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Human GPLD1 ELISA Kit for Sandwich ELISA - ABIN423573
Lindqvist, Wallinder, Bergström, Henriksson: Plasma glycosylphosphatidylinositol phospholipase D (GPI-PLD) and abdominal aortic aneurysm. in International journal of clinical and experimental medicine 2012
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Human GPLD1 ELISA Kit for Sandwich ELISA - ABIN840378
Rosso, Lhomme, Meroño, Sorroche, Catoggio, Soriano, Saucedo, Malah, Dauteuille, Boero, Lesnik, Robillard, John Chapman, Brites, Kontush: Altered lipidome and antioxidative activity of small, dense HDL in normolipidemic rheumatoid arthritis: relevance of inflammation. in Atherosclerosis 2014
Study discovered novel and independent associations of prediabetes and related traits with MASP1 (show MASP1 ELISA Kits), and some evidence for associations with THBS1 (show THBS1 ELISA Kits), GPLD1 and ApoA-IV (show APOA4 ELISA Kits), suggesting a role for these proteins in the pathophysiology of type 2 diabetes.
c-Myc (show MYC ELISA Kits) influences GPI (show GNPDA1 ELISA Kits)-AP signaling transcriptionally and posttranslational and represses GPI (show GNPDA1 ELISA Kits)-AP anti-proliferative signaling in tumors
An observed increase in PLD (show PLD ELISA Kits) activity was mediated through boosting the binding of PLD (show PLD ELISA Kits) with dynamin (show DNM1 ELISA Kits) which in turn facilitated fibronectin (show FN1 ELISA Kits)-induced cell spreading.
Low aggressive MCF-7 breast cancer cells have low endogenous PLD (show PLD ELISA Kits) enzymatic activity and cell invasion, concomitant with high expression of miR (show MLXIP ELISA Kits)-203, -887, and -3619 and miR (show MLXIP ELISA Kits)-182 and miR (show MLXIP ELISA Kits)-182.
suggest that the down-regulation of GPI-PLD protein may be involved in prion (show PRNP ELISA Kits) propagation in the brains of prion (show PRNP ELISA Kits) diseases
our findings showed that ANRIL is an lncRNA responsible in anti-tumorigenesis caused by PLD (show PLD ELISA Kits) inhibition and combined incorporation of ANRIL into PLD (show PLD ELISA Kits) inhibition-induced anti-tumorigenic signaling network
AMPK (show PRKAA1 ELISA Kits) suppresses PLD (show PLD ELISA Kits) activity, and PLD (show PLD ELISA Kits) suppresses AMPK (show PRKAA1 ELISA Kits) via mTOR (show FRAP1 ELISA Kits).
Functional regulation of phospholipase D (show PLD ELISA Kits) expression in cancer and inflammation.
Phospholipase D (show PLD ELISA Kits) and the maintenance of phosphatidic acid levels for regulation of mammalian target of rapamycin (mTOR (show FRAP1 ELISA Kits)).
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.
Overexpressing GPI-PLD in an insulinoma (show RPS15 ELISA Kits) cell line enhanced glucose-stimulated insulin (show INS ELISA Kits) secretion, suggesting that enhanced insulin (show INS ELISA Kits) secretion in vivo may have contributed to the improved glucose tolerance.
GPI-PLD expression was significantly increased in highly malignant. H-ras (show HRAS ELISA Kits)-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 (show PLD ELISA Kits) influences triglyceride-rich lipoprotein metabolism.
Results suggest that cell-specific Gpld1- or peptidase-dependent pathways for prostasin (show PRSS8 ELISA Kits) secretion may control prostasin (show PRSS8 ELISA Kits) functions in a tissue-specific manner.
PLD (show PLD ELISA Kits) 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