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Abundant Synthesis of the Transformation-induced Protein of Neoplastic Human Fibroblasts, Plastin, in Normal Lymphocytes¹

Armand Hammer Cancer Research Center, Linus Pauling Institute of Science and Medicine, Palo Alto, California 94306 [D. G., G. L., S. B., J. L.], and Department of Medical Microbiology, University of South Florida School of Medicine, Tampa, Florida 33612 [J. D.]

The transformation-induced protein plastin (p219; M_r 68,000, pl 5.3) is a reliable cytosolic marker for neoplastic human fibroblasts. Fibroblasts transformed in vitro by chemical carcinogens or SV40 virus and tumor-derived cancer cells of fibroblastoid or epithelioid origin usually express plastin and p220, a minor phosphorylated form of plastin. We report here that plastin is expressed as one of the most abundant proteins of normal, untransformed lymphocytes. The phosphorylated form of plastin was detectable in adherent monocytes but not in purified T- or NK lymphocytes. We also demonstrate that an allelic variant or mutated form of plastin exhibiting altered charge is found at a reduced frequency in the human population. We discuss the possible significance of these observations in terms of evaluating the role of plastin induction in expression of the cancerous phenotype of fibroblasts.

¹ This work was supported in part by a grant from the National Cancer Institute (Grant CA-34763) and funding from the Japan Shipbuilding Foundation to J. L.

² To whom requests for reprints should be addressed. Supported by funds donated to the Linus Pauling Institute by Robert Sabin.

Received 5/22/85. Revised 8/ 1/85. Accepted 8/ 6/85.

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