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An observed increase in PLD activity was mediated through boosting the binding of PLD with dynamin (show DNM1 Proteins) which in turn facilitated fibronectin (show FN1 Proteins)-induced cell spreading.
Low aggressive MCF-7 breast cancer cells have low endogenous PLD enzymatic activity and cell invasion, concomitant with high expression of miR (show MLXIP Proteins)-203, -887, and -3619 and miR (show MLXIP Proteins)-182 and miR (show MLXIP Proteins)-182.
suggest that the down-regulation of GPI-PLD protein may be involved in prion (show PRNP Proteins) propagation in the brains of prion (show PRNP Proteins) diseases
our findings showed that ANRIL is an lncRNA responsible in anti-tumorigenesis caused by PLD inhibition and combined incorporation of ANRIL into PLD inhibition-induced anti-tumorigenic signaling network
AMPK (show PRKAA1 Proteins) suppresses PLD activity, and PLD suppresses AMPK (show PRKAA1 Proteins) via mTOR (show FRAP1 Proteins).
Functional regulation of phospholipase D expression in cancer and inflammation.
Phospholipase D and the maintenance of phosphatidic acid levels for regulation of mammalian target of rapamycin (mTOR (show FRAP1 Proteins)).
At the cellular level, PLD and its reaction product, phosphatidate, interact with a large number of protein partners that are directly related to the actin cytoskeleton and cell migration.
PLD1 and PLD2 (show PLD2 Proteins) mutants inhibit very-low-density lipoprotein-induced aldosterone production in HAC15 cells.
This study indicated that PLD participates in the same signaling pathway in this breast cancer cell line.
Overexpressing GPI-PLD in an insulinoma (show RPS15 Proteins) cell line enhanced glucose-stimulated insulin (show INS Proteins) secretion, suggesting that enhanced insulin (show INS Proteins) secretion in vivo may have contributed to the improved glucose tolerance.
GPI-PLD expression was significantly increased in highly malignant. H-ras (show HRAS Proteins)-transfected murine bladder carcinoma cells as compared to the low malignant, non-transfected parental cells.
His29, His125, His133 and His158 are required for GPI-PLD catalytic activity
Glycosylphosphatidylinositol-specific phospholipase D influences triglyceride-rich lipoprotein metabolism.
Results suggest that cell-specific Gpld1- or peptidase-dependent pathways for prostasin (show PRSS8 Proteins) secretion may control prostasin (show PRSS8 Proteins) functions in a tissue-specific manner.
PLD plays an important role in inflammatory responses and could be involved in a mechanism for the regulation of endothelial barrier function during hyperoxic lung injury
Many proteins are tethered to the extracellular face of eukaryotic plasma membranes by a glycosylphosphatidylinositol (GPI) anchor. The GPI-anchor is a glycolipid found on many blood cells. The protein encoded by this gene is a GPI degrading enzyme. Glycosylphosphatidylinositol specific phospholipase D1 hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, thereby releasing the attached protein from the plasma membrane.
glycosylphosphatidylinositol specific phospholipase D1
, phosphatidylinositol-glycan-specific phospholipase D-like
, glycosylphosphatidylinositol specific phospholipase d1
, GPI-specific phospholipase D
, PI-G PLD
, glycoprotein phospholipase D
, phosphatidylinositol-glycan-specific phospholipase D
, glycosyl-phosphatidylinositol-specific phospholipase D
, glycosylphosphatidylinositol phospholipase D