A Novel Approach for the characterization of Proteoglycans and Biosynthetic Enzymes in a snail model

• Processo: 11/18280-4
• Modalidade de apoio: Auxílio à Pesquisa - Publicações científicas - Artigo
• Data de Início da vigência: 01 de outubro de 2011
• Data de Término da vigência: 31 de março de 2012
• Área do conhecimento: Ciências Biológicas - Bioquímica - Biologia Molecular
• Pesquisador responsável: Helena Bonciani Nader
• Beneficiário: Helena Bonciani Nader
• Instituição Sede: Instituto Nacional de Farmacologia (INFAR). Universidade Federal de São Paulo (UNIFESP). Campus São Paulo. São Paulo , SP, Brasil
• Assunto(s): Achatina fulica Heparitina sulfato Espectrometria de massas Glicosaminoglicanos Biossíntese
• Palavra(s)-Chave do Pesquisador: acharan sulfato | Achatina fulica | Biossintese | Espectrometria de massas | glicosaminoglicanos | Heparan sulfato | Espectrometria de massas

Resumo

Proteoglycans encompass a heterogeneous group of glycoconjugates where proteins are substituted with linear, highly negatively charged glycosaminoglycan chains. Sulfated glycosaminoglycans are ubiquitous to the animal kingdom of the Eukarya domain. Information on the distribution and characterization of proteoglycans in invertebrate tissues is limited and restricted to a few species. With the use of multidimensional protein identification technology and immunohistochemistry, this study shows for the first time the presence and tissue localization of different proteoglycans, such as perlecan, aggrecan, and heparan sulfate proteoglycan, among others, in organs of the gastropoda Achatina fulica. Through a proteomic analysis of Golgi proteins and immunohistochemistry of tissue sections, we detected the machinery involved in glycosaminoglycan biosynthesis, related to polymer formation (polymerases), as well as secondary modifications (sulfation and epimerization). Therefore, this work not only identifies both the proteoglycan core proteins and glycosaminoglycan biosynthetic enzymes in invertebrates but also provides a novel method for the study of glycosaminoglycan and proteoglycan evolution. (AU)