Polylysine-Containing Peptides, Including the Carboxyl-Terminal Segment of the Human c-Ki-ras 2 Protein, Affect the Activity of Some Key Membrane Enzymes

• Published in: Proceedings of the National Academy of Sciences - PNAS 1987-01, Vol.84 (2), p.324-328
• Main Authors: Gatica, Marta, Allende, Catherine C., Antonelli, Marcelo, Allende, Jorge E.
• Format: Article
• Language: English
• Subjects: 1-Phosphatidylinositol 4-Kinase; adenylate cyclase; Adenylyl Cyclases - metabolism; Animals; Cell Membrane - enzymology; Cell membranes; Enzymes; Female; Gels; Histones; Humans; Kinetics; Membrane Lipids - biosynthesis; Membrane proteins; Membrane Proteins - metabolism; Molecular Weight; Oocytes; Oocytes - drug effects; Oocytes - enzymology; P branes; peptides; Peptides - pharmacology; phosphatidylinositol kinase; Phosphatidylinositols; Phospholipids - biosynthesis; Phosphoproteins - isolation & purification; Phosphorylation; Phosphotransferases - metabolism; Polylysine - pharmacology; protein kinase; Protein Kinases - metabolism; Proteins; Proto-Oncogene Proteins - pharmacology; Proto-Oncogene Proteins p21(ras); Xenopus; Xenopus laevis
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.84.2.324

Polylysine-containing peptides are found to affect membrane protein kinases, phosphatidylinositol kinases, and adenylate cyclase. Poly(L-lysine), poly(D-lysine), random copolymers of lysine and serine or lysine and alanine, and poly(L-ornithine) produced large increases in the in vitro phosphorylation of some membrane proteins present in Xenopus laevis oocyte membranes. Poly(L-arginine) did not cause a similar stimulation. In these membranes the phosphorylation of polydisperse protein of approximately 25 kDa was also greatly increased by 1 mM spermine and spermidine, by 10 μ M histone H1, or by 200 μ M peptide containing the 14-residue sequence at the carboxyl terminus of the human c-Ki-ras 2 gene product, which has eight lysines. Similar specific stimulation of protein phosphorylation was observed with membranes of NG-108-15 nerve cells in culture. Polylysine peptides, including the c-Ki-ras 2 segment, also stimulate the in vitro phosphorylation of membrane inositolphospholipids, to produce mainly phosphatidylinositol 4-phosphate and less phosphatidylinositol 4,5-bisphosphate. Polylysine also alters the activity of oocyte adenylate cyclase, assayed in the presence of either F- or 5′-guanylyl imidodiphosphate.