DESENVOLVIMENTO DE MATERIAL MULTIMÁDIA NO ENSINO DE BIOLOGIA

oai:ojs.eademfoco.cecierj.edu.br:article/5Apresentamos uma metodologia de produção de aulas multimídia para estudantes do curso de Licenciatura em Ciências Biológicas, na modalidade semipresencial. Nosso método tem como base um conteúdo disponibilizado sob a forma de animações interativas. Através de uma navegação linear, o aluno possui pleno controle do andamento da aula, tendo como estímulos a riqueza visual e a interatividade, permitindo caminhar no seu próprio tempo até a completa compreensão do conteúdo. Este conteúdo se apresenta em uma linguagem coloquial simulando a presença de um professor competente e simpático, além de descomplicado. Toda a estrutura da aula é fundamentada no construtivismo e no cognitivismo e cada um dos aspectos envolvidos na produção do material multimídia, como cores, tipografia, animações, analogias e bom humor são utilizados como estratégias motivadoras e facilitadoras do processo de aprendizado. Uma equipe especializada na produção gráfica, acompanhada de pós-graduados em biociências, revisores de português e de conteúdo produz cada aula, discutindo aspectos relevantes do ensino-aprendizagem. O resultado é um material multimídia rico, disponibilizado em CD e/ou online, que permite que o aluno aprenda sozinho

The interaction of Thrombospondins with extracellular matrix proteins

The thrombospondins (TSPs) are a family of five matricellular proteins that appear to function as adapter molecules to guide extracellular matrix synthesis and tissue remodeling in a variety of normal and disease settings. Various TSPs have been shown to bind to fibronectin, laminin, matrilins, collagens and other extracellular matrix (ECM) proteins. The importance of TSP-1 in this context is underscored by the fact that it is rapidly deposited at the sites of tissue damage by platelets. An association of TSPs with collagens has been known for over 25 years. The observation that the disruption of the TSP-2 gene in mice leads to collagen fibril abnormalities provided important in vivo evidence that these interactions are physiologically important. Recent biochemical studies have shown that TSP-5 promotes collagen fibril assembly and structural studies suggest that TSPs may interact with collagens through a highly conserved potential metal ion dependent adhesion site (MIDAS). These interactions are critical for normal tissue homeostasis, tumor progression and the etiology of skeletal dysplasias

The Calreticulin-Binding Sequence of Thrombospondin 1 Regulates Collagen Expression and Organization During Tissue Remodeling

Amino acids 17-35 of the thrombospondin1 (TSP1) N-terminal domain (NTD) bind cell surface calreticulin to signal focal adhesion disassembly, cell migration, and anoikis resistance in vitro. However, the in vivo relevance of this signaling pathway has not been previously determined. We engineered local in vivo expression of the TSP1 calreticulin-binding sequence to determine the role of TSP1 in tissue remodeling. Surgical sponges impregnated with a plasmid encoding the secreted calreticulin-binding sequence [NTD (1-35)-EGFP] or a control sequence [mod NTD (1-35)-EGFP] tagged with enhanced green fluorescent protein were implanted subcutaneously in mice. Sponges expressing NTD (1-35)-EFGP formed a highly organized capsule despite no differences in cellular composition, suggesting stimulation of collagen deposition by the calreticulin-binding sequence of TSP1. TSP1, recombinant NTD, or a peptide of the TSP1 calreticulin-binding sequence (hep I) increased both collagen expression and matrix deposition by fibroblasts in vitro. TSP1 stimulation of collagen was inhibited by a peptide that blocks TSP1 binding to calreticulin, demonstrating the requirement for cell surface calreticulin. Collagen stimulation was independent of TGF-β activity and Smad phosphorylation but was blocked by an Akt inhibitor, suggesting that signaling through the Akt pathway is important for regulation of collagen through TSP1 binding to calreticulin. These studies identify a novel function for the NTD of TSP1 as a mediator of collagen expression and deposition during tissue remodeling