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LOPAP (Lonomia obliqua prothrombin activator protease): cloning and expression in Pichia pastoris yeast, design of a synthetic peptide, structural analysis and evaluation of its potential applications.

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Author(s):
Linda Christian Carrijo Carvalho
Total Authors: 1
Document type: Doctoral Thesis
Press: São Paulo.
Institution: Universidade de São Paulo (USP). Instituto de Ciências Biomédicas (ICB/SDI)
Defense date:
Examining board members:
Ana Marisa Chudzinski Tavassi; Heloisa Sobreiro Selistre de Araújo; Viviane Maimoni Gonçalves; Elizabeth Angelica Leme Martins; Marimelia Aparecida Porcionatto
Advisor: Ana Marisa Chudzinski Tavassi
Abstract

Lopap is a prothrombin activator from the L. obliqua caterpillar, belongs to the lipocalin family, and displays antiapoptotic activity. Lopap was obtained in the recombinant form (rLopap) in the P. pastoris yeast, by a scaled up methodology, and its activity was evaluated in vitro and in vivo. Treatment with rLopap reduced the bleeding time in animals anticoagulated with enoxaparin. On the other hand, a Lopap-derived peptide, designated antiapoptotic peptide (AP), was able to induce collagen synthesis in fibroblast culture and in the animal dermis. The region corresponding to AP had similar physical and structural properties when compared with other antiapoptotic lipocalins. These results open perspectives for the use of Lopap, as a procoagulante molecule, and the use of AP, based on its cell modulation effects, as a cosmetic component, aiding tissue repair and in dysfunctions involving cell death and loss of collagen. (AU)