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Identification of myristoylated alanine-rich C kinase substrate (MARCKS) in astrocytes
Journal article   Open access

Identification of myristoylated alanine-rich C kinase substrate (MARCKS) in astrocytes

Ljubisa Vitkovic, Vincent J Aloyo, Shigeru Maeda, Deborha L Benzil, Joseph P Bressler and Dana C Hilt
Frontiers in bioscience, v 10(1), pp 160-165
01 Jan 2005
DOI: https://doi.org/10.2741/1517
PMID: 15574358
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.2741/1517View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze),  Open

Abstract

Animals Astrocytes - cytology Astrocytes - metabolism Autoradiography Cell Membrane - metabolism Cell Proliferation Cells, Cultured Cytokines - metabolism Electrophoresis, Gel, Two-Dimensional GAP-43 Protein - chemistry Intracellular Signaling Peptides and Proteins - metabolism Intracellular Signaling Peptides and Proteins - physiology Membrane Proteins - metabolism Membrane Proteins - physiology Myristoylated Alanine-Rich C Kinase Substrate Neuroglia - metabolism Protein Kinase C - metabolism Rats Tetradecanoylphorbol Acetate - pharmacology
We have characterized membrane-associated substrates of Ca2+-dependent kinases in primary rat astrocytes by in vitro phosphorylation, 2-dimensional gel electrophoresis and autoradiography. The most prominent among these were three acidic, protein kinase C (PKC) substrates. These are important because they likely transduce cytokine and other neuro-immune modulatory signals mediated by PKC. We now show that one of these phosphoproteins is myristoylated alanine-rich PKC kinase substrate (MARCKS) or phosphomyristin C. The identity was corroborated by one- and 2- dimensional immunoblotting with an MARCKS-specific polyclonal antibody. Exposing primary astrocytes to phorbol 12-myristate 13-acetate stimulated phosphorylation of this protein. The level of MARCKS appeared inversely proportional to the proliferative potential of astrocytes because it was lower in spontaneously transformed as compared to passaged or confluent cells. These data are consistent with previous reports and indicate that one of three major acidic membrane-associated PKC substrates in astrocytes is MARCKS. Thus, MARCKS is likely near-proximal transducer of PKC-mediated signals in astrocytes.

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Industry collaboration
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Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
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