Ignet

Gene Information

Gene symbol: GPLD1

Gene name: glycosylphosphatidylinositol specific phospholipase D1

HGNC ID: 4459

Related Genes

#	Gene Symbol	Number of hits
1	ABCA1	1 hits
2	ABCB11	1 hits
3	ABHD12	1 hits
4	ABO	1 hits
5	ADCY10	1 hits
6	AGRN	1 hits
7	AGT	1 hits
8	AKR1B1	1 hits
9	APLP2	1 hits
10	ARC	1 hits
11	ARF1	1 hits
12	ASGR1	1 hits
13	ATP8B1	1 hits
14	BST2	1 hits
15	C1R	1 hits
16	C1S	1 hits
17	CD276	1 hits
18	CD81	1 hits
19	CDH6	1 hits
20	CDKN2A	1 hits
21	EFNA1	1 hits
22	ENPP2	1 hits
23	EPHA2	1 hits
24	EPSTI1	1 hits
25	FADS1	1 hits
26	FADS2	1 hits
27	FPR1	1 hits
28	FUT2	1 hits
29	GCKR	1 hits
30	GGT1	1 hits
31	GSTT1	1 hits
32	GSTT2	1 hits
33	HEXA	1 hits
34	HNF1A	1 hits
35	IAPP	1 hits
36	ID2	1 hits
37	IFITM1	1 hits
38	IGF1	1 hits
39	INS	1 hits
40	JAK2	1 hits
41	JMJD1C	1 hits
42	LGALS3BP	1 hits
43	LGALS9	1 hits
44	MAP2K1	1 hits
45	MAPK1	1 hits
46	MAPK3	1 hits
47	MAPK6	1 hits
48	MET	1 hits
49	MFGE8	1 hits
50	MICAL3	1 hits
51	MLXIPL	1 hits
52	NMB	1 hits
53	PIGA	1 hits
54	PIK3CA	1 hits
55	PLA2G1B	1 hits
56	PLCB1	1 hits
57	PLD2	1 hits
58	PNPLA3	1 hits
59	PPAP2A	1 hits
60	PPP1R3B	1 hits
61	PPRC1	1 hits
62	PRKAA1	1 hits
63	PRKCA	1 hits
64	PRKCB1	1 hits
65	PRKCSH	1 hits
66	PRKCZ	1 hits
67	PTK2B	1 hits
68	RORA	1 hits
69	RPL3	1 hits
70	SERPING1	1 hits
71	SLC2A2	1 hits
72	SLC2A4	1 hits
73	ST3GAL4	1 hits
74	STAT4	1 hits
75	TGM2	1 hits
76	TIMP2	1 hits
77	TNNT2	1 hits
78	TRIB1	1 hits
79	TYK2	1 hits
80	ZHX2	1 hits
81	ZNF827	1 hits

Related Sentences

#	PMID	Sentence
1	1402897	These results support the conclusion that protein kinase C modulates phospholipase D activity in nerve and suggest that in diabetic nerve the enzyme activation mechanism may possess increased sensitivity.
2	1636507	These findings support the conclusion that DAG is principally derived from phosphoinositides by phospholipase C hydrolysis, but a minor fraction could be derived from phosphatidylcholine either by the action of phospholipase C or via phospholipase D and PA phosphatase.
3	2675833	In neonatal rat islet cells prelabelled with [14C-methyl] choline, the phorbol ester 12-O-tetradecanoylphorbol-13-acetate rapidly activated a phospholipase D-like mechanism as suggested by the accumulation in cells and medium of choline (but not of phosphorylcholine or glycerophosphorylcholine, markers for phospholipase C and phospholipase A2 action on phosphatidylcholine).
4	2675833	Phospholipase D was also activated by ionomycin or sodium fluoride; however, this was accompanied by parallel increases in diglyceride, monoacylglycerol and arachidonic acid in the absence of phosphorylcholine generation, suggesting that these agents also activated a phospholipase C-diglyceride lipase pathway acting on non-choline-containing phosphoglycerides (presumably phosphoinositides).
5	2675833	Larkins, Diabetes, in press), our findings suggest for the first time a possible role for phospholipase D activation in the stimulation of insulin release and may imply a novel site of action for phorbol esters in the regulation of exocytosis.
6	2675833	In neonatal rat islet cells prelabelled with [14C-methyl] choline, the phorbol ester 12-O-tetradecanoylphorbol-13-acetate rapidly activated a phospholipase D-like mechanism as suggested by the accumulation in cells and medium of choline (but not of phosphorylcholine or glycerophosphorylcholine, markers for phospholipase C and phospholipase A2 action on phosphatidylcholine).
7	2675833	Phospholipase D was also activated by ionomycin or sodium fluoride; however, this was accompanied by parallel increases in diglyceride, monoacylglycerol and arachidonic acid in the absence of phosphorylcholine generation, suggesting that these agents also activated a phospholipase C-diglyceride lipase pathway acting on non-choline-containing phosphoglycerides (presumably phosphoinositides).
8	2675833	Larkins, Diabetes, in press), our findings suggest for the first time a possible role for phospholipase D activation in the stimulation of insulin release and may imply a novel site of action for phorbol esters in the regulation of exocytosis.
9	2675833	In neonatal rat islet cells prelabelled with [14C-methyl] choline, the phorbol ester 12-O-tetradecanoylphorbol-13-acetate rapidly activated a phospholipase D-like mechanism as suggested by the accumulation in cells and medium of choline (but not of phosphorylcholine or glycerophosphorylcholine, markers for phospholipase C and phospholipase A2 action on phosphatidylcholine).
10	2675833	Phospholipase D was also activated by ionomycin or sodium fluoride; however, this was accompanied by parallel increases in diglyceride, monoacylglycerol and arachidonic acid in the absence of phosphorylcholine generation, suggesting that these agents also activated a phospholipase C-diglyceride lipase pathway acting on non-choline-containing phosphoglycerides (presumably phosphoinositides).
11	2675833	Larkins, Diabetes, in press), our findings suggest for the first time a possible role for phospholipase D activation in the stimulation of insulin release and may imply a novel site of action for phorbol esters in the regulation of exocytosis.
12	7653525	In the presence of ethanol, ANG II markedly increased phosphatidylethanol (PEt) formation, indicating activation of phospholipase D (PLD).
13	7653525	ANG II was shown to increase the mass of three separate PA species, one of which apparently originated from DAG kinase action on PC-phospholipase C (PLC)-produced DAG, providing evidence for PC-PLC activity.
14	7653525	These results demonstrate that multiple lipid signals propagated via collateral stimulation of PLC and PLD are generated by specific activation of the vascular type 1a ANG II receptor.
15	7791518	Under the present conditions, N-acetyl-beta-glucosaminidase release and superoxide generation, which are known to be dependent on phospholipase D activation, were higher in the cells from diabetic rats than those in the cells from control rats.
16	7867887	Phospholipase D hydrolysis of lipids from human retinal pigment epithelial cells constitutively overexpressing the aldose reductase gene yielded a sorbitol-like compound whose appearance was increased by glucose exposure and was decreased by an aldose reductase inhibitor.
17	8611143	The phosphatidylinositol 3-kinase inhibitor, wortmannin, inhibits insulin-induced activation of phosphatidylcholine hydrolysis and associated protein kinase C translocation in rat adipocytes.
18	8611143	We questioned whether phosphatidylinositol 3-kinase (PI 3-kinase) and protein kinase C (PKC) function as interrelated signalling mechanisms during insulin action in rat adipocytes.
19	8611143	Insulin rapidly activated a phospholipase D that hydrolyses phosphatidylcholine (PC), and this activation was accompanied by increases in diacylglycerol and translocative activation of PKC-alpha and PKC-beta in the plasma membrane.
20	8611143	Wortmannin, an apparently specific PI 3-kinase inhibitor, inhibited insulin-stimulated, phospholipase D-dependent PC hydrolysis and subsequent translocation of PKC-alpha and PKC-beta to the plasma membrane.
21	8611143	Our findings suggest that insulin acts through PI 3-kinase to activate a PC-specific phospholipase D and causes the translocative activation of PKC-alpha and PKC-beta in plasma membranes of rat adipocytes.
22	8611143	The phosphatidylinositol 3-kinase inhibitor, wortmannin, inhibits insulin-induced activation of phosphatidylcholine hydrolysis and associated protein kinase C translocation in rat adipocytes.
23	8611143	We questioned whether phosphatidylinositol 3-kinase (PI 3-kinase) and protein kinase C (PKC) function as interrelated signalling mechanisms during insulin action in rat adipocytes.
24	8611143	Insulin rapidly activated a phospholipase D that hydrolyses phosphatidylcholine (PC), and this activation was accompanied by increases in diacylglycerol and translocative activation of PKC-alpha and PKC-beta in the plasma membrane.
25	8611143	Wortmannin, an apparently specific PI 3-kinase inhibitor, inhibited insulin-stimulated, phospholipase D-dependent PC hydrolysis and subsequent translocation of PKC-alpha and PKC-beta to the plasma membrane.
26	8611143	Our findings suggest that insulin acts through PI 3-kinase to activate a PC-specific phospholipase D and causes the translocative activation of PKC-alpha and PKC-beta in plasma membranes of rat adipocytes.
27	8611143	The phosphatidylinositol 3-kinase inhibitor, wortmannin, inhibits insulin-induced activation of phosphatidylcholine hydrolysis and associated protein kinase C translocation in rat adipocytes.
28	8611143	We questioned whether phosphatidylinositol 3-kinase (PI 3-kinase) and protein kinase C (PKC) function as interrelated signalling mechanisms during insulin action in rat adipocytes.
29	8611143	Insulin rapidly activated a phospholipase D that hydrolyses phosphatidylcholine (PC), and this activation was accompanied by increases in diacylglycerol and translocative activation of PKC-alpha and PKC-beta in the plasma membrane.
30	8611143	Wortmannin, an apparently specific PI 3-kinase inhibitor, inhibited insulin-stimulated, phospholipase D-dependent PC hydrolysis and subsequent translocation of PKC-alpha and PKC-beta to the plasma membrane.
31	8611143	Our findings suggest that insulin acts through PI 3-kinase to activate a PC-specific phospholipase D and causes the translocative activation of PKC-alpha and PKC-beta in plasma membranes of rat adipocytes.
32	8699936	Phosphatidic acid, a phospholipase D (PLD) -mediated product of membrane phosphatidylcholine is decreased in response to FMLP.
33	8699936	These data show that decreased superoxide generation by neutrophils in insulin-dependent diabetics is, in part, due to impaired activation of phospholipase D and is solely due to high glucose concentrations.
34	8699936	Phosphatidic acid, a phospholipase D (PLD) -mediated product of membrane phosphatidylcholine is decreased in response to FMLP.
35	8699936	These data show that decreased superoxide generation by neutrophils in insulin-dependent diabetics is, in part, due to impaired activation of phospholipase D and is solely due to high glucose concentrations.
36	8922363	Six of the obtained sequences showed homology to known precursor proteins, three of which--GLUT2 receptor, phosphatidylinositol-glycan-specific phospholipase D, and 5-hydroxytryptamine-1F receptor--have a limited, tissue-specific expression.
37	9500869	Experimental evidence suggests that the myocardial phospholipase D (PLD)-phosphatidate phosphohydrolase (PAP) signalling pathway may regulate Ca2+ movements and contractile performance of the heart.
38	9500869	As abnormal Ca2+ homeostasis is associated with diabetic cardiomyopathy, we examined the functional status of the PLD/PAP pathway in sarcolemmal (SL) membranes isolated from insulin-dependent diabetic rat hearts at 8 weeks after a single i.v. injection of streptozotocin (65 mh/kg b.w.).
39	9500869	Two weeks of insulin therapy to the 6 week diabetic animals normalized PLD, while PAP activity and PtdOH level were significantly modified, but had not completely reverted to control values.
40	9555086	Neuromedin B activates phospholipase D through both PKC-dependent and PKC-independent mechanisms.
41	9555086	The actions of neuromedin B (NMB), a recently discovered mammalian bombesin-related peptide, are mediated by interacting with a distinct receptor; however, little is known about its cellular basis of action.
42	9555086	The purpose of the present study was to determine whether activation of the NMB receptor causes activation of PLD and to explore whether this activation was coupled to PLC activation.
43	9555086	Increases in PLD activity were rapid and NMB was 100-fold more potent than gastrin-releasing peptide (GRP).
44	9555086	The Ca2+-ATPase inhibitor, thapsigargin, did not affect NMB- or TPA-stimulated PLD activities, although it blocked completely the NMB-induced increase in [Ca2+]i.
45	9555086	These data indicate that NMB receptor activation is coupled to both PLC and PLD.
46	9555086	In contrast to a number of other phospholipase C-coupled receptors, NMB receptor stimulated changes in [Ca2+]i do not contribute to PLD activation.
47	9726234	Eight mRNAs were overexpressed in ob/ob muscle: Id2 (a negative regulator of the basic helix-loop-helix family of transcription factors), fast skeletal muscle troponin T, ribosomal protein L3, the integral protein of the peroxisomal membrane 22PMP, the mammalian homolog of geranylgeranyl pyrophosphate synthase, an mRNA related to phosphatidylinositol-glycan-specific phospholipase D, and two unknown mRNAs.
48	9726234	Because the primary genetic defect in the ob/ob mouse is known to be in the leptin gene, these data indicate how acquired alterations in gene expression of multiple classes of proteins may play a role in the complex pathogenesis of insulin resistance in obesity and diabetes.
49	9765358	[DPhe6,betaAla11,Phe13,Nle14]Bn(6-14) stimulated phospholipase D activity and a concentration-dependent release of [3H]inositol phosphate (EC50 = 25 nM) and intracellular calcium (EC50 = 14 nM); the increases in intracellular calcium were primarily from intracellular stores. hBRS-3 activation was not coupled to changes in adenylate cyclase activity, [3H]-thymidine incorporation or cell proliferation.
50	10353842	However, stable fBB4-R cell lines were obtained in CHO-K1 cells which were shown to faithfully demonstrate the correct pharmacology of the related Bn receptor, the GRP receptor, when expressed in these cells.
51	10353842	Three of the five classes of Bn receptor antagonists that interacted with higher affinity with the fBB4-R functioned as fBB4-R antagonists and two as partial agonists. fBB4-R activation stimulated increases in phospholipase D (PLD) over the same range of concentrations at which it activated phospholipase C.
52	10748000	We conclude that GH rapidly increases the beta-cell cytoplasmic free [Ca(2+)] and also evokes a similar increase in DAG content via a phosphatidylcholine-specific phospholipase C, but does not affect mitogen-activated protein kinases, phospholipase D, or the cAMP signaling pathway.
53	10919268	Among the different IL-1beta-induced genes, there was an early and transient increase in phospholipase D-1 (PLD1) expression.
54	10919268	PLD1 can induce phosphatidic acid formation and subsequent activation of protein kinase C, a process which stimulates insulin release.
55	10919268	By using different combinations of primers and RT-PCR, we observed that IL-1beta induces an early increase (2 and 6 h) in the expression of both alternatively spliced isoforms of PLD1 (PLD1alpha and 1b).
56	10919268	NG-methyl-L-arginine (LMA), a blocker of the inducible form of nitric oxide synthase (iNOS), prevented this late inhibitory effect of IL-1beta, suggesting that IL-1beta-induced decrease in PLD1a expression is NO-mediated.
57	10919268	IL-1beta induced an early (2-6 h) and sustained (16-24 h) increase in PLD1a mRNA expression in insulin-producing RINm5F cells.
58	10919268	RINm5F cells, but not primary beta-cells, expressed PLD2, and the expression of this gene was not affected by IL-1beta.
59	10919268	In conclusion, we have shown that the cytokine IL-1beta regulates PLD1 expression in primary and clonal beta-cells.
60	10919268	The early induction of PLD1 probably contributes to the early stimulatory effects of IL-1beta on islet insulin release.
61	11404232	Insulin may regulate GPI-PLD expression, because insulin treatment of diabetic NOD mice corrected the hyperglycemia along with reducing serum GPI-PLD activity and liver mRNA.
62	11463795	Glucose activates protein kinase C-zeta /lambda through proline-rich tyrosine kinase-2, extracellular signal-regulated kinase, and phospholipase D: a novel mechanism for activating glucose transporter translocation.
63	11463795	Insulin controls glucose uptake by translocating GLUT4 and other glucose transporters to the plasma membrane in muscle and adipose tissues by a mechanism that appears to require protein kinase C (PKC)-zeta/lambda operating downstream of phosphatidylinositol 3-kinase.
64	11463795	Presently, we found that glucose acutely activated PKC-zeta/lambda in rat adipocytes and rat skeletal muscle preparations by a mechanism that was independent of phosphatidylinositol 3-kinase but, interestingly, dependent on the apparently sequential activation of the dantrolene-sensitive, nonreceptor proline-rich tyrosine kinase-2; components of the extracellular signal-regulated kinase (ERK) pathway, including, GRB2, SOS, RAS, RAF, MEK1 and ERK1/2; and, most interestingly, phospholipase D, thus yielding increases in phosphatidic acid, a known activator of PKC-zeta/lambda.
65	11463795	This activation of PKC-zeta/lambda, moreover, appeared to be required for glucose-induced increases in GLUT4 translocation and glucose transport in adipocytes and muscle cells.
66	11463795	Glucose activates protein kinase C-zeta /lambda through proline-rich tyrosine kinase-2, extracellular signal-regulated kinase, and phospholipase D: a novel mechanism for activating glucose transporter translocation.
67	11463795	Insulin controls glucose uptake by translocating GLUT4 and other glucose transporters to the plasma membrane in muscle and adipose tissues by a mechanism that appears to require protein kinase C (PKC)-zeta/lambda operating downstream of phosphatidylinositol 3-kinase.
68	11463795	Presently, we found that glucose acutely activated PKC-zeta/lambda in rat adipocytes and rat skeletal muscle preparations by a mechanism that was independent of phosphatidylinositol 3-kinase but, interestingly, dependent on the apparently sequential activation of the dantrolene-sensitive, nonreceptor proline-rich tyrosine kinase-2; components of the extracellular signal-regulated kinase (ERK) pathway, including, GRB2, SOS, RAS, RAF, MEK1 and ERK1/2; and, most interestingly, phospholipase D, thus yielding increases in phosphatidic acid, a known activator of PKC-zeta/lambda.
69	11463795	This activation of PKC-zeta/lambda, moreover, appeared to be required for glucose-induced increases in GLUT4 translocation and glucose transport in adipocytes and muscle cells.
70	11855934	Insulin reduces serum glycosylphosphatidylinositol phospholipase D levels in human type I diabetic patients and streptozotocin diabetic rats.
71	11855934	The enzyme glycosylphosphatidylinositol phospholipase D has a postulated role in the insulin-mimetic signaling pathway of glycosylphosphatidylinositol compounds.
72	11855934	Insulin therefore decreases glycosylphosphatidylinositol phospholipase D synthesis in diabetic animals resulting in decreased serum enzyme levels, suggesting a relationship between this enzyme and the function of insulin.
73	11855934	Insulin reduces serum glycosylphosphatidylinositol phospholipase D levels in human type I diabetic patients and streptozotocin diabetic rats.
74	11855934	The enzyme glycosylphosphatidylinositol phospholipase D has a postulated role in the insulin-mimetic signaling pathway of glycosylphosphatidylinositol compounds.
75	11855934	Insulin therefore decreases glycosylphosphatidylinositol phospholipase D synthesis in diabetic animals resulting in decreased serum enzyme levels, suggesting a relationship between this enzyme and the function of insulin.
76	11855934	Insulin reduces serum glycosylphosphatidylinositol phospholipase D levels in human type I diabetic patients and streptozotocin diabetic rats.
77	11855934	The enzyme glycosylphosphatidylinositol phospholipase D has a postulated role in the insulin-mimetic signaling pathway of glycosylphosphatidylinositol compounds.
78	11855934	Insulin therefore decreases glycosylphosphatidylinositol phospholipase D synthesis in diabetic animals resulting in decreased serum enzyme levels, suggesting a relationship between this enzyme and the function of insulin.
79	12067836	Considerable evidence suggests that atypical protein kinase C isoforms (aPKCs), serving downstream of insulin receptor substrates and phosphatidylinositol (PI) 3-kinase, are required for insulin-stimulated glucose transport in skeletal muscle and adipocytes.
80	12067836	More recent findings further suggest that aPKCs are activated and required for glucose transport responses while serving downstream of 1) proline-rich tyrosine kinase-2, extracellular signal-regulated kinase, and phospholipase D, as during the actions of high concentrations of carbohydrates (glucose, sorbitol) and agents that activate 5'-AMP-activated protein kinase (exercise, 5-amino-imidazole-4-carboxamide-1-beta-D-riboside, dinitrophenol), and 2) Cbl-dependent PI 3-kinase, as during the action of insulin-sensitizing thiazolidinediones.
81	12138107	Oleate and linoleate enhance the growth-promoting effects of insulin-like growth factor-I through a phospholipase D-dependent pathway in arterial smooth muscle cells.
82	12138107	We show that lesions from diabetic pigs fed a cholesterol-rich diet contain abundant insulin-like growth factor-I (IGF-I), in contrast to lesions from non-diabetic pigs.
83	12862207	The changes in ARC and PRC were similar in the control and early-diabetic cells, but greater changes were observed in late-diabetic cells.
84	12862207	In late-diabetic cells, treatment with a phospholipase C inhibitor did not alter the pressure control of ARC or PRC; however, treatment with a phospholipase D inhibitor did inhibit the changes in ARC and PRC with transmural pressure.
85	12941779	S100B-RAGE-mediated augmentation of angiotensin II-induced activation of JAK2 in vascular smooth muscle cells is dependent on PLD2.
86	12941779	We recently found that activation of janus kinase 2 (JAK2) is essential for the Ang II-induced proliferation of vascular smooth muscle cells (VSMCs) and that high glucose augments Ang II-induced proliferation of VSMCs by increasing signal transduction through activation of JAK2.
87	12941779	Here, we demonstrate that S100B, a ligand for the receptor of advanced glycation end products (RAGEs), augmented both Ang II-induced tyrosine phosphorylation of JAK2 and cell proliferation in VSMCs in a receptor-dependent manner.
88	12941779	We also found that S100B-RAGE interaction triggered intracellular generation of reactive oxygen species (ROS), VSMC proliferation, and JAK2 tyrosine phosphorylation via activation of phospholipase D (PLD)2.
89	12941779	These results provide direct evidence for linkages between PLD2, ROS production, and S100B-RAGE-induced enhancement of Ang II-induced cell proliferation and activation of JAK2 in VSMCs.
90	14648804	The role of phospholipase D in Glut-4 translocation.
91	14648804	Insulin-stimulated Glut-4 translocation is regulated through a complex pathway.
92	14648804	Phospholipase D facilitates Glut-4 translocation at potentially multiple steps in its outward movement.
93	14648804	Current investigation is centered on Phospholipase D promotion of Glut-4-containing membrane vesicle trafficking and vesicle fusion into the plasma membrane, in part through activation of atypical protein kinase C isoforms.
94	14648804	The role of phospholipase D in Glut-4 translocation.
95	14648804	Insulin-stimulated Glut-4 translocation is regulated through a complex pathway.
96	14648804	Phospholipase D facilitates Glut-4 translocation at potentially multiple steps in its outward movement.
97	14648804	Current investigation is centered on Phospholipase D promotion of Glut-4-containing membrane vesicle trafficking and vesicle fusion into the plasma membrane, in part through activation of atypical protein kinase C isoforms.
98	14648804	The role of phospholipase D in Glut-4 translocation.
99	14648804	Insulin-stimulated Glut-4 translocation is regulated through a complex pathway.
100	14648804	Phospholipase D facilitates Glut-4 translocation at potentially multiple steps in its outward movement.
101	14648804	Current investigation is centered on Phospholipase D promotion of Glut-4-containing membrane vesicle trafficking and vesicle fusion into the plasma membrane, in part through activation of atypical protein kinase C isoforms.
102	14748713	The lipases involved include arylacetamide deacetylase and/or triacylglycerol hydrolase.
103	14748713	Some, however, are returned to the cytosolic pool in a process that is stimulated by insulin and inhibited by microsomal triacylglycerol transfer protein (MTP).
104	14748713	Phospholipids also contribute to VLDL TAG in a process which involves ADP-ribosylation factor-1 (ARF-1)-mediated activation of phospholipase D.
105	15030177	We studied the activation of Arf, PKC betaI and phospholipase D (PLD) in MCs cultured under normal or high glucose conditions.
106	15030177	MCs cultured in high glucose medium exhibited predominantly cytosolic localization of PKC betaI, Arf3 and Arf6.
107	15030177	However, phorbol ester (PMA) stimulation of cells cultured in high glucose significantly enhanced membrane association of PKC betaI and Arf6, but not Arf3.
108	15194230	Using a highly specific and very sensitive RNase protection assay, we found that the GPI-PLD expressed in adult/post-natal brain, antrum and insulin-producing cells is identical to that isolated from liver.
109	15194230	In addition, GPI-PLD mRNA levels were higher in 4-week old animals compared to older animals, and the GPI-PLD mRNA levels increased in mice that developed insulin dependent type 1 diabetes spontaneously.
110	15194230	Using a highly specific and very sensitive RNase protection assay, we found that the GPI-PLD expressed in adult/post-natal brain, antrum and insulin-producing cells is identical to that isolated from liver.
111	15194230	In addition, GPI-PLD mRNA levels were higher in 4-week old animals compared to older animals, and the GPI-PLD mRNA levels increased in mice that developed insulin dependent type 1 diabetes spontaneously.
112	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
113	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
114	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
115	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
116	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
117	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
118	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
119	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
120	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
121	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
122	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
123	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
124	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
125	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
126	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
127	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
128	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
129	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
130	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
131	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
132	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
133	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
134	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
135	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
136	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
137	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
138	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
139	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
140	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
141	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
142	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
143	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
144	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
145	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
146	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
147	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
148	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
149	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
150	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
151	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
152	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
153	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
154	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
155	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
156	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
157	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
158	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
159	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
160	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
161	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
162	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
163	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
164	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
165	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
166	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
167	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
168	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
169	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
170	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
171	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
172	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
173	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
174	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
175	15259000	Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes.
176	15259000	Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid.
177	15259000	Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD.
178	15259000	In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics.
179	15259000	No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid.
180	15259000	Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro.
181	15259000	GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro.
182	15259000	GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets.
183	15259000	Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes.
184	16118212	Unsaturated fatty acids phosphorylate and destabilize ABCA1 through a phospholipase D2 pathway.
185	16118212	ATP-binding cassette transporter ABCA1 mediates the transport of cholesterol and phospholipids from cells to HDL apolipoproteins and thus modulates HDL levels and atherogenesis.
186	16118212	Unsaturated but not saturated fatty acids stimulated phospholipase D (PLD) activity, the PLD inhibitor 1-butanol prevented the unsaturated fatty acid-induced reduction in ABCA1 levels, and the PLD2 activator mastoparan markedly reduced ABCA1 protein levels, implicating a role for PLD2 in the ABCA1 destabilizing effects of fatty acids.
187	16118212	PLD2 small interfering RNA abolished the ability of unsaturated fatty acids to inhibit lipid transport activity, to reduce protein levels, and to increase serine phosphorylation of ABCA1.
188	16118212	The diacylglycerol analog oleoylacetylglycerol also reduced ABCA1 protein levels and increased its serine phosphorylation, suggesting that PLD2-generated diacylglycerols promote the destabilizing phosphorylation of ABCA1.
189	16118212	These data provide evidence that intracellular unsaturated acyl-CoA derivatives destabilize ABCA1 by activating a PLD2 signaling pathway.
190	16640329	An N(6)-3-iodobenzyl-3'-ureido adenosine derivative 10 activated phospholipase C in COS-7 cells (EC(50) = 0.18 microM) or phospholipase D in chick primary cardiomyocytes, both mediated by a mutant (H272E), but not the wild-type, A(3)AR.
191	17325386	Unsaturated fatty acids phosphorylate and destabilize ABCA1 through a protein kinase C delta pathway.
192	17325386	We previously reported that unsaturated fatty acids destabilize ABCA1 in murine macrophages and ABCA1-transfected baby hamster kidney cells by increasing its serine phosphorylation through a phospholipase D (PLD) pathway.
193	17325386	The protein kinase C delta (PKCdelta)-specific inhibitor rottlerin and PKCdelta small interfering RNA completely abolished the ability of unsaturated fatty acids to inhibit lipid transport activity, to reduce protein levels, and to increase serine phosphorylation of ABCA1, implicating a role for PKCdelta in the ABCA1-destabilizing effects of fatty acids.
194	18561091	Transcriptome studies of endometrial samples recovered during the pre-attachment period identified many interferon-stimulated genes, genes that are possibly involved in embryo-maternal immune modulation ( C1S, C1R, C4, SERPING1, UTMP, CD81, IFITM1, BST2), as well as genes affecting cell adhesion ( AGRN, CD81, LGALS3BP, LGALS9, GPLD1, MFGE8, and TGM2) and remodeling of the endometrium ( CLDN4, MEP1B, LGMN, MMP19, TIMP2, TGM2, MET, and EPSTI1).
195	22001757	We identified 69 candidate genes, including genes involved in biliary transport (ATP8B1 and ABCB11), glucose, carbohydrate and lipid metabolism (FADS1, FADS2, GCKR, JMJD1C, HNF1A, MLXIPL, PNPLA3, PPP1R3B, SLC2A2 and TRIB1), glycoprotein biosynthesis and cell surface glycobiology (ABO, ASGR1, FUT2, GPLD1 and ST3GAL4), inflammation and immunity (CD276, CDH6, GCKR, HNF1A, HPR, ITGA1, RORA and STAT4) and glutathione metabolism (GSTT1, GSTT2 and GGT), as well as several genes of uncertain or unknown function (including ABHD12, EFHD1, EFNA1, EPHA2, MICAL3 and ZNF827).
196	23455471	Among various enzymes involved, phospholipases A1 or A2, phospholipase C, phospholipase D, autotaxin and sphingomyelinase are engaged in membrane lipid remodelling during early stages of mineralization and cell maturation in mineralization-competent cells.