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Regulation of cadherin-mediated adhesion by the small GTP-binding protein Rho in small cell lung carcinoma cells. Cancer Res 1997 May 01;57(9):1785-93

Date

05/01/1997

Pubmed ID

9135023

Scopus ID

2-s2.0-0030904698 (requires institutional sign-in at Scopus site)   35 Citations

Abstract

Metastasis is one of the most important factors responsible for the pathogenesis of small cell lung carcinoma (SCLC). SCLC cells express cadherins, which are homophilic cell-cell adhesion molecules that play an important role in the regulation of metastasis. We present the first evidence that altering the activity of the small GTP-binding protein Rho induces cadherin-mediated adhesion. ADP-ribosylation of Rho upon incubation or electroporation with recombinant C3 exoenzyme induces rapid aggregation and compaction of SCLC cells. Aggregation and compaction induced by C3 exoenzyme are diminished by removal of extracellular Ca2+ and by the HECD blocking antibody to E-cadherin but not by antibodies to other adhesion molecules. Altering the activity of Rho by ADP-ribosylation does not alter surface expression of E-cadherin, but it alters G actin content, as indicated by the binding of DNase I. Treatment with cytochalasin D also alters G actin content and increases aggregation and compaction of SCLC cells. These findings implicate Rho in the regulation of cadherin-mediated adhesion and identify Rho as a potential therapeutic target for the control of SCLC metastasis.

Author List

Tokman MG, Porter RA, Williams CL

Author

Carol L. Williams PhD Professor in the Pharmacology and Toxicology department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

ADP Ribose Transferases
Actin Cytoskeleton
Actins
Adenosine Diphosphate Ribose
Botulinum Toxins
Cadherins
Carcinoma, Small Cell
Cell Adhesion
Cell Aggregation
Cytochalasin D
Cytoskeleton
GTP-Binding Proteins
Humans
Lung Neoplasms
Time Factors
Tumor Cells, Cultured
rho GTP-Binding Proteins