Group V Secretory Phospholipase A₂ Regulates Endocytosis of Acetylated LDL by Transcriptional Activation of PGK1 in RAW264.7 Macrophage Cell Line.

ABSTRACT:

Aims

It was suggested that group V secretory phospholipase A₂ (sPLA₂-V) existed in the nucleus. This study examined whether nuclear sPLA₂-V plays a role in endocytosis of acetylated low-density lipoprotein (AcLDL) in monocyte/macrophage-like cell line RAW264.7 cells.

Methods

RAW264.7 cells were transfected with shRNA vector targeting sPLA₂-V (sPLA₂-V-knockdown [KD] cells) or empty vector (sPLA₂-V-wild-type [WT] cells). AcLDL endocytosis was assessed by incubation with ¹²⁵I-AcLDL or AcLDL conjugated with pHrodo. Actin polymerization was assessed by flow cytometry using Alexa Fluor 546-phalloidin.

Results

In immunofluorescence microscopic studies, sPLA₂-V was detected in the nucleus.

SUBMITTER: Fujioka D 

PROVIDER: S-EPMC9135649 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature