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Data show that phospholipase D2 (PLD2)-produced phosphatidic acid (PA) promoted cell invasion through the the expression of angiogenin (ANG) in clear cell renal cell carcinoma (ccRCC) cells.
AQP3 siRNA and PLD2 siRNA significantly downregulated the mRNA and protein levels of AQP3 and PLD2 in the A431 cells; inhibiting proliferation and promoting apoptosis in vitro.
PLD2 is involved into pathogenesis of a vast array of human diseases, and as such it can be targeted for therapy. (Review)
Slug is a positive regulator, and Snail a negative regulator, of PLD2 expression.
Data suggest that elevated membrane tension acts through phospholipase D2 (PLD2) and the mammalian target of rapamycin complex 2 (mTORC2) to limit actin nucleation.
results suggest that the small GTPase RalA plays an important role in promoting invagination and trafficking of caveolae, not by potentiating the association between Cav-1 and FilA but by stimulating PLD2-mediated generation of phosphatidic acid.
Suggest PLD expression in high grade serous ovarian carcinoma may have a role in mediating progression to effusions and chemoresistance.
PLD2 functions as a key mediator in the VEGF-mediated angiogenic functions of endothelial cells.
PLD2 protein itself interacts with HIF-1alpha, prolyl hydroxylase (PHD) and VHL to promote degradation of HIF-1alpha via the proteasomal pathway independent of lipase activity.
PLD2-mediated production of phosphatidic acid contributed to the control of EGFR exposure to ligand through a multipronged transcriptional and posttranscriptional program during the out-of-control accumulation of EGFR signaling in cancer cells.
These results suggest that PLD2 expression in colon cancer cells is up-regulated via HIF1-alpha in response to hypoxic stress and underscores the crucial role of HIF1-alpha-induced PLD2 in tumor growth.
A 3D model of the PLD2 by combining homology and ab initio 3 dimensional structural modeling methods, and docking conformation, is reported.
PLD2 expression regulates formation of Golgi tubules in Hela cells.
Results indicate distinctive roles of phospholipase D PLD1 and PLD2 isoforms in pathological conditions in retinal pigment epithelium (RPE).
Phospholipase D is involved in the formation of Golgi associated clathrin coated vesicles in human parotid duct cells
PLD2, but not PLD1, directly binds to the C terminus of TREK1 and TREK2.
Ectopic expression of PLD1 or PLD2 in human glioma U87 cells increased the expression of hypoxia-inducible factor-1alpha protein.
Knockdown of PLD2 induces autophagy in colorectal cancer cells.
Inhibition of PLD2 accelerated the accumulation of MxA in foci as early as 30 min postinfection. .. PLD facilitates the rapid endocytosis of influenza virus, permitting viral escape from innate immune detection
Out of these myriads of functions, PLD is becoming recognized as a major player in cell migration, cell invasion, and cancer metastasis.
Results suggest that PLD2 is the isoform that mediates aldosterone secretion and likely priming.
PLD2 is pivotal in the regulation of the integrity of epithelial tight junctions and occludin turn over, thereby implicating it in the pathogenesis of colitis.
High PLD2 expression is associated with Lung Metastasis of Breast Cancer.
Pld1-/- and Pld2-/- mice present elevated free fatty acids (FFA) levels and are insulin as well as glucose intolerant. In conclusion, these data suggest that deficiency of PLD1 or PLD2 activity promotes development of overweight and diabetes.
PLD1/2 signaling pathways are involved in mitogenic signaling in astrocytes.
Data show that although phospholipase D PLD1 deficiency impaired Fc epsilon receptor FcepsilonRI-mediated signaling and mast cell function, phospholipase D PLD2 deficiency actually enhanced these pathways.
PLD2 in neutrophils is essential for the pathogenesis of experimental sepsis
The impact of polyunsaturated fatty acid (PUFA) supplementation on phospholipase D (PLD) trafficking and activity in mast cells was investigated.
AQP3 has a pro-differentiative role in epidermal keratinocytes and PLD2 activity is necessary for this effect.
phosphatidic acid and phospholipase D1 and D2 have roles in leukocyte adhesion
PLD1 and PLD2 have roles in platelet alpha-granule secretion
Demonstrate a novel role for endothelial PLD2 in the survival and migration of ECs under hypoxia via the expression of hypoxia-inducible factor-1alpha and in pathological retinal angiogenesis and tumor angiogenesis in vivo.
Pharmacological PLD inhibition might provide a safe therapeutic strategy to prevent arterial thrombosis and ischemic stroke.
PLD2 is a unique GEF, with the PX being the major catalytic domain for its GEF activity, whereas the pleckstrin homology domain assists in the PX-mediated activity
Data show that the Phospholipase D2 (PLD2)-GTPase Rac2 protein-protein interaction is sufficient for the guanine nucleotide exchange factor (GEF) function.
study reports that a heterotrimeric protein complex exists between PLD2, Grb2, and WASp in vivo, which is integral to phagocytosis
PLD2 positively affects Rac2 GTP loading activity of macrophages. PLD2 drives early chemotaxis. During early cell chemotaxis, PLD2 translocates to the cell membrane and facilitates lamellipodium extension.
Walnut extract induced internalization of the LPS receptor, toll-like receptor 4, and that the anti-inflammatory effects of walnut were dependent on functional activation of phospholipase D2.
Phospholipase D2-dependent inhibition of the nuclear hormone receptor PPARgamma by cyclic phosphatidic acid.
Lipopolysaccharide-induced NO synthesis and iNOS expression were blocked by PLD2 siRNA, suggesting that lipopolysaccharide upregulates NO synthesis through PLD2.
The results indicate that PKC could be the final target and an integrator molecule of different signaling pathways triggered by angiotensin II (Ang II), which could explain the sustained activation of Na(+)-ATPase by Ang II.
The protein encoded by this gene catalyzes the hydrolysis of phosphatidylcholine to phosphatidic acid and choline. The activity of the encoded enzyme is enhanced by phosphatidylinositol 4,5-bisphosphate and ADP-ribosylation factor-1. This protein localizes to the peripheral membrane and may be involved in cytoskeletal organization, cell cycle control, transcriptional regulation, and/or regulated secretion. Two transcript variants encoding different isoforms have been found for this gene.
, phospholipase D2-like
, choline phosphatase 2
, phosphatidylcholine-hydrolyzing phospholipase D2
, PLD 2
, phospholipase D gene 2