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A lipocalin sequence signature modulates cell survival
Author(s) -
Chudzinski-Tavassi Ana Marisa,
Carrijo-Carvalho Linda C.,
Waismam Kaline,
Farsky Sandra H.P.,
Ramos Oscar H.P.,
Reis Cleyson V.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.05.008
Subject(s) - lipocalin , sequence (biology) , signature (topology) , computational biology , biology , evolutionary biology , genetics , biochemistry , mathematics , geometry
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.