Regulation of astrocyte morphology by RhoA and lysophosphatidic acid

Exp Cell Res. 1998 Dec 15;245(2):252-62. doi: 10.1006/excr.1998.4224.

Abstract

Astrocytes in the CNS undergo morphological changes and start to proliferate after breakdown of the blood-brain barrier. In culture, proliferating astrocytes have a flat, polygonal shape. When treated with cAMP-raising agents, astrocytes adopt a stellate, process-bearing morphology resembling their in vivo appearance. Stellation is accompanied by loss of actin stress fibers and focal adhesions. Lysophosphatidic acid (LPA), a blood-borne mitogen that signals through its cognate G protein-coupled receptor, stimulates DNA synthesis in astrocytes and causes rapid reversal of cAMP-induced stellation. LPA reversal of stellation is initiated by f-actin reassembly and tyrosine phosphorylation of focal adhesion proteins such as paxillin. Botulinum C3 toxin, which inactivates the Rho GTPase, mimics cAMP-raising agents in inducing stellation, f-actin disassembly, paxillin dephosphorylation, and growth arrest. However, unlike cAMP-induced stellation, C3-induced stellation cannot be reversed by LPA. Conversely, astrocytes expressing activated RhoA fail to undergo cAMP-induced stellation. Thus, RhoA controls astrocyte morphology in that active RhoA directs LPA reversal of stellation, while inactivation of RhoA is sufficient to induce stellation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP Ribose Transferases / pharmacology
  • Actins / metabolism
  • Animals
  • Astrocytes / cytology*
  • Astrocytes / drug effects
  • Botulinum Toxins*
  • Cell Adhesion / drug effects
  • Cell Size / drug effects
  • Cells, Cultured
  • Colforsin / pharmacology
  • Cyclic AMP / agonists
  • Cyclic AMP / physiology
  • Cytochalasin B / pharmacology
  • Cytoskeletal Proteins / metabolism
  • Cytoskeleton / drug effects
  • Cytoskeleton / ultrastructure
  • DNA / biosynthesis
  • GTP-Binding Proteins / antagonists & inhibitors
  • GTP-Binding Proteins / genetics
  • GTP-Binding Proteins / metabolism*
  • Lysophospholipids / antagonists & inhibitors
  • Lysophospholipids / pharmacology*
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Paxillin
  • Phosphoproteins / metabolism
  • Phosphotyrosine / metabolism
  • Prosencephalon
  • Rats
  • Virulence Factors, Bordetella / pharmacology
  • rhoA GTP-Binding Protein

Substances

  • Actins
  • Cytoskeletal Proteins
  • Lysophospholipids
  • Paxillin
  • Phosphoproteins
  • Pxn protein, rat
  • Virulence Factors, Bordetella
  • Colforsin
  • Phosphotyrosine
  • Cytochalasin B
  • DNA
  • Cyclic AMP
  • ADP Ribose Transferases
  • exoenzyme C3, Clostridium botulinum
  • Mitogen-Activated Protein Kinase 1
  • Botulinum Toxins
  • GTP-Binding Proteins
  • rhoA GTP-Binding Protein