing polydeoxynucleotides onto a primer in the absence of a template (1,2). This enzyme is found both in the thymus and the bone marrow of birds, rodents, and humans (3-7). Whether the marrow cells that contain terminal transferase are related to thymocytes, or are on a separate pathway of differentiation, is not yet known (7,8). To determine the lineage of the murine bone marrow cells that have terminal transferase, we have investigated whether these cells have the antigen Thy-1 induced on the cells by treatment with thymopoietin (9). Thymopoietin is known to induce a set of characteristic T-cell markers including the Thy-1 alloantigen on the surface of a subpopulation of bone marrow cells committed to T-cell differentiation (prothymocytes) (10). Destruction of Thy- 1-positive cells after exposure to thymopoietin allows elimination of a substantial fraction of those bone marrow cells that can repopulate an irradiated thymus (11). We find that such an elimination after induction with the thymic polypeptide removes a substantial amount of terminal transferase from the bone marrow cell population, suggesting that at least one-half of the marrow cells bearing this enzyme are related to those found in the thymus.

Additional Information

© 1976 Rockefeller University Press. Received for publication 7 May 1976; Published August 1, 1976. Supported by grants AI-12174 and CA-14051 from NIH and by a contract from the Virus Cancer Program of the National Cancer Institute. We are very grateful for the technical and theoretical advice and antibody supplied by Doctors E. A. Boyse and M. P. Scheid. These experiments would not have been possible without the technical assistance of Joan Hugenberger and Laila Boudreau.

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August 19, 2023
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