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Title: A novel approach for the characterisation of proteoglycans and biosynthetic enzymes in a snail model
Authors: Gesteira, Tarsis Ferreira [UNIFESP]
Coulson-Thomas, Vivien Jane [UNIFESP]
Ogata, Fernando Toshio [UNIFESP]
Farias, Eduardo Henrique Cunha de [UNIFESP]
Cavalheiro, Renan Pelluzzi [UNIFESP]
Lima, Marcelo Andrade [UNIFESP]
Cunha, Gabriel L. A [UNIFESP]
Nakayasu, Ernesto S
Almeida, Igor Correia de
Toma, Leny [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Univ Texas El Paso
Keywords: Achatina fulica
Acharan sulfate
Proteomic analysis
Issue Date: 1-Dec-2011
Publisher: Elsevier B.V.
Citation: Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1814, n. 12, p. 1862-1869, 2011.
Abstract: Proteoglycans encompass a heterogeneous group of glycoconjugates where proteins are substituted with linear, highly negatively charged glycosaminoglycan chains. Sulphated glycosaminoglycans are ubiquitous to the animal kingdom of the Eukarya domain. Information on the distribution and characterisation of proteoglycans in invertebrate tissues is limited and restricted to a few species. By the use of multidimensional protein identification technology and immunohistochemistry, this study shows for the first time the presence and tissue localisation of different proteoglycans, such as perlecan, aggrecan, and heparan sulphate proteoglycan, amongst 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 (sulphation and uronic acid 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. (C) 2011 Elsevier B.V. All rights reserved.
ISSN: 1570-9639
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