Phosphorylation of the MARCKS family of protein kinase C substrates in human B chronic lymphocytic leukemia cells

Leukemia. 1995 May;9(5):834-9.

Abstract

Incubation of B chronic lymphocytic leukemia (B-CLL) cells with phorbol esters resulted in the phosphorylation of three Triton-soluble, heat-stable, acidic proteins with apparent M(r) of 80 KDa, 60 KDa and 43 KDa. The characteristics of the three proteins suggested that they could be related to the myristoylated, alanine-rich, C-kinase substrate (MARCKS). p80 was immunoprecipitated with an antibody against the N-terminal peptide of MARCKS. p43 co-migrated with mouse MRP/Mac-MARCKS (MARCKS-related protein). p60 is the most prominent substrate of protein kinase C in B-CLL cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • B-Lymphocytes / enzymology*
  • B-Lymphocytes / metabolism
  • Humans
  • Intracellular Signaling Peptides and Proteins*
  • Leukemia, Lymphocytic, Chronic, B-Cell / enzymology*
  • Leukemia, Lymphocytic, Chronic, B-Cell / metabolism
  • Membrane Proteins*
  • Molecular Sequence Data
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Neoplasm Proteins / metabolism*
  • Phosphorylation
  • Precipitin Tests
  • Protein Kinase C / metabolism*
  • Proteins / metabolism*
  • RNA, Messenger / metabolism
  • Substrate Specificity
  • Tetradecanoylphorbol Acetate / pharmacology
  • Tumor Cells, Cultured

Substances

  • Intracellular Signaling Peptides and Proteins
  • MARCKS protein, human
  • Marcks protein, mouse
  • Membrane Proteins
  • Neoplasm Proteins
  • Proteins
  • RNA, Messenger
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate