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During studies on the influence of Fv-2 on the cycle state of the erythroid burst-forming unit (BFU-E), an activity was found in bone marrow supernatants from C57BL/6 (B6) mice that shut down DNA synthesis of the BFU-E in vitro. It acted within minutes, its action was completely reversed by a single wash, and it appeared specific to the BFU-E. The activity-causing substance, being macromolecular, heat stable, and trypsin-sensitive, was evidently a protein and was named negative regulatory protein. We purified a negative regulatory protein from a bone marrow-derived "B6 Pan" cell line with properties thus far indistinguishable from those of the negative regulatory protein obtained directly from B6 marrow. By gel filtration the protein has a Mr of approximately equal to 79,000, by cation- and anion-exchange chromatography it appears to be a neutral molecule at physiological pH, and the molecule does not bind to Con A. After five sequential chromatographic steps, we obtained a preparation active at a concentration of 25 ng/ml. Our findings are compatible with the hypothesis that quiescence of BFU-E with respect to DNA synthesis in vivo in B6 mice is mediated by negative regulatory protein molecules.

proceedings of the national academy of sciences of the united states of america

Negative regulation of DNA synthesis in early erythropoietic progenitor cells (BFU-E) by a protein purified from the medium of C57BL/6 mouse marrow cells.