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LPS upregulates palmitoylated enzymes of the phosphatidylinositol cycle. An insight from proteomic studies.

ABSTRACT: The studies aim at revealing changes of the level of fatty-acylated proteins induced by LPS in RAW264 macrophage-like cells

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture, Macrophage

SUBMITTER: Monika Zareba-Koziol

LAB HEAD: Katarzyna Kwiatkowska

PROVIDER: PXD007918 | Pride | 2017-12-15

REPOSITORIES: Pride

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Publications

Lipopolysaccharide Upregulates Palmitoylated Enzymes of the Phosphatidylinositol Cycle: An Insight from Proteomic Studies.

Sobocińska Justyna J Roszczenko-Jasińska Paula P Zaręba-Kozioł Monika M Hromada-Judycka Aneta A Matveichuk Orest V OV Traczyk Gabriela G Łukasiuk Katarzyna K Kwiatkowska Katarzyna K

Molecular & cellular proteomics : MCP 20171207 2

Lipopolysaccharide (LPS) is a component of the outer membrane of Gram-negative bacteria that induces strong proinflammatory reactions of mammals. These processes are triggered upon sequential binding of LPS to CD14, a GPI-linked plasma membrane raft protein, and to the TLR4/MD2 receptor complex. We have found earlier that upon LPS binding, CD14 triggers generation of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P<sub>2</sub>], a lipid controlling subsequent proinflammatory cytokine production. ...[more]

PMID: 29217618

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