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Department of Cell Biology [C. A. O., N. E. W.], Community Oncology Program [V. G. V.], and Department of General Surgery [S. E. S.], The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030
The Ca2+- and phospholipid-dependent protein kinase, protein kinase C (PKC), is a critical enzyme in the regulation of cell growth. In this report, we demonstrate elevated expression of PKC activity in surgical specimens of eight of nine spontaneous human breast tumors, as compared with the expression of PKC activity in normal breast tissue obtained from the same patients. The mean PKC specific activity in histologically normal breast tissue was 166 ± 63 pmol 32P/min/mg, whereas the mean PKC specific activity in the breast tumors was 460 ± 182 pmol 32P/min/mg (P = 0.0003; Student's t test). The low interpatient variability among the PKC levels observed in the histologically normal breast tissue specimens and the significant elevation of PKC levels observed in the tumors indicate that elevated expression of PKC activity in breast tissue is a potential marker for malignant disease in the breast.
1 This research was supported by National Cancer Institute Core Grant CA16672 to the University of Texas M. D. Anderson Cancer Center.
2 To whom requests for reprints should be addressed.
Received 10/11/88. Revised 2/16/89. Accepted 3/21/89.
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