Protein kinase C down-regulation, and not transient activation, correlates with melanocyte growth

Cancer Res. 1991 Jun 15;51(12):3281-8.

Abstract

The nontumorigenic, immortal line of murine melanocytes, Mel-ab, requires the continual presence of biologically active phorbol esters for growth (R.E. Wilson et al., Cancer Res., 49:711-716, 1989). Comparable treatments of B16 murine melanoma cells result in partial inhibition of cell proliferation. The role of protein kinase C (PKC) in the modulation of growth of cells from these two melanocytic cell lines has been investigated. Significant levels of PKC were present in quiescent Mel-ab cells as determined by Western blotting, whereas no immunoreactive protein was detected in cell extracts from either proliferating Mel-ab or B16.F1 cells. Phosphorylation of a Mr 80,000 protein, which by one- and two-dimensional gel analysis comigrated with the known Mr 80,000 protein substrate of PKC in fibroblasts, was induced in 12-O-tetradecanoylphorbol-13-acetate-stimulated quiescent Mel-ab cells but not in proliferating Mel-ab cells or B16.F1 melanoma cells. Direct measurement of PKC activity in these cells demonstrated a 10-fold greater level of activity in quiescent Mel-ab cells (262 +/- 50 pmol/min/mg SD) compared with growing cells (22.8 +/- 11.8 pmol/min/mg SD). An intermediate level of activity was detected in proliferating B16.F1 melanoma cells (148.5 +/- 20.4 pmol/min/mg SD). The subcellular distribution of PKC was dependent upon the growth state of the cells such that quiescent Mel-ab cells displayed a higher level of activity in the cytosol, whereas growing Mel-ab cells displayed greater activity in the particulate fraction. Like many other transformed lines, B16.F1 melanoma cells constitutively expressed the majority of enzyme activity in the particulate fraction. Measurement of [3H]phorbol ester binding in intact cells paralleled the PKC activation data such that quiescent Mel-ab cells displayed binding of 1612 +/- 147 cpm/10(6) cells, whereas proliferating Mel-ab and B16.F1 melanoma cells displayed binding of 652 +/- 28 and 947 +/- 81 cpm/10(6) cells, respectively. Membrane-permeant diacylglycerol analogues, which activated but did not down-regulate PKC, were devoid of growth-stimulating effects on melanocytes, even in the presence of the specific diacylglycerol kinase inhibitor, R59022. Together, these data show that PKC down-regulation, and not activation, correlates with the growth of melanocytes in culture.

MeSH terms

  • Animals
  • Caenorhabditis elegans Proteins*
  • Carrier Proteins
  • Cell Division* / drug effects
  • Cell Line
  • Enzyme Activation
  • Kinetics
  • Melanocytes / cytology*
  • Melanocytes / drug effects
  • Melanocytes / enzymology
  • Melanoma, Experimental / enzymology
  • Melanoma, Experimental / pathology
  • Mice
  • Phorbol 12,13-Dibutyrate / metabolism
  • Phosphoproteins / isolation & purification
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Receptors, Drug / metabolism
  • Tetradecanoylphorbol Acetate / pharmacology

Substances

  • Caenorhabditis elegans Proteins
  • Carrier Proteins
  • Phosphoproteins
  • Receptors, Drug
  • phorbol ester binding protein
  • phorbol ester receptor
  • Phorbol 12,13-Dibutyrate
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate