The possible role of the activity of mycobacterium leprae hsp65 on the experimental autoimmune uveitis [EAU] (2004)
- Authors:
- USP affiliated authors: FERNANDES, BEATRIZ LIEBLICH - ICB ; RIZZO, LUIZ VICENTE - ICB
- Unidade: ICB
- Subjects: IMUNOLOGIA; MICROBIOLOGIA
- Language: Inglês
- Abstract: Heat shock proteins of the hsp60 family are molecular chaperones that guide several steps during synthesis, transport and degradation of proteins. They are abundant in prokaryotic and eukaryotic cells and highly conserved during evolution. Both the microbial and the mammalian hsp60 belong to an important protein family that are major targets for the immune defense against infection. On the other hand, the microbial hsp60 have been implicated in autoimmune diseases, such as chronic inammation and atherosclerosis. The amino acid sequence alignment of M. leprae hsp65 (chaperonin 2) with the E. coli HslVU protease suggested two putative threonine catalytic groups, one in the Ndomain (Thr136-Lys168-Tyr264) and the other in the C-domain (Thr375-Lys409-Ser502); mutagenesis studies showed that the amino acid residues Thr375-Lys409-Ser502 at the C-domain form the catalytic group carries out the main proteolytic activity of the M. leprae hsp65. In the present study, it was compared the amino acid sequences of several hsps belonging to the hsp60 family, mainly the M. leprae hsp65. The possible pathophysiological implication of the proteolytic activity of the M. leprae hsp65 in autoimmune diseases is under investigation throughout the experimental autoimmune uveitis (EAU) induced by immunization of the highly susceptible B10.RIII recombinant isogenic mouse with the Interphotoreceptor Retinoid Binding Protein (IRBP), and both the humoral and cellular immune responses will be determined
- Imprenta:
- Source:
- Título do periódico: Programa e resumos
- Conference titles: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq
-
ABNT
MARENGO, E. B.; PORTARO, F. C. V.; COMMODARO, A. G.; et al. The possible role of the activity of mycobacterium leprae hsp65 on the experimental autoimmune uveitis [EAU]. Anais.. Caxambu: [s.n.], 2004. -
APA
Marengo, E. B., Portaro, F. C. V., Commodaro, A. G., Moraes, L. D. V., Hayashi, M. A., Pimenta, D. C., et al. (2004). The possible role of the activity of mycobacterium leprae hsp65 on the experimental autoimmune uveitis [EAU]. In Programa e resumos. Caxambu. -
NLM
Marengo EB, Portaro FCV, Commodaro AG, Moraes LDV, Hayashi MA, Pimenta DC, Fernandes BL, Rizzo LV, Yamane T, Camargo ACM de, Sant'Anna OA. The possible role of the activity of mycobacterium leprae hsp65 on the experimental autoimmune uveitis [EAU]. Programa e resumos. 2004 ; -
Vancouver
Marengo EB, Portaro FCV, Commodaro AG, Moraes LDV, Hayashi MA, Pimenta DC, Fernandes BL, Rizzo LV, Yamane T, Camargo ACM de, Sant'Anna OA. The possible role of the activity of mycobacterium leprae hsp65 on the experimental autoimmune uveitis [EAU]. Programa e resumos. 2004 ; - The possible role of the hsp65 of Mycobacterium leprae in the experimental acute uveitis (EAU) and systemic lupus erythematosus (SLE) autoimmune diseases
- The role of the proteolytic activity of Mycobacterium leprae hsp65 on Experimental Autoimmune Uveitis (EAU) and Systemic Lupus Erythematosus (SLE)
- Catalytic properties of hsp65 from Mycobacterium leprae: possible involvement in autoimmune disease
- Distinguishing cytosolic oligopeptidases through kinetic parameters using quenched fluorescence substrates
- Regulacao da expressao do gene da alfa-amilase de bacillus subtilis pelo promotor 010 do bacteriofago t7
- Análise da instabilidade genética em Proteus mirabilis: o exemplo da protease extracelular
- ZapA, a possible virulence factor from Proteus mirabilis exhibits broas protease substrate specificity
- Expressao de genes que codificam produtos toxicos em e. Coli
- Expressao de proteinas utilizando o sistema p1
- Possível envolvimento da atividade proteolítica da hsp65 de M. Leprae na auto-imunidade e processos inflamatórios
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas