Proteomic analysis of lipid rafts from RBL-2H3 mast cells
Nenhuma Miniatura disponível
Data
2019
Título da Revista
ISSN da Revista
Título de Volume
Editor
Resumo
Lipid rafts are highly ordered membrane microdomains enriched in cholesterol,
glycosphingolipids, and certain proteins. They are involved in the regulation of cellular processes in
diverse cell types, including mast cells (MCs). The MC lipid raft protein composition was assessed
using qualitative mass spectrometric characterization of the proteome from detergent-resistant
membrane fractions from RBL-2H3 MCs. Using two different post-isolation treatment methods, a
total of 949 lipid raft associated proteins were identified. The majority of these MC lipid raft proteins
had already been described in the RaftProtV2 database and are among highest cited/experimentally
validated lipid raft proteins. Additionally, more than half of the identified proteins had lipid
modifications and/or transmembrane domains. Classification of identified proteins into functional
categories showed that the proteins were associated with cellular membrane compartments, and with
some biological and molecular functions, such as regulation, localization, binding, catalytic activity,
and response to stimulus. Furthermore, functional enrichment analysis demonstrated an intimate
involvement of identified proteins with various aspects of MC biological processes, especially those
related to regulated secretion, organization/stabilization of macromolecules complexes, and signal
transduction. This study represents the first comprehensive proteomic profile of MC lipid rafts
and provides additional information to elucidate immunoregulatory functions coordinated by raft
proteins in MCs.
Descrição
Palavras-chave
Lipid rafts, Membrane proteins, Protein localization, Regulated secretion, Signaling pathway, Proteome, Mast cells
Citação
FREITAS FILHO, Edismauro Garcia et al. Proteomic analysis of lipid rafts from RBL-2H3 mast cells. International Journal of Molecular Sciences, Basel, v. 20, n. 16, e3904, 2019. DOI: 10.3390/ijms20163904. Disponível em: https://www.mdpi.com/1422-0067/20/16/3904; Acesso em: 22 nov. 2024.