| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 10871925 | FEBS Letters | 2010 | 5 Pages | 
Abstract
												Lipocalins are β-barrel proteins, which share three conserved motifs in their amino acid sequence. In this study, we identified by a peptide mapping approach, a seven-amino acid sequence related to one of these motifs (motif 2) that modulates cell survival. A synthetic peptide based on an insect lipocalin displayed cytoprotective activity in serum-deprived endothelial cells and leucocytes. This activity was dependent on nitric oxide synthase. This sequence was found within several lipocalins, including apolipoprotein D, retinol binding protein, lipocalin-type prostaglandin D synthase, and many unknown proteins, suggesting that it is a sequence signature and a lipocalin conserved property.
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											Authors
												Ana Marisa Chudzinski-Tavassi, Linda C. Carrijo-Carvalho, Kaline Waismam, Sandra H.P. Farsky, Oscar H.P. Ramos, Cleyson V. Reis, 
											