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study uncovers two competing processes triggered by Picornaviridae virus entry: activation of a pore-activated clearance pathway and recruitment of a PLA2G16 phospholipase to enable genome release
Demonstrate increased PLA2G16 expression activates the MAPK (show MAPK1 ELISA Kits) pathway to enhance osteosarcoma metastasis.
our results revealed that H-rev107 is also involved in lipid accumulation in liver cells through the POR (show POR ELISA Kits) pathway via its PLA2 (show YWHAZ ELISA Kits) activity.
Results show that osteosarcoma patients with metastasis showed higher expression of PLA2G16 at both the mRNA and protein levels and shorter overall survival suggesting it as significant prognostic factor for poor outcome.
the flexible main loop of H-REV107, but not that of TIG3, is critical for its NTD to modulate its CTD in inducing cell death.
crystal structure of the HRASLS3-LRAT chimeric enzyme in a thioester catalytic intermediate state revealed a major structural rearrangement accompanied by three-dimensional domain swapping dimerization not observed in native HRASLS
several mutant p53 (show TP53 ELISA Kits) proteins bind the Pla2g16 promoter at E26 transformation-specific (ETS (show ETS1 ELISA Kits)) binding motifs and knockdown of ETS2 (show ETS2 ELISA Kits) suppressed mutant p53 (show TP53 ELISA Kits) induction of Pla2g16.
Our study further suggests that the PLA/AT activity of H-rev107 may play an important role in H-rev107-mediated RAS suppression.
an alternate mechanism for AdPLA in promoting adipose tissue lipolysis that is not contingent on the release of arachidonic acid and that is compatible with its combined PLA(1 (show POU2F3 ELISA Kits))/A(2) activity
Data show that acyl-modified forms of HRAS (show HRAS ELISA Kits)-like tumor suppressors HRASLS2 and HRASLS3 mimicking lipolytic activity of lecithin retinol acyltransferase LRAT (show LRAT ELISA Kits).
H-rev107, through PTGDS, suppressed cell migration and invasion. Data suggest that the PGD2-cAMP-SOX9 signal pathway might play an important role in H-rev107-mediated cancer cell invasion in testes.
H-rev107 interferes with the biosynthesis of ether-type lipids and is responsible for the dysfunction of peroxisomes in H-rev107-expressing cells.
identification of an Sp1/Sp3-binding GC-box required for the transcription of H-rev107 (H-rev107)
study found that AdPLA that was previously known as H-Rev-107/HRASLS3 is an adipose-specific, calcium-dependent histidine PLA2 (show PLA2G2A ELISA Kits)
HRASLS3 as one of the downstream effectors of PPARgamma (show PPARG ELISA Kits) action in adipogenesis.
Single nucleotide polymorphisms in the adipose specific phospholipase A2 are associated with growth traits in cattle.
gene whose expression is suppressed by HRAS
HRAS-like suppressor 3
, H-rev 107 protein homolog
, group XVI phospholipase A1/A2
, group XVI phospholipase A2
, Ca-independent phospholipase A1/2
, HRAS-like suppressor 1
, adipose-specific PLA2
, adipose-specific phospholipase A2
, renal carcinoma antigen NY-REN-65
, H-rev 107 protein
, HRAS like suppressor 3
, LRAT-like protein 3
, Hras-revertant gene 107 (expression down-regulated in HRAS-transformed rat 208F fibroblasts)