Abstract
Abstract Microarray and qPCR analyses revealed that pre-transformed murine B cells and a variety of human and murine B cell lymphomas constitutively express high levels of Pftk1, a CDC2-related kinase. Expression of Pftk1 also was induced in normal b cells following activation. These findings suggest that Pftk1 is associated with B cell activation and that dysregulation of expression may be an early event in B cell transformation. While the function of Pftk1 in B cells is unknown, published studies on adipocytes suggest that it may have a regulatory role in glycolysis. Concurrent with the increased expression of Pftk1 in B cell tumors, there is a 2–6 fold increase in the levels of transcripts for genes encoding the glycolytic pathway enzymes, including Hk2, Pgam1, Ldh1, and Pkm2. Currently, we are using a variety of molecular approaches to further investigate the relationship between enhanced Pftk1 expression and increased glycolysis in malignant B cells and to determine whether Pftk1 functions as an oncogene. This work was supported by Arthritis Foundation Chapter Research Grant and NIH grant CA82872-02 awarded to W.F.D.
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