Affordable Access

Phosphatidic acid activation of protein kinase C in LA-N-1 neuroblastoma cells

Authors
Journal
Neuroscience Letters
0304-3940
Publisher
Elsevier
Publication Date
Volume
201
Issue
3
Identifiers
DOI: 10.1016/0304-3940(95)12178-1
Keywords
  • Phosphatidic Acid
  • Phorbol Ester
  • Neuroblastoma Cells
  • Protein Kinase C
  • Phospholipases
Disciplines
  • Biology

Abstract

Abstract Phosphatidic acid (PA), a hydrolytic product of phospholipase D activity, stimulated cytosolic protein kinase C (PKC) activity when LA-N-1 neuroblastoma cells in culture were treated with PA, without translocating the enzyme to the membrane. Treatment of cells with 12- O-tetradecanoylphorbol-13-acetate (TPA) translocated and activated PKC in a dogmatic manner. Partially purified PKC activity derived from LA-N-1 neuroblastoma cells was stimulated by PA alone or in the presence of phosphatidylserine or TPA, without affecting [ 3H]phorbol dibutyrate binding, indicating that the site of action of PA was different from the phorbol ester or diacylglycerol binding site. These results suggest an unorthodox pattern of PKC stimulation mediated by PA which appears to be yet another mode of PA signal transduction.

There are no comments yet on this publication. Be the first to share your thoughts.