Resultado do

Prêmio José Ribeiro do Valle 2006
 
Primeiro lugar
 Segundo lugar
 Outros trabalhos apresentados
Comissão Julgadora

 

O prêmio José Ribeiro do Valle, oferecido a cada ano pela SBFTE, visa identificar a cada ano os melhores trabalhos científicos desenvolvidos por jovens investigadores na área da Farmacologia. Entre os trabalhos inscritos para esta nona edição do prêmio, foram selecionados cinco finalistas, que fizeram apresentações de seus respectivos trabalhos perante comissão julgadora, em sessão pública durante o 38o Congresso Brasileiro de Farmacologia e Terapêutica Experimental, em Ribeirão Preto, SP. Os cinco finalistas escolhidos para a edição de 2006 foram:
Primeiro lugar
FBXO25, AN F-BOX PROTEIN HOMOLOGUE OF ATROGIN-1, IS NOT INDUCED IN ATROPHYING MUSCLE
 Maragno, A. L. G. C.1; Baqui, M. M. A.2; Yokoo, S.1; Manfiolli, A. O.1; Sakagute, L. H.1; Gomes, M. D.1 - 1FMRP - USP - Bioquímica e Imunologia; 2FMRP - USP - Biologia Celular e Molecular
 Atrogin-1/MAFbx/FBXO32 is a muscle-specific ubiquitin-ligase (E3) that is dramatically increased in atrophying muscle. Here we have investigated the functional relationship between atrogin-1 and FBXO25 which shares 65% amino acid identity. Using a RT-PCR we demonstrated that FBXO25 is highly expressed in brain, kidney, and intestine, whereas atrogin-1 expression is largely restricted to striate muscle. FBXO25 was shown here to contain a functional F-box domain that binds to Skp1 and thereby to Roc1 and Cul1, the major components of SCF-type E3s. In addition, the productive SCF complex containing FBXO25 showed ubiquitin ligase activity. Immunofluorescence studies in transfected B16-F10 cells showed that FBXO25 colocalize in the nucleus with Skp1, thus, indicating that putative substrates of FBXO25 may be nuclear proteins. We investigated the differential expression of atrogin-1 and FBXO25 in fasted and dexamethasone-treated mice and also in rats with streptozotocin-induced diabetes. Although the atrogin-1 was strongly induced in muscle in all three models, no changes were observed in the expression of FBXO25. Therefore, here we have shown that FBXO25 is a novel F-box protein analogous to atrogin-1, which is not involved in muscle atrophy. These data contribute to elucidate the role of FBXO25 in the ubiquitin-proteasome pathway. Supported by: FAPESP and FAEPA.
Segundo lugar
AMYLOID-b (A b) PEPTIDE ACTIVATES NF-kB THROUGH NMDA-p21ras PATHWAY IN CEREBELLAR PRIMARY CELL CULTURE. Kawamoto, E. M.1; Lepsch, B. L.1; Cury-Boaventura, M. F.2; Sa Lima, L.1; Munhoz, C. D.1; Avellar, M. C. W.3; Mattson, M. P.4; Scavone, C.1 - 1USP - Pharmacology; 2USP - Physiology; 3UNIFESP - EPM - Pharmacology; 4NIA - Neurosciences
 Introduction: It has been shown Ab cause synaptic dysfunction and render neurons vulnerable to excitotoxicity. NF-kB is a transcription factor, linked to survival and apoptosis, modulated by  Ab in neurons and glia. Our aim was evaluate some of the mechanisms by which this occurs. Methods: Cerebellar cell culture was treated with different concentrations of Ab (500nM, 1mM, 2mM) in different time points (6, 12, 24 h). Cells were incubated with MK-801 (NMDA antagonist), Manumycin A (rasfarnesyltransferase inhibitor), PD98059 (MAPK inhibitor), LY294002 (PI3 kinase inhibitor) 20 min before Ab. Nuclear extracts were isolated and EMSA used to measure changes in NF-kB activity in competition studies with specific and non-specific unlabeled double-strand oligonucleotide and super-shift assays with specific antibodies against NF-kB subunits. FACS assay to measure cell viability and Western blot to p65 were performed. Results: Ab induces a time dose-dependent activation of NF-kB (peak of activation 12h/1mM), and both p50/p65 and p50/p50 dimers were involved. This activation was reverted by MK-801, Manumycin A and partially reduced by PD98059 and LY294002. FACS assay showed that none of these treatments caused cell death. Discussion: These results suggest that Ab activates NF-kB by NMDA-p21ras through MAPK and PI3-kinase pathways in cerebellar cell culture. Supported by: FAPESP, CNPq, Bunka grant/Sumitomo Bank
Outros trabalhos apresentados
ANGIOTENSIN II INDUCES KININ B1 RECEPTORS. Ceravolo, G. S.1; Nigro, D.1; Tostes, R. C. A.1; Fortes, Z. B.1; Carvalho, M. H. C.1 - 1USP - Farmacologia
ALPHA-1-ACID GLYCOPROTEIN FROM SERUM OF SEPTIC PATIENTS INHIBITS NEUTROPHIL MIGRATION. Spiller, F.1; Mestriner, F. L. A. C.2; Laure, H. J.3; Tavares-Murta, B. M.4; Rosa, J. C.5; Basile-Filho, A.6; Ferreira, S. H.1; Greene, L. J.3; Cunha, F. de Q.1 - 1FMRP - USP - Farmacologia; 2FMRP - USP - Clínica Médica; 3Centro de Química de Proteínas e Centro Regional de Hemoterapia - Biologia Celular, Molecular e Bioagentes Patogênicos; 4UFTM - Ciências Biológicas; 5FMRP - USP - Biologia Celular, Molecular e Bioagentes Patogênicos; 6FMRP - USP - Cirurgia e Anatomia
RELEVANCE OF CELL MIGRATION FOR NOCICEPTIVE AND INFLAMMATORY RESPONSES INDUCED BY PAF. Marotta, D. M.1; Fernandes, E. S.1; Quintao, N. L. M.1; Costa, R.1; Leal, P. C.2; Campos, M. M.3; Calixto, J. B.1 - 1UFSC - Farmacologia; 2UFSC - QMC/CFM; 3PUC - RS - Faculdade de Odontologia
Comissão Julgadora

  • Profa. Dra. Maria Cristina de O. Salgado, FAculdade de Medicina de Ribeirão Preto (FMRP-USP) (Presidente)

  • Prof. Dr. Emer S. Ferro, Instituto de Ciências Biomédicas (ICB-USP)

  • Profa. Dra. Patricia T. Bozza, Fundação Oswaldo Cruz (FIOCRUZ)