Control of T lymphocyte morphology by the GTPase Rho

BMC Cell Biol. 2003 Feb 24:4:2. doi: 10.1186/1471-2121-4-2. Epub 2003 Feb 24.

Abstract

Background: Rho family GTPase regulation of the actin cytoskeleton governs a variety of cell responses. In this report, we have analyzed the role of the GTPase Rho in maintenance of the T lymphocyte actin cytoskeleton.

Results: Inactivation of the GTPase Rho in the human T lymphocytic cell line HPB-ALL does not inhibit constitutively high adhesion to the integrin beta1 substrate fibronectin. It did however result in the aberrant extension of finger-like dendritic processes on the substrates VCAM-1, Fn, and mAb specific to beta1 integrins. Time-lapse video microscopy demonstrated that C3 induced extensions were primarily the result of an altered pseudopod elongation rather than retraction. Once the stellate pseudopodia extended, none retracted, and cells became completely immobile. Filipodial structures were absent and the dendritic-like processes in C3 treated cells were rich in filamentous actin. Immunolocalization of RhoA in untreated HPB-ALL cells spreading on fibronectin demonstrated a diffuse staining pattern within the pseudopodia. In C3 treated cells, clusters of RhoA were pronounced and localized within the altered extensions.

Conclusions: GTPase Rho is actively involved in the regulation of T lymphocyte morphology and motility.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • ADP Ribose Transferases / metabolism
  • ADP Ribose Transferases / pharmacology
  • Actins / metabolism
  • Adenosine Diphosphate Ribose / metabolism
  • Botulinum Toxins / metabolism
  • Botulinum Toxins / pharmacology
  • Cell Adhesion / drug effects
  • Cell Division / drug effects
  • Cell Size / drug effects
  • Cell Surface Extensions / drug effects
  • Cell Surface Extensions / metabolism
  • Fibronectins / pharmacology
  • Humans
  • Microscopy, Video / methods
  • T-Lymphocytes / drug effects
  • T-Lymphocytes / enzymology*
  • T-Lymphocytes / metabolism
  • Tumor Cells, Cultured
  • rho GTP-Binding Proteins / metabolism*
  • rhoA GTP-Binding Protein / metabolism

Substances

  • Actins
  • Fibronectins
  • Adenosine Diphosphate Ribose
  • ADP Ribose Transferases
  • exoenzyme C3, Clostridium botulinum
  • Botulinum Toxins
  • rho GTP-Binding Proteins
  • rhoA GTP-Binding Protein