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PLD2 protein itself interacts with HIF-1alpha (show HIF1A ELISA Kits), prolyl hydroxylase (PHD (show PDC ELISA Kits)) and VHL (show VHL ELISA Kits) to promote degradation of HIF-1alpha (show HIF1A ELISA Kits) via the proteasomal pathway independent of lipase (show LIPG ELISA Kits) activity.
PLD2-mediated production of phosphatidic acid contributed to the control of EGFR (show EGFR ELISA Kits) exposure to ligand through a multipronged transcriptional and posttranscriptional program during the out-of-control accumulation of EGFR (show EGFR ELISA Kits) signaling in cancer cells.
These results suggest that PLD2 expression in colon cancer cells is up-regulated via HIF1-alpha (show HIF1A ELISA Kits) in response to hypoxic stress and underscores the crucial role of HIF1-alpha (show HIF1A ELISA Kits)-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 (show PLD ELISA Kits) 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 (show KCNK2 ELISA Kits) and TREK2 (show KCNK10 ELISA Kits).
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.
Results suggest that PLD2 is the isoform that mediates aldosterone secretion and likely priming.
PLD1/2 signaling pathways are involved in mitogenic signaling in astrocytes.
Data show that although phospholipase D PLD1 (show PLD ELISA Kits) deficiency impaired Fc epsilon receptor FcepsilonRI (show FCER1A ELISA Kits)-mediated signaling and mast cell function, phospholipase D (show PLD ELISA Kits) 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 (show PLD ELISA Kits)) trafficking and activity in mast cells was investigated.
AQP3 (show AQP3 ELISA Kits) 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 (show PLD ELISA Kits) inhibition might provide a safe therapeutic strategy to prevent arterial thrombosis and ischemic stroke.
PLD2 is a unique GEF (show ARHGEF2 ELISA Kits), with the PX being the major catalytic domain for its GEF (show ARHGEF2 ELISA Kits) activity, whereas the pleckstrin (show PLEK ELISA Kits) homology domain assists in the PX-mediated activity
The results indicate that PKC (show FYN ELISA Kits) 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 (show DNAH8 ELISA Kits) by Ang II (show AGT ELISA Kits).
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