Ignet

Gene Information

Gene symbol: DGKB

Gene name: diacylglycerol kinase, beta 90kDa

HGNC ID: 2850

Synonyms: KIAA0718, DGK, DGK-BETA

Related Genes

#	Gene Symbol	Number of hits
1	ADRA2A	1 hits
2	CAT	1 hits
3	CRY2	1 hits
4	DDHD2	1 hits
5	DGKA	1 hits
6	DGKD	1 hits
7	DGKQ	1 hits
8	EGF	1 hits
9	F2	1 hits
10	FADS1	1 hits
11	G6PC2	1 hits
12	GCK	1 hits
13	GIPR	1 hits
14	GLIS3	1 hits
15	IGF1	1 hits
16	INS	1 hits
17	IRS1	1 hits
18	MADD	1 hits
19	MTNR1B	1 hits
20	PDGFA	1 hits
21	PLCB1	1 hits
22	PPARG	1 hits
23	PRKCA	1 hits
24	PROX1	1 hits
25	SLC2A2	1 hits
26	SLC30A8	1 hits
27	TCF7L2	1 hits
28	TMEM195	1 hits

Related Sentences

#	PMID	Sentence
1	11415460	We have previously shown that unsaturated fatty acids amplify platelet-derived-growth-factor (PDGF)-induced protein kinase C (PKC) activation in vascular smooth-muscle cells (VSMCs).
2	11415460	Fractionation of VSMC extracts demonstrated that the DGK alpha isoform was the major DGK activity present.
3	11415460	PDGF markedly increased the DGK activity of cultured cells.
4	11415460	An inhibitor selective for the DGK alpha isoform, R59949 [3-[2-[4-(bis-(4-fluorophenyl)methylene]piperidin-1-yl)ethyl]-2,3-dihydro-2-thioxo-4(1H)-quinazolinone], abolished the growth-factor-induced increase in DGK activity, but had little effect on basal activity.
5	11415460	PDGF thus selectively activates DGKalpha.
6	11415460	Epidermal growth factor and alpha-thrombin stimulated total DGK activity similarly to PDGF.
7	11415460	Activation by epidermal growth factor was sensitive to R59949, again suggesting involvement of DGKalpha.
8	11415460	We have previously shown that unsaturated fatty acids amplify platelet-derived-growth-factor (PDGF)-induced protein kinase C (PKC) activation in vascular smooth-muscle cells (VSMCs).
9	11415460	Fractionation of VSMC extracts demonstrated that the DGK alpha isoform was the major DGK activity present.
10	11415460	PDGF markedly increased the DGK activity of cultured cells.
11	11415460	An inhibitor selective for the DGK alpha isoform, R59949 [3-[2-[4-(bis-(4-fluorophenyl)methylene]piperidin-1-yl)ethyl]-2,3-dihydro-2-thioxo-4(1H)-quinazolinone], abolished the growth-factor-induced increase in DGK activity, but had little effect on basal activity.
12	11415460	PDGF thus selectively activates DGKalpha.
13	11415460	Epidermal growth factor and alpha-thrombin stimulated total DGK activity similarly to PDGF.
14	11415460	Activation by epidermal growth factor was sensitive to R59949, again suggesting involvement of DGKalpha.
15	11415460	We have previously shown that unsaturated fatty acids amplify platelet-derived-growth-factor (PDGF)-induced protein kinase C (PKC) activation in vascular smooth-muscle cells (VSMCs).
16	11415460	Fractionation of VSMC extracts demonstrated that the DGK alpha isoform was the major DGK activity present.
17	11415460	PDGF markedly increased the DGK activity of cultured cells.
18	11415460	An inhibitor selective for the DGK alpha isoform, R59949 [3-[2-[4-(bis-(4-fluorophenyl)methylene]piperidin-1-yl)ethyl]-2,3-dihydro-2-thioxo-4(1H)-quinazolinone], abolished the growth-factor-induced increase in DGK activity, but had little effect on basal activity.
19	11415460	PDGF thus selectively activates DGKalpha.
20	11415460	Epidermal growth factor and alpha-thrombin stimulated total DGK activity similarly to PDGF.
21	11415460	Activation by epidermal growth factor was sensitive to R59949, again suggesting involvement of DGKalpha.
22	11415460	We have previously shown that unsaturated fatty acids amplify platelet-derived-growth-factor (PDGF)-induced protein kinase C (PKC) activation in vascular smooth-muscle cells (VSMCs).
23	11415460	Fractionation of VSMC extracts demonstrated that the DGK alpha isoform was the major DGK activity present.
24	11415460	PDGF markedly increased the DGK activity of cultured cells.
25	11415460	An inhibitor selective for the DGK alpha isoform, R59949 [3-[2-[4-(bis-(4-fluorophenyl)methylene]piperidin-1-yl)ethyl]-2,3-dihydro-2-thioxo-4(1H)-quinazolinone], abolished the growth-factor-induced increase in DGK activity, but had little effect on basal activity.
26	11415460	PDGF thus selectively activates DGKalpha.
27	11415460	Epidermal growth factor and alpha-thrombin stimulated total DGK activity similarly to PDGF.
28	11415460	Activation by epidermal growth factor was sensitive to R59949, again suggesting involvement of DGKalpha.
29	15117825	PPARgamma agonists ameliorate endothelial cell activation via inhibition of diacylglycerol-protein kinase C signaling pathway: role of diacylglycerol kinase.
30	15117825	Subject- Peroxisome proliferator-activated receptor (PPAR)-gamma agonists are emerging as potential protectors against inflammatory cardiovascular diseases including atherosclerosis and diabetic complications.
31	15117825	We report here that PPARgamma agonists, thiazolidinedione class drugs (TZDs), or 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2) were capable of activating diacylglycerol (DAG) kinase (DGK), resulting in attenuation of DAG levels and inhibition of protein kinase C (PKC) activation.
32	15117825	The PPARgamma agonist-induced DGK was completely blocked by a dominant-negative mutant of PPARgamma, indicating an essential receptor-dependent action.
33	15117825	These findings thus demonstrate a novel molecular action of PPARgamma agonists to suppress the DAG-PKC signaling pathway via upregulation of an endogenous attenuator, DGK.
34	15117825	PPARgamma agonists ameliorate endothelial cell activation via inhibition of diacylglycerol-protein kinase C signaling pathway: role of diacylglycerol kinase.
35	15117825	Subject- Peroxisome proliferator-activated receptor (PPAR)-gamma agonists are emerging as potential protectors against inflammatory cardiovascular diseases including atherosclerosis and diabetic complications.
36	15117825	We report here that PPARgamma agonists, thiazolidinedione class drugs (TZDs), or 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2) were capable of activating diacylglycerol (DAG) kinase (DGK), resulting in attenuation of DAG levels and inhibition of protein kinase C (PKC) activation.
37	15117825	The PPARgamma agonist-induced DGK was completely blocked by a dominant-negative mutant of PPARgamma, indicating an essential receptor-dependent action.
38	15117825	These findings thus demonstrate a novel molecular action of PPARgamma agonists to suppress the DAG-PKC signaling pathway via upregulation of an endogenous attenuator, DGK.
39	15117825	PPARgamma agonists ameliorate endothelial cell activation via inhibition of diacylglycerol-protein kinase C signaling pathway: role of diacylglycerol kinase.
40	15117825	Subject- Peroxisome proliferator-activated receptor (PPAR)-gamma agonists are emerging as potential protectors against inflammatory cardiovascular diseases including atherosclerosis and diabetic complications.
41	15117825	We report here that PPARgamma agonists, thiazolidinedione class drugs (TZDs), or 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2) were capable of activating diacylglycerol (DAG) kinase (DGK), resulting in attenuation of DAG levels and inhibition of protein kinase C (PKC) activation.
42	15117825	The PPARgamma agonist-induced DGK was completely blocked by a dominant-negative mutant of PPARgamma, indicating an essential receptor-dependent action.
43	15117825	These findings thus demonstrate a novel molecular action of PPARgamma agonists to suppress the DAG-PKC signaling pathway via upregulation of an endogenous attenuator, DGK.
44	15315262	The present study demonstrated that diacylglycerol kinase (DGK) activity in diabetic gastric smooth muscle in the resting state was approximately 3.5-fold greater than that in controls.
45	15315262	However, oral administration of TJ-43 (1% of food intake) or subcutaneous insulin injection (12 units/kg/day) in streptozotocin-induced diabetic rats (DM) for 2 weeks prevented DGK abnormalities based on the control level.
46	15315262	Increased DGK activity in the resting state of DM was inhibited significantly by R59022, neomycin or staurosporine; in contrast, these drugs did not affect DGK activity in controls, insulin-treated DM or TJ-43-treated DM.
47	15315262	Results suggested that TJ-43 treatment influenced the hyperreactivity of DGK and DAG formation via phospholipase C activity.
48	15315262	The present study demonstrated that diacylglycerol kinase (DGK) activity in diabetic gastric smooth muscle in the resting state was approximately 3.5-fold greater than that in controls.
49	15315262	However, oral administration of TJ-43 (1% of food intake) or subcutaneous insulin injection (12 units/kg/day) in streptozotocin-induced diabetic rats (DM) for 2 weeks prevented DGK abnormalities based on the control level.
50	15315262	Increased DGK activity in the resting state of DM was inhibited significantly by R59022, neomycin or staurosporine; in contrast, these drugs did not affect DGK activity in controls, insulin-treated DM or TJ-43-treated DM.
51	15315262	Results suggested that TJ-43 treatment influenced the hyperreactivity of DGK and DAG formation via phospholipase C activity.
52	15315262	The present study demonstrated that diacylglycerol kinase (DGK) activity in diabetic gastric smooth muscle in the resting state was approximately 3.5-fold greater than that in controls.
53	15315262	However, oral administration of TJ-43 (1% of food intake) or subcutaneous insulin injection (12 units/kg/day) in streptozotocin-induced diabetic rats (DM) for 2 weeks prevented DGK abnormalities based on the control level.
54	15315262	Increased DGK activity in the resting state of DM was inhibited significantly by R59022, neomycin or staurosporine; in contrast, these drugs did not affect DGK activity in controls, insulin-treated DM or TJ-43-treated DM.
55	15315262	Results suggested that TJ-43 treatment influenced the hyperreactivity of DGK and DAG formation via phospholipase C activity.
56	15315262	The present study demonstrated that diacylglycerol kinase (DGK) activity in diabetic gastric smooth muscle in the resting state was approximately 3.5-fold greater than that in controls.
57	15315262	However, oral administration of TJ-43 (1% of food intake) or subcutaneous insulin injection (12 units/kg/day) in streptozotocin-induced diabetic rats (DM) for 2 weeks prevented DGK abnormalities based on the control level.
58	15315262	Increased DGK activity in the resting state of DM was inhibited significantly by R59022, neomycin or staurosporine; in contrast, these drugs did not affect DGK activity in controls, insulin-treated DM or TJ-43-treated DM.
59	15315262	Results suggested that TJ-43 treatment influenced the hyperreactivity of DGK and DAG formation via phospholipase C activity.
60	18267070	Downregulation of diacylglycerol kinase delta contributes to hyperglycemia-induced insulin resistance.
61	18267070	We identified reduced diacylglycerol kinase delta (DGKdelta) expression and DGK activity in skeletal muscle from type 2 diabetic patients.
62	18267070	In diabetic animals, reduced DGKdelta protein and DGK kinase activity were restored upon correction of glycemia.
63	18267070	DGKdelta haploinsufficiency increased diacylglycerol content, reduced peripheral insulin sensitivity, insulin signaling, and glucose transport, and led to age-dependent obesity.
64	18267070	We reveal a previously unrecognized role for DGKdelta in contributing to hyperglycemia-induced peripheral insulin resistance and thereby exacerbating the severity of type 2 diabetes.
65	18267070	DGKdelta deficiency causes peripheral insulin resistance and metabolic inflexibility.
66	18267070	Downregulation of diacylglycerol kinase delta contributes to hyperglycemia-induced insulin resistance.
67	18267070	We identified reduced diacylglycerol kinase delta (DGKdelta) expression and DGK activity in skeletal muscle from type 2 diabetic patients.
68	18267070	In diabetic animals, reduced DGKdelta protein and DGK kinase activity were restored upon correction of glycemia.
69	18267070	DGKdelta haploinsufficiency increased diacylglycerol content, reduced peripheral insulin sensitivity, insulin signaling, and glucose transport, and led to age-dependent obesity.
70	18267070	We reveal a previously unrecognized role for DGKdelta in contributing to hyperglycemia-induced peripheral insulin resistance and thereby exacerbating the severity of type 2 diabetes.
71	18267070	DGKdelta deficiency causes peripheral insulin resistance and metabolic inflexibility.
72	20185807	Defects in insulin processing and insulin secretion were seen in glucose-raising allele carriers at TCF7L2, SCL30A8, GIPR, and C2CD4B.
73	20185807	Abnormalities in early insulin secretion were suggested in glucose-raising allele carriers at MTNR1B, GCK, FADS1, DGKB, and PROX1 (lower insulinogenic index; no association with proinsulin or insulin sensitivity).
74	20185807	Two loci previously associated with fasting insulin (GCKR and IGF1) were associated with OGTT-derived insulin sensitivity indices in a consistent direction.
75	20419449	Variants at DGKB/TMEM195, ADRA2A, GLIS3 and C2CD4B loci are associated with reduced glucose-stimulated beta cell function in middle-aged Danish people.
76	21103350	Variants from GIPR, TCF7L2, DGKB, MADD, CRY2, GLIS3, PROX1, SLC30A8 and IGF1 are associated with glucose metabolism in the Chinese.
77	21725595	We previously reported that d-α-tocopherol, well known as an antioxidant, enhances diacylglycerol kinase (DGK) activity, leading to the reduction of excess DAG accumulation and PKC activation in the glomeruli of streptozotocin-induced diabetic rats.
78	21725595	Mesangial cells were exposed to hydrogen peroxide (H2O2) (10-1000 μM) in the presence or absence of 300 U/ml catalase, followed by measurement of DGK activity.
79	21725595	The addition of antioxidative enzyme catalase to the cells reversed the H2O2-mediated down-regulation of DGK activity.
80	21725595	We previously reported that d-α-tocopherol, well known as an antioxidant, enhances diacylglycerol kinase (DGK) activity, leading to the reduction of excess DAG accumulation and PKC activation in the glomeruli of streptozotocin-induced diabetic rats.
81	21725595	Mesangial cells were exposed to hydrogen peroxide (H2O2) (10-1000 μM) in the presence or absence of 300 U/ml catalase, followed by measurement of DGK activity.
82	21725595	The addition of antioxidative enzyme catalase to the cells reversed the H2O2-mediated down-regulation of DGK activity.
83	21725595	We previously reported that d-α-tocopherol, well known as an antioxidant, enhances diacylglycerol kinase (DGK) activity, leading to the reduction of excess DAG accumulation and PKC activation in the glomeruli of streptozotocin-induced diabetic rats.
84	21725595	Mesangial cells were exposed to hydrogen peroxide (H2O2) (10-1000 μM) in the presence or absence of 300 U/ml catalase, followed by measurement of DGK activity.
85	21725595	The addition of antioxidative enzyme catalase to the cells reversed the H2O2-mediated down-regulation of DGK activity.
86	22974639	The type II diacylglycerol kinases (DGKs) contain several functional domains such as a pleckstrin homology (PH) domain, two C1 domains and a sterile α-motif (SAM) domain.
87	22974639	Moreover, a high extracellular concentration of glucose activated DGKδ in skeletal muscle cells, which was followed by a reduction in the intracellular diacylglycerol levels and the inactivation of protein kinase Cα, the enzyme that phosphorylates and inactivates the insulin receptor.
88	22984004	Diacylglycerol kinase (DGK) phosphorylates diacylglycerol (DAG) to produce phosphatidic acid (PA) and plays an important role in signal transduction by modulating the balance between these signalling lipids.
89	22984506	We genotyped previously reported polymorphisms (or their proxies) in/near G6PC2, MTNR1B, GCK, DGKB, GCKR, ADCY5, MADD, CRY2, ADRA2A, FADS1, PROX1, SLC2A2, GLIS3, C2CD4B, IGF1, and IRS1 in 3,548 Diabetes Prevention Program participants.