SmPKC1, a new protein kinase C identified in the platyhelminth parasite Schistosoma mansoni

dc.contributor.authorBahia, Diana
dc.contributor.authorAvelar, Livia
dc.contributor.authorMortara, Renato A.
dc.contributor.authorKhayath, Naji
dc.contributor.authorYan, Yutao
dc.contributor.authorNoel, Christophe
dc.contributor.authorCapron, Monique
dc.contributor.authorDissous, Colette
dc.contributor.authorPierce, Raymond J.
dc.contributor.authorOliveira, Guilherme
dc.contributor.institutionInst Pasteur
dc.contributor.institutionFiocruz MS
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionNewcastle Univ
dc.contributor.institutionSanta Casa Misericordia Belo Horizonte
dc.description.abstractSchistosoma mansoni signal transduction pathways are promising sources of target molecules for the development of novel control strategies against this platyhelminth parasite of humans. Members of the protein kinase C (PKC) family play key roles in such pathways activated by both receptor tyrosine kinases and other receptors, controlling a variety of physiological processes. Here, we report the cloning and molecular characterization of the first PKC identified in S. mansoni. Structural analysis indicated that SmPKC1 exhibits all the features typical of the conventional PKC subfamily. the gene structure was determined in silico and found to comprise a total of 15 exons and 14 introns. This structure is highly conserved; all intron positions are also present in the human PKC beta gene and most of the exon sizes are identical. Using PCR on genomic DNA we were able to show that putative orthologues of SmPKC1 are present in 9 Schistosoma species. SmPKC1 expression is developmentally regulated with the highest level of transcripts in miracidia, whereas SmPKC1 protein expression is higher in the sporocyst. the localization of SmPKC1 on the sporocyst ridge cyton and in schistosomula acetabular glands suggests that the enzyme plays a role in signal transduction pathways associated with larval transformation. (c) 2006 Elsevier Inc. All rights reserved.en
dc.description.affiliationInst Pasteur, INSERM, U547, F-59019 Lille, France
dc.description.affiliationFiocruz MS, Ctr Pesquisas Rene Rachou, BR-30190002 Belo Horizonte, MG, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, BR-04023900 São Paulo, Brazil
dc.description.affiliationNewcastle Univ, Sch Biol, Inst Res Environm & Sustainabil, Newcastle Upon Tyne NE1 7RU, Tyne & Wear, England
dc.description.affiliationSanta Casa Misericordia Belo Horizonte, Programa Pos Grad & Pesquisa, BR-30150221 Belo Horizonte, MG, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, BR-04023900 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 345, n. 3, p. 1138-1148, 2006.
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsAcesso restrito
dc.subjectprotein kinase Cen
dc.subjectSchistosoma mansonien
dc.subjectsignal transductionen
dc.titleSmPKC1, a new protein kinase C identified in the platyhelminth parasite Schistosoma mansonien