Words similar to adp-ribosylation
Example sentences for: adp-ribosylation
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The involvement of Rho GTPases in regulating integrin dependent events such as leukocyte homotypic aggregation and in chemokine upregulation of integrin-mediated adhesion has recently been identified [ 18 19 ] . ADP-ribosylation of Rho in neutrophils by treatment with C3 not only inhibits cellular locomotion, but augments chemoattractant induced actin polymerization [ 20 21 ] . Moreover, inactivation of Rho in monocytic cells leads to accelerated formation of filopodia, and it has been proposed that Rho is a negative regulator of actin polymerization within this cell type [ 22 ] . Active Rho is also required for normal morphology, motility, and cytolytic activity of IL-2 activated NK cells [ 23 24 ] . We and others have demonstrated the importance of Rho in T lymphocyte activation [ 25 26 ] . Given the role played by Rho in the regulation of actin microfilaments in other cell types, and the indispensability of a functional actin cytoskeleton in lymphocyte motility and activation, it is of importance to study Rho's role in the regulation of T lymphocyte integrin function and maintenance of cytoskeletal organization.
The phenotype induced by ADP-ribosylation of Rho in T lymphocytes appeared different than that induced in fibroblast models, where microinjection of C3 results in fibroblast retraction of pseudopodia, with the cell body rounding up eventually to become non-adherent [ 17 ] . Video time-lapse microscopy demonstrated the elongation of aberrant pseudopods in HPB-ALL cells plated on the β1 substrate VCAM-1, rather than an altered retraction of already formed pseudopods.
ADP-ribosylation of Rho proteins by C3 exoenzyme prevents neurite retraction in the specialized growth cone of developing neurons, and in fact promotes neurite outgrowth in the same fashion as microinjection of purified dominant negative RhoA T19N [ 39 ] . In these instances, neuronal N1E-115 cell outgrowth induced by inactivation of RhoA was mimicked by microinjection of Rac1- or Cdc42-GST fusion proteins, and could be abolished by coinjection of dominant negative Cdc42 T17Nor Rac1 T17N [ 39 ] . From these results, the authors concluded that inactivation of RhoA by C3 exoenzyme treatment resulted in the activation of Rac1 and Cdc42 GTPases, suggesting the mutually exclusive function of RhoA and Rac1/Cdc42.
Electroporation of C3 induces complete ADP-ribosylation of Rho in HPB-ALL
ADP-ribosylation of Rho proteins in chemoattractant stimulated neutrophils [ 20 21 ] and in both monocytic lines and fresh blood monocytes [ 22 38 ] results in actin filament polymerization.
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