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1.
Experimental & Molecular Medicine ; : 483-491, 2012.
Article in English | WPRIM | ID: wpr-192554

ABSTRACT

Phosphatidylinositol 3-kinase (PI3K) is essential for both G protein-coupled receptor (GPCR)- and receptor tyrosine kinase (RTK)-mediated cancer cell migration. Here, we have shown that maximum migration is achieved by full activation of phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 (P-Rex1) in the presence of Gbetagamma and PI3K signaling pathways. Lysophosphatidic acid (LPA)-induced migration was higher than that of epidermal growth factor (EGF)-induced migration; however, LPA-induced activation of Akt was lower than that stimulated by EGF. LPA-induced migration was partially blocked by either Gbetagamma or RTK inhibitor and completely blocked by both inhibitors. LPA-induced migration was synergistically increased in the presence of EGF and vice versa. In correlation with these results, sphingosine-1-phosphate (S1P)-induced migration was also synergistically induced in the presence of insulin-like growth factor-1 (IGF-1). Finally, silencing of P-Rex1 abolished the synergism in migration as well as in Rac activation. Moreover, synergistic activation of MMP-2 and cancer cell invasion was attenuated by silencing of P-Rex1. Given these results, we suggest that P-Rex1 requires both Gbetagamma and PI3K signaling pathways for synergistic activation of Rac, thereby inducing maximum cancer cell migration and invasion.


Subject(s)
Humans , Cell Line, Tumor , Cell Movement/drug effects , Enzyme Activation/drug effects , GTP-Binding Protein beta Subunits/metabolism , GTP-Binding Protein gamma Subunits/metabolism , Guanine Nucleotide Exchange Factors/metabolism , Lysophospholipids/pharmacology , Neoplasms/enzymology , Phosphatidylinositol 3-Kinases/metabolism , Proto-Oncogene Proteins c-akt/metabolism , Receptors, G-Protein-Coupled/metabolism , Signal Transduction
2.
Sci. med ; 21(1)jan.-mar. 2011.
Article in Portuguese | LILACS | ID: lil-593782

ABSTRACT

Objetivos: revisar o assunto proteína G e seus mecanismos de transdução celular, de forma abrangente e didática.Fonte de dados: foram revisados artigos específicos sobre o tema, disponíveis em periódicos eletrônicos e encontrados através das bases de dados LILACS, PubMed e SciELO.Síntese dos dados: a transdução de sinais é uma função fisiológica que intermedeia o estímulo externo e a resposta celular, sendo o passo de conversão intracelular do agonismo de várias substâncias. Os compostos proteicos envolvidos nessa atividade estão presentes em todos os sistemas do organismo; consequentemente, disfunções na sua estrutura culminam em estados patológicos diversos. A descrição da dinâmica da transdução, da estrutura e funções da proteína G e do seu papel em algumas doenças foram abordados nesta revisão.Conclusões: a revisão da literatura mostra que o tema proteína G não tem gerado muitos trabalhos experimentais.Entretanto, o estudo desse composto protéico evidencia sua grande importância na fisiologia, indicando que disfunções na sua estrutura resultam em vários estados patológicos.


Aims: To review, in a comprehensive and didactic way, the issue G protein and its mechanisms of cellular transduction.Source of data: Articles that address the specific issue, available online, and found through the databases LILACS, PubMed and SciELO, were reviewed.Summary of findings: Signal transduction is a physiological function that mediates the external stimulus and cellular response; it is the conversion step of agonism of several intracellular substances. The protein compounds involved in this activity are present in all body systems, thus dysfunction in its structure results in several pathological states.The description of the dynamics of transduction, structure and functions of G protein and its role in some diseases were addressed in this review.Conclusions: The literature review shows that the subject protein G has not generated many experimental studies.However, the study of this protein compound makes evident its great importance in physiology and indicates that dysfunctions in its structure result in various pathological conditions.


Subject(s)
Humans , Chronic Disease , Population Dynamics , Oxidative Stress , Health Transition
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