Ignet

Gene Information

Gene symbol: PRKAA1

Gene name: protein kinase, AMP-activated, alpha 1 catalytic subunit

HGNC ID: 9376

Synonyms: AMPKa1

Related Genes

#	Gene Symbol	Number of hits
1	ACACA	1 hits
2	ACACB	1 hits
3	ADIPOQ	1 hits
4	ADIPOR1	1 hits
5	ADIPOR2	1 hits
6	AGT	1 hits
7	AHSG	1 hits
8	ATIC	1 hits
9	BCAR1	1 hits
10	BCL2	1 hits
11	CAMKK2	1 hits
12	CARM1	1 hits
13	CCL26	1 hits
14	CD36	1 hits
15	CFTR	1 hits
16	CNR1	1 hits
17	CPT1A	1 hits
18	FUNDC1	1 hits
19	H6PD	1 hits
20	HIF1A	1 hits
21	IL17A	1 hits
22	INS	1 hits
23	MAFK	1 hits
24	MAP1LC3A	1 hits
25	MAP3K5	1 hits
26	MAPK1	1 hits
27	MARCH8	1 hits
28	NFE2L2	1 hits
29	NOS2A	1 hits
30	NOS3	1 hits
31	NOTCH1	1 hits
32	NOX4	1 hits
33	NOX5	1 hits
34	NPHS1	1 hits
35	NPHS2	1 hits
36	NRF1	1 hits
37	PPARA	1 hits
38	PPARGC1A	1 hits
39	PRKAA2	1 hits
40	PRKAR1A	1 hits
41	PRKD1	1 hits
42	SETD2	1 hits
43	SIRT1	1 hits
44	SIRT3	1 hits
45	SLC12A1	1 hits
46	STAT3	1 hits
47	STK11	1 hits
48	SYNPO	1 hits
49	TP53	1 hits
50	TRPV1	1 hits
51	TSC1	1 hits
52	TSC2	1 hits
53	TXN	1 hits
54	TXNIP	1 hits
55	ULK1	1 hits
56	VASP	1 hits

Related Sentences

#	PMID	Sentence
1	35069849	Gastrodin inhibits high glucose-induced inflammation, oxidative stress and apoptosis in podocytes by activating the AMPK/Nrf2 signaling pathway.
2	35069849	Gastrodin inhibits high glucose-induced inflammation, oxidative stress and apoptosis in podocytes by activating the AMPK/Nrf2 signaling pathway.
3	35069849	Gastrodin inhibits high glucose-induced inflammation, oxidative stress and apoptosis in podocytes by activating the AMPK/Nrf2 signaling pathway.
4	35069849	Gastrodin inhibits high glucose-induced inflammation, oxidative stress and apoptosis in podocytes by activating the AMPK/Nrf2 signaling pathway.
5	35069849	Cell viability was evaluated using Cell Counting Kit-8 assay and secretion levels of TNF-α, IL-1β and IL-6 were measured using ELISA.
6	35069849	Cell viability was evaluated using Cell Counting Kit-8 assay and secretion levels of TNF-α, IL-1β and IL-6 were measured using ELISA.
7	35069849	Cell viability was evaluated using Cell Counting Kit-8 assay and secretion levels of TNF-α, IL-1β and IL-6 were measured using ELISA.
8	35069849	Cell viability was evaluated using Cell Counting Kit-8 assay and secretion levels of TNF-α, IL-1β and IL-6 were measured using ELISA.
9	35069849	Additionally, cell apoptosis was analyzed by TUNEL assay, whilst protein expressions related to inflammation, apoptosis and the 5'-AMP-activated protein kinase (AMPK)/nuclear factor erythroid 2-related factor 2 (Nrf2) signaling pathway were measured by western blot analysis.
10	35069849	Additionally, cell apoptosis was analyzed by TUNEL assay, whilst protein expressions related to inflammation, apoptosis and the 5'-AMP-activated protein kinase (AMPK)/nuclear factor erythroid 2-related factor 2 (Nrf2) signaling pathway were measured by western blot analysis.
11	35069849	Additionally, cell apoptosis was analyzed by TUNEL assay, whilst protein expressions related to inflammation, apoptosis and the 5'-AMP-activated protein kinase (AMPK)/nuclear factor erythroid 2-related factor 2 (Nrf2) signaling pathway were measured by western blot analysis.
12	35069849	Additionally, cell apoptosis was analyzed by TUNEL assay, whilst protein expressions related to inflammation, apoptosis and the 5'-AMP-activated protein kinase (AMPK)/nuclear factor erythroid 2-related factor 2 (Nrf2) signaling pathway were measured by western blot analysis.
13	35069849	Furthermore, gastrodin promoted activation of the AMPK/Nrf2 pathway in MPC5 cells.
14	35069849	Furthermore, gastrodin promoted activation of the AMPK/Nrf2 pathway in MPC5 cells.
15	35069849	Furthermore, gastrodin promoted activation of the AMPK/Nrf2 pathway in MPC5 cells.
16	35069849	Furthermore, gastrodin promoted activation of the AMPK/Nrf2 pathway in MPC5 cells.
17	35069849	To conclude, treatment of MPC5 cells with gastrodin can attenuate HG-induced inflammation, oxidative stress and cell apoptosis by activating the AMPK/Nrf2 signaling pathway.
18	35069849	To conclude, treatment of MPC5 cells with gastrodin can attenuate HG-induced inflammation, oxidative stress and cell apoptosis by activating the AMPK/Nrf2 signaling pathway.
19	35069849	To conclude, treatment of MPC5 cells with gastrodin can attenuate HG-induced inflammation, oxidative stress and cell apoptosis by activating the AMPK/Nrf2 signaling pathway.
20	35069849	To conclude, treatment of MPC5 cells with gastrodin can attenuate HG-induced inflammation, oxidative stress and cell apoptosis by activating the AMPK/Nrf2 signaling pathway.
21	34974186	Various key findings in podocyte autophagy were reported in the past ten years, such as the role of endoplasmic reticulum (ER) stress in podocyte autophagy impairment, podocyte autophagy-related gene, essential roles of the signaling pathways: Mammalian Target of Rapamycin (mTOR)/ Phosphoinositide 3-kinase (PI3k)/ serine/threonine kinase 1 (Akt) in podocyte autophagy.
22	34974186	Sirtuin-1 was reported to have a vital key role in mTOR signaling, 5'AMP-activated protein kinase (AMPK) regulation, autophagy activation, and various critical pathways associated with podocyte's function and health; it has potential value to podocyte injury pathogenesis investigation.
23	33897448	Silencing of miR-150-5p Ameliorates Diabetic Nephropathy by Targeting SIRT1/p53/AMPK Pathway.
24	33897448	Importantly, we found that the silencing of miR-150-5p promoted the interaction between SIRT1 and p53, causing the suppression of p53 acetylation in podocytes and kidney tissue.
25	33459165	We determined that NIC binding to podocytes in concentrations achieved with CS and ECs activated NADPH oxidase, which sets in motion a dysfunctional molecular network integrated by cyclooxygenase 2, known to induce podocyte injury; downregulation of AMP-activated protein kinase, important for maintaining cellular energy stores and antioxidation; and upregulation of CD36, which increased lipid uptake and promoted apoptosis.
26	33459165	We determined that NIC binding to podocytes in concentrations achieved with CS and ECs activated NADPH oxidase, which sets in motion a dysfunctional molecular network integrated by cyclooxygenase 2, known to induce podocyte injury; downregulation of AMP-activated protein kinase, important for maintaining cellular energy stores and antioxidation; and upregulation of CD36, which increased lipid uptake and promoted apoptosis.
27	33459165	NEW & NOTEWORTHY In this study, we demonstrate that nicotine increases the production of reactive oxygen species, increases cyclooxygenase-2 expression, and upregulates Cd36 while inducing downregulation of AMP-activated protein kinase.
28	33459165	NEW & NOTEWORTHY In this study, we demonstrate that nicotine increases the production of reactive oxygen species, increases cyclooxygenase-2 expression, and upregulates Cd36 while inducing downregulation of AMP-activated protein kinase.
29	32997989	In addition, blocking NAPDH synthesis by knocking down H6PD mimicked the beneficial role of RYGB surgery through activation of AMPK in podocytes.
30	32781053	AMPK participates in insulin signaling, therefore controls glucose uptake and podocytes insulin sensitivity.
31	32781053	It is also involved in insulin-dependent cytoskeleton reorganization in podocytes, mediating glomerular albumin permeability.
32	32276962	The primary drivers of autophagy in states of nutrient and oxygen deprivation-sirtuin-1 (SIRT1), AMP-activated protein kinase (AMPK), and hypoxia-inducible factors (HIF-1α and HIF-2α)-can exert renoprotective effects by promoting autophagic flux and by exerting direct effects on sodium transport and inflammasome activation.
33	32276962	The primary drivers of autophagy in states of nutrient and oxygen deprivation-sirtuin-1 (SIRT1), AMP-activated protein kinase (AMPK), and hypoxia-inducible factors (HIF-1α and HIF-2α)-can exert renoprotective effects by promoting autophagic flux and by exerting direct effects on sodium transport and inflammasome activation.
34	32276962	Type 2 diabetes is characterized by marked suppression of SIRT1 and AMPK, leading to a diminution in autophagic flux in glomerular podocytes and renal tubules and markedly increasing their susceptibility to renal injury.
35	32276962	Type 2 diabetes is characterized by marked suppression of SIRT1 and AMPK, leading to a diminution in autophagic flux in glomerular podocytes and renal tubules and markedly increasing their susceptibility to renal injury.
36	32276962	In contrast, the effects of sodium-glucose cotransporter-2 (SGLT2) inhibitors may be related primarily to enhanced SIRT1 and HIF-2α signaling; this can explain the effects of SGLT2 inhibitors to promote ketonemia and erythrocytosis and potentially underlies their actions to increase autophagy and mute inflammation in the diabetic kidney.
37	32276962	In contrast, the effects of sodium-glucose cotransporter-2 (SGLT2) inhibitors may be related primarily to enhanced SIRT1 and HIF-2α signaling; this can explain the effects of SGLT2 inhibitors to promote ketonemia and erythrocytosis and potentially underlies their actions to increase autophagy and mute inflammation in the diabetic kidney.
38	32061660	Mechanistically, TRPV1-mediated transient Ca²⁺ influx activated 5' AMP-activated protein kinase (AMPK) that reduced the transcription of Fundc1, a key molecule participating in MAMs formation.
39	32061660	Mechanistically, TRPV1-mediated transient Ca²⁺ influx activated 5' AMP-activated protein kinase (AMPK) that reduced the transcription of Fundc1, a key molecule participating in MAMs formation.
40	32061660	Inhibition of AMPK or overexpression of Fundc1 obviously blocked the inhibitory effect of capsaicin on MAMs formation and functional decline in podocytes.
41	32061660	Inhibition of AMPK or overexpression of Fundc1 obviously blocked the inhibitory effect of capsaicin on MAMs formation and functional decline in podocytes.
42	31865844	Instead we present data showing that autophagy in podocytes is mainly controlled by AMP-activated protein kinase (AMPK) and ULK1 (unc-51 like kinase 1).
43	31865844	Instead we present data showing that autophagy in podocytes is mainly controlled by AMP-activated protein kinase (AMPK) and ULK1 (unc-51 like kinase 1).
44	31865844	Abbreviations: AICAR: 5-aminoimidazole-4-carboxamide ribonucleotide; AMPK: AMP-activated protein kinase; ATG: autophagy related; BW: body weight; Cq: chloroquine; ER: endoplasmic reticulum; ESRD: end stage renal disease; FACS: fluorescence activated cell sorting; GFP: green fluorescent protein; i.p.: intra peritoneal; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; MTOR: mechanistic target of rapamycin kinase; NPHS1: nephrosis 1, nephrin; NPHS2: nephrosis 2, podocin; PLA: proximity-ligation assay; PRKAA: 5'-AMP-activated protein kinase catalytic subunit alpha; RPTOR/RAPTOR: regulatory associated protein of MTOR, complex 1; RFP: red fluorescent protein; TSC1: tuberous sclerosis 1; ULK1: unc-51 like kinase 1.
45	31865844	Abbreviations: AICAR: 5-aminoimidazole-4-carboxamide ribonucleotide; AMPK: AMP-activated protein kinase; ATG: autophagy related; BW: body weight; Cq: chloroquine; ER: endoplasmic reticulum; ESRD: end stage renal disease; FACS: fluorescence activated cell sorting; GFP: green fluorescent protein; i.p.: intra peritoneal; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; MTOR: mechanistic target of rapamycin kinase; NPHS1: nephrosis 1, nephrin; NPHS2: nephrosis 2, podocin; PLA: proximity-ligation assay; PRKAA: 5'-AMP-activated protein kinase catalytic subunit alpha; RPTOR/RAPTOR: regulatory associated protein of MTOR, complex 1; RFP: red fluorescent protein; TSC1: tuberous sclerosis 1; ULK1: unc-51 like kinase 1.
46	30968998	Vasodilator-stimulated phosphoprotein (VASP) is a 39-kDa protein belonging to the Ena/VASP protein family, which is involved in adhesion, migration, cell-cell interaction, and regulation of pathways connected with actin cytoskeleton remodeling.
47	30968998	VASP is phosphorylated at Tyr39, Ser157, Ser239, Thr278, and Ser322 mainly by tyrosine kinase Abl, cAMP-dependent protein kinase, protein kinase G, AMP-activated protein kinase, and protein kinase D1, respectively.
48	29449563	In cultured HGECs and podocytes, cinacalcet decreased oxidative stress and apoptosis and increased autophagy that were attributed to the increment of intracellular Ca²⁺ concentration and the phosphorylation of Ca²⁺/calmodulin-dependent protein kinase kinaseβ (CaMKKβ)-Liver kinase B1 (LKB1)-AMPK and their downstream signals including the phosphorylation of endothelial nitric oxide synthase (eNOS) and increases in superoxide dismutases and B cell leukemia/lymphoma 2/BCL-2-associated X protein expression.
49	29449563	In cultured HGECs and podocytes, cinacalcet decreased oxidative stress and apoptosis and increased autophagy that were attributed to the increment of intracellular Ca²⁺ concentration and the phosphorylation of Ca²⁺/calmodulin-dependent protein kinase kinaseβ (CaMKKβ)-Liver kinase B1 (LKB1)-AMPK and their downstream signals including the phosphorylation of endothelial nitric oxide synthase (eNOS) and increases in superoxide dismutases and B cell leukemia/lymphoma 2/BCL-2-associated X protein expression.
50	29449563	Subsequent activation of AMPK was followed by the activation of peroxisome proliferator-activated receptor γ coactivator-1α and phospho-Ser¹¹⁷⁷eNOS-nitric oxide, resulting in a decrease in apoptosis and oxidative stress as well as an increase in autophagy.Our results suggest that cinacalcet increases intracellular Ca²⁺ followed by an activation of CaMKKβ-LKB1-AMPK signaling in GECs and podocytes in the kidney, which provides a novel therapeutic means for type 2 diabetic nephropathy by modulation of apoptosis and autophagy.
51	29449563	Subsequent activation of AMPK was followed by the activation of peroxisome proliferator-activated receptor γ coactivator-1α and phospho-Ser¹¹⁷⁷eNOS-nitric oxide, resulting in a decrease in apoptosis and oxidative stress as well as an increase in autophagy.Our results suggest that cinacalcet increases intracellular Ca²⁺ followed by an activation of CaMKKβ-LKB1-AMPK signaling in GECs and podocytes in the kidney, which provides a novel therapeutic means for type 2 diabetic nephropathy by modulation of apoptosis and autophagy.
52	29330340	Adiponectin exerts renoprotective effects against diabetic nephropathy (DN) by activating the AMP-activated protein kinase (AMPK)/peroxisome proliferative-activated receptor-α (PPARα) pathway through adiponectin receptors (AdipoRs).
53	29330340	Adiponectin exerts renoprotective effects against diabetic nephropathy (DN) by activating the AMP-activated protein kinase (AMPK)/peroxisome proliferative-activated receptor-α (PPARα) pathway through adiponectin receptors (AdipoRs).
54	29330340	Adiponectin exerts renoprotective effects against diabetic nephropathy (DN) by activating the AMP-activated protein kinase (AMPK)/peroxisome proliferative-activated receptor-α (PPARα) pathway through adiponectin receptors (AdipoRs).
55	29330340	Adiponectin exerts renoprotective effects against diabetic nephropathy (DN) by activating the AMP-activated protein kinase (AMPK)/peroxisome proliferative-activated receptor-α (PPARα) pathway through adiponectin receptors (AdipoRs).
56	29330340	Expression of AdipoR1, AdipoR2, and Ca²⁺/calmodulin-dependent protein kinase kinase-β (CaMKKβ) and numbers of phosphorylated liver kinase B1 (LKB1)- and AMPK-positive cells significantly decreased in the glomeruli of early stage human DN.
57	29330340	Expression of AdipoR1, AdipoR2, and Ca²⁺/calmodulin-dependent protein kinase kinase-β (CaMKKβ) and numbers of phosphorylated liver kinase B1 (LKB1)- and AMPK-positive cells significantly decreased in the glomeruli of early stage human DN.
58	29330340	Expression of AdipoR1, AdipoR2, and Ca²⁺/calmodulin-dependent protein kinase kinase-β (CaMKKβ) and numbers of phosphorylated liver kinase B1 (LKB1)- and AMPK-positive cells significantly decreased in the glomeruli of early stage human DN.
59	29330340	Expression of AdipoR1, AdipoR2, and Ca²⁺/calmodulin-dependent protein kinase kinase-β (CaMKKβ) and numbers of phosphorylated liver kinase B1 (LKB1)- and AMPK-positive cells significantly decreased in the glomeruli of early stage human DN.
60	29330340	AdipoRon exerted renoprotective effects by directly activating intrarenal AdipoR1 and AdipoR2, which increased CaMKKβ, phosphorylated Ser⁴³¹LKB1, phosphorylated Thr¹⁷²AMPK, and PPARα expression independently of the systemic effects of adiponectin.
61	29330340	AdipoRon exerted renoprotective effects by directly activating intrarenal AdipoR1 and AdipoR2, which increased CaMKKβ, phosphorylated Ser⁴³¹LKB1, phosphorylated Thr¹⁷²AMPK, and PPARα expression independently of the systemic effects of adiponectin.
62	29330340	AdipoRon exerted renoprotective effects by directly activating intrarenal AdipoR1 and AdipoR2, which increased CaMKKβ, phosphorylated Ser⁴³¹LKB1, phosphorylated Thr¹⁷²AMPK, and PPARα expression independently of the systemic effects of adiponectin.
63	29330340	AdipoRon exerted renoprotective effects by directly activating intrarenal AdipoR1 and AdipoR2, which increased CaMKKβ, phosphorylated Ser⁴³¹LKB1, phosphorylated Thr¹⁷²AMPK, and PPARα expression independently of the systemic effects of adiponectin.
64	29330340	In high-glucose-treated human GECs and murine podocytes, AdipoRon increased intracellular Ca²⁺ levels that activated a CaMKKβ/phosphorylated Ser⁴³¹LKB1/phosphorylated Thr¹⁷²AMPK/PPARα pathway and downstream signaling, thus decreasing high-glucose-induced oxidative stress and apoptosis and improving endothelial dysfunction.
65	29330340	In high-glucose-treated human GECs and murine podocytes, AdipoRon increased intracellular Ca²⁺ levels that activated a CaMKKβ/phosphorylated Ser⁴³¹LKB1/phosphorylated Thr¹⁷²AMPK/PPARα pathway and downstream signaling, thus decreasing high-glucose-induced oxidative stress and apoptosis and improving endothelial dysfunction.
66	29330340	In high-glucose-treated human GECs and murine podocytes, AdipoRon increased intracellular Ca²⁺ levels that activated a CaMKKβ/phosphorylated Ser⁴³¹LKB1/phosphorylated Thr¹⁷²AMPK/PPARα pathway and downstream signaling, thus decreasing high-glucose-induced oxidative stress and apoptosis and improving endothelial dysfunction.
67	29330340	In high-glucose-treated human GECs and murine podocytes, AdipoRon increased intracellular Ca²⁺ levels that activated a CaMKKβ/phosphorylated Ser⁴³¹LKB1/phosphorylated Thr¹⁷²AMPK/PPARα pathway and downstream signaling, thus decreasing high-glucose-induced oxidative stress and apoptosis and improving endothelial dysfunction.
68	29175208	A single nucleotide polymorphism (SNP) within the acetyl CoA carboxylase (ACC) β gene (ACACB), rs2268388, has been shown to be associated with susceptibility to development of proteinuria in patients with type 2 diabetes.
69	29175208	In STZ-induced diabetic mice, ACACB-transgenic mice showed a significant increase in urinary albumin excretion, accompanied by decreased synaptopodin expression and podocin mislocalization in podocytes, compared with wild-type mice.
70	29175208	In cultured murine podocytes, overexpression of ACACB significantly decreased synaptopodin expression and reorganized stress fibers under high glucose conditions, but not in normal glucose conditions.
71	29175208	The decrease of synaptopodin expression and reorganized stress fibers observed in ACACB overexpressing cells cultured under high glucose conditions was reversed by a treatment of 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranoside (AICAR), activator of AMP-activated protein kinase (AMPK).
72	29089371	FXR/TGR5 Dual Agonist Prevents Progression of Nephropathy in Diabetes and Obesity.
73	29089371	Bile acids are ligands for the nuclear hormone receptor farnesoid X receptor (FXR) and the G protein-coupled receptor TGR5.
74	29089371	We have shown that FXR and TGR5 have renoprotective roles in diabetes- and obesity-related kidney disease.
75	29089371	We administered the FXR/TGR5 dual agonist INT-767 to DBA/2J mice with streptozotocin-induced diabetes, db/db mice with type 2 diabetes, and C57BL/6J mice with high-fat diet-induced obesity.
76	29089371	We also examined the individual effects of the selective FXR agonist obeticholic acid (OCA) and the TGR5 agonist INT-777 in diabetic mice.
77	29089371	The FXR agonist OCA and the TGR5 agonist INT-777 modulated distinct renal signaling pathways involved in the pathogenesis and treatment of diabetic nephropathy.
78	29089371	Treatment of diabetic DBA/2J and db/db mice with the dual FXR/TGR5 agonist INT-767 improved proteinuria and prevented podocyte injury, mesangial expansion, and tubulointerstitial fibrosis.
79	29089371	INT-767 exerted coordinated effects on multiple pathways, including stimulation of a signaling cascade involving AMP-activated protein kinase, sirtuin 1, PGC-1α, sirtuin 3, estrogen-related receptor-α, and Nrf-1; inhibition of endoplasmic reticulum stress; and inhibition of enhanced renal fatty acid and cholesterol metabolism.
80	29089371	These results identify the renal signaling pathways regulated by FXR and TGR5, which may be promising targets for the treatment of nephropathy in diabetes and obesity.
81	27051236	Angiotensin II Modulates p130Cas of Podocytes by the Suppression of AMP-Activated Protein Kinase.
82	27051236	Angiotensin II Modulates p130Cas of Podocytes by the Suppression of AMP-Activated Protein Kinase.
83	27051236	Angiotensin II Modulates p130Cas of Podocytes by the Suppression of AMP-Activated Protein Kinase.
84	27051236	Angiotensin II Modulates p130Cas of Podocytes by the Suppression of AMP-Activated Protein Kinase.
85	27051236	Angiotensin II Modulates p130Cas of Podocytes by the Suppression of AMP-Activated Protein Kinase.
86	27051236	Angiotensin II Modulates p130Cas of Podocytes by the Suppression of AMP-Activated Protein Kinase.
87	27051236	We have previously found that Ang II suppressed podocyte AMP-activated protein kinase (AMPK) via Ang II type 1 receptor and MAPK signaling pathway.
88	27051236	We have previously found that Ang II suppressed podocyte AMP-activated protein kinase (AMPK) via Ang II type 1 receptor and MAPK signaling pathway.
89	27051236	We have previously found that Ang II suppressed podocyte AMP-activated protein kinase (AMPK) via Ang II type 1 receptor and MAPK signaling pathway.
90	27051236	We have previously found that Ang II suppressed podocyte AMP-activated protein kinase (AMPK) via Ang II type 1 receptor and MAPK signaling pathway.
91	27051236	We have previously found that Ang II suppressed podocyte AMP-activated protein kinase (AMPK) via Ang II type 1 receptor and MAPK signaling pathway.
92	27051236	We have previously found that Ang II suppressed podocyte AMP-activated protein kinase (AMPK) via Ang II type 1 receptor and MAPK signaling pathway.
93	27051236	In the present study, we investigated the roles of AMPK on the changes of p130Cas of podocyte by Ang II.
94	27051236	In the present study, we investigated the roles of AMPK on the changes of p130Cas of podocyte by Ang II.
95	27051236	In the present study, we investigated the roles of AMPK on the changes of p130Cas of podocyte by Ang II.
96	27051236	In the present study, we investigated the roles of AMPK on the changes of p130Cas of podocyte by Ang II.
97	27051236	In the present study, we investigated the roles of AMPK on the changes of p130Cas of podocyte by Ang II.
98	27051236	In the present study, we investigated the roles of AMPK on the changes of p130Cas of podocyte by Ang II.
99	27051236	We cultured mouse podocytes and treated them with various concentrations of Ang II and AMPK-modulating agents and analyzed the changes of p130Cas by confocal imaging and western blotting.
100	27051236	We cultured mouse podocytes and treated them with various concentrations of Ang II and AMPK-modulating agents and analyzed the changes of p130Cas by confocal imaging and western blotting.
101	27051236	We cultured mouse podocytes and treated them with various concentrations of Ang II and AMPK-modulating agents and analyzed the changes of p130Cas by confocal imaging and western blotting.
102	27051236	We cultured mouse podocytes and treated them with various concentrations of Ang II and AMPK-modulating agents and analyzed the changes of p130Cas by confocal imaging and western blotting.
103	27051236	We cultured mouse podocytes and treated them with various concentrations of Ang II and AMPK-modulating agents and analyzed the changes of p130Cas by confocal imaging and western blotting.
104	27051236	We cultured mouse podocytes and treated them with various concentrations of Ang II and AMPK-modulating agents and analyzed the changes of p130Cas by confocal imaging and western blotting.
105	27051236	In immunofluorescence study, Ang II decreased the intensity of p130Cas and changed its localization from peripheral cytoplasm into peri-nuclear areas in a concentrated pattern in podocytes.
106	27051236	In immunofluorescence study, Ang II decreased the intensity of p130Cas and changed its localization from peripheral cytoplasm into peri-nuclear areas in a concentrated pattern in podocytes.
107	27051236	In immunofluorescence study, Ang II decreased the intensity of p130Cas and changed its localization from peripheral cytoplasm into peri-nuclear areas in a concentrated pattern in podocytes.
108	27051236	In immunofluorescence study, Ang II decreased the intensity of p130Cas and changed its localization from peripheral cytoplasm into peri-nuclear areas in a concentrated pattern in podocytes.
109	27051236	In immunofluorescence study, Ang II decreased the intensity of p130Cas and changed its localization from peripheral cytoplasm into peri-nuclear areas in a concentrated pattern in podocytes.
110	27051236	In immunofluorescence study, Ang II decreased the intensity of p130Cas and changed its localization from peripheral cytoplasm into peri-nuclear areas in a concentrated pattern in podocytes.
111	27051236	Ang II also reduced the amount of p130Cas in time and dose-sensitive manners.
112	27051236	Ang II also reduced the amount of p130Cas in time and dose-sensitive manners.
113	27051236	Ang II also reduced the amount of p130Cas in time and dose-sensitive manners.
114	27051236	Ang II also reduced the amount of p130Cas in time and dose-sensitive manners.
115	27051236	Ang II also reduced the amount of p130Cas in time and dose-sensitive manners.
116	27051236	Ang II also reduced the amount of p130Cas in time and dose-sensitive manners.
117	27051236	AMPK activators, metformin and AICAR, restored the suppressed and mal-localized p130Cas significantly, whereas, compound C, an AMPK inhibitor, further aggravated the changes of p130Cas.
118	27051236	AMPK activators, metformin and AICAR, restored the suppressed and mal-localized p130Cas significantly, whereas, compound C, an AMPK inhibitor, further aggravated the changes of p130Cas.
119	27051236	AMPK activators, metformin and AICAR, restored the suppressed and mal-localized p130Cas significantly, whereas, compound C, an AMPK inhibitor, further aggravated the changes of p130Cas.
120	27051236	AMPK activators, metformin and AICAR, restored the suppressed and mal-localized p130Cas significantly, whereas, compound C, an AMPK inhibitor, further aggravated the changes of p130Cas.
121	27051236	AMPK activators, metformin and AICAR, restored the suppressed and mal-localized p130Cas significantly, whereas, compound C, an AMPK inhibitor, further aggravated the changes of p130Cas.
122	27051236	AMPK activators, metformin and AICAR, restored the suppressed and mal-localized p130Cas significantly, whereas, compound C, an AMPK inhibitor, further aggravated the changes of p130Cas.
123	27051236	Losartan, an Ang II type 1 receptor antagonist, recovered the abnormal changes of p130Cas suppressed by Ang II.
124	27051236	Losartan, an Ang II type 1 receptor antagonist, recovered the abnormal changes of p130Cas suppressed by Ang II.
125	27051236	Losartan, an Ang II type 1 receptor antagonist, recovered the abnormal changes of p130Cas suppressed by Ang II.
126	27051236	Losartan, an Ang II type 1 receptor antagonist, recovered the abnormal changes of p130Cas suppressed by Ang II.
127	27051236	Losartan, an Ang II type 1 receptor antagonist, recovered the abnormal changes of p130Cas suppressed by Ang II.
128	27051236	Losartan, an Ang II type 1 receptor antagonist, recovered the abnormal changes of p130Cas suppressed by Ang II.
129	27051236	These results suggest that Ang II induces the relocalization and suppression of podocyte p130Cas by the suppression of AMPK via Ang II type 1 receptor, which would contribute to Ang II-induced podocyte injury.
130	27051236	These results suggest that Ang II induces the relocalization and suppression of podocyte p130Cas by the suppression of AMPK via Ang II type 1 receptor, which would contribute to Ang II-induced podocyte injury.
131	27051236	These results suggest that Ang II induces the relocalization and suppression of podocyte p130Cas by the suppression of AMPK via Ang II type 1 receptor, which would contribute to Ang II-induced podocyte injury.
132	27051236	These results suggest that Ang II induces the relocalization and suppression of podocyte p130Cas by the suppression of AMPK via Ang II type 1 receptor, which would contribute to Ang II-induced podocyte injury.
133	27051236	These results suggest that Ang II induces the relocalization and suppression of podocyte p130Cas by the suppression of AMPK via Ang II type 1 receptor, which would contribute to Ang II-induced podocyte injury.
134	27051236	These results suggest that Ang II induces the relocalization and suppression of podocyte p130Cas by the suppression of AMPK via Ang II type 1 receptor, which would contribute to Ang II-induced podocyte injury.
135	26690487	AMP-activated protein kinase (AMPK) and acetyl-CoA carboxylase (ACC) are important regulators of fatty acid oxidation, which is frequently abnormal in the kidney with CKD.
136	26334030	Protective effects were also observed after administration of IL-17F but not IL-17C or IL-17E.
137	26334030	Mechanistically, IL-17A administration suppressed phosphorylation of signal transducer and activator of transcription 3, a central mediator of fibrosis, upregulated anti-inflammatory microglia/macrophage WAP domain protein in an AMP-activated protein kinase-dependent manner and favorably modulated renal oxidative stress and AMP-activated protein kinase activation.
138	25752605	N(ω)-Nitro-L-arginine methyl ester and 1H-[1,2,4]-oxadiazolo-[4,3-a]-quinoxalin-1-one, inhibitors of NO synthase (NOS) and soluble guanylyl cyclase, respectively, abolished tadalafil induction of H2S and AMPK phosphorylation.
139	25752605	N(ω)-Nitro-L-arginine methyl ester and 1H-[1,2,4]-oxadiazolo-[4,3-a]-quinoxalin-1-one, inhibitors of NO synthase (NOS) and soluble guanylyl cyclase, respectively, abolished tadalafil induction of H2S and AMPK phosphorylation.
140	25752605	Tadalafil rapidly augmented inducible NOS (iNOS) expression by increasing its mRNA, and siRNA for iNOS and 1400W, an iNOS blocker, inhibited tadalafil stimulation of CSE expression and AMPK phosphorylation.
141	25752605	Tadalafil rapidly augmented inducible NOS (iNOS) expression by increasing its mRNA, and siRNA for iNOS and 1400W, an iNOS blocker, inhibited tadalafil stimulation of CSE expression and AMPK phosphorylation.
142	24941909	Further, GSPE significantly decreased 24 h albumin levels and increased the expression of nephrin and podocalyxin.
143	24941909	Finally, GSPE activated the expression of PGC-1α, silent mating type information regulation 2 homolog 1 (SIRT1) and AMP-activated protein kinase (AMPK).
144	24726896	Ubiquitination-dependent CARM1 degradation facilitates Notch1-mediated podocyte apoptosis in diabetic nephropathy.
145	24726896	In this study, we found that high-glucose treatment increased Notch1 and Jagged-1 expression, the transcriptional activity of Hes, and podocyte apoptosis, and decreased the expression of coactivator-associated arginine methyltransferase 1 (CARM1) in rat podocytes.
146	24726896	Transient transfection of CARM1 reversed high-glucose-induced Notch1 expression, the transcriptional activity of Hes, and podocyte apoptosis.
147	24726896	Moreover, the silencing of CARM1 using siRNA increased Notch1 expression, the transcriptional activity of Hes, and podocyte apoptosis.
148	24726896	Here, we demonstrate that AMP-activated protein kinase alpha (AMPKα) and cannabinoid receptor 1 (CB1R) are regulated by CARM1 and that high-glucose-induced podocyte apoptosis is mediated by a CARM1-AMPKα-Notch1-CB1R signaling axis.
149	24726896	Together, our data provide evidence that ubiquitination-dependent CARM1 degradation in podocytes in diabetes promotes podocyte apoptosis via Notch1 activation.
150	24726896	Strategies to preserve CARM1 expression or reduce the enzymatic activity of a ubiquitin ligase specific for CARM1 could be used to prevent podocyte loss in diabetic nephropathy.
151	24378334	5'-AMP-activated protein kinase attenuates adriamycin-induced oxidative podocyte injury through thioredoxin-mediated suppression of the apoptosis signal-regulating kinase 1-P38 signaling pathway.
152	24378334	5'-AMP-activated protein kinase attenuates adriamycin-induced oxidative podocyte injury through thioredoxin-mediated suppression of the apoptosis signal-regulating kinase 1-P38 signaling pathway.
153	24378334	5'-AMP-activated protein kinase attenuates adriamycin-induced oxidative podocyte injury through thioredoxin-mediated suppression of the apoptosis signal-regulating kinase 1-P38 signaling pathway.
154	24378334	This effect was associated with strong suppression of oxidative stress-sensitive kinase apoptosis signal-regulating kinase 1 (ASK1) and P38 without obvious influence on ROS level.
155	24378334	This effect was associated with strong suppression of oxidative stress-sensitive kinase apoptosis signal-regulating kinase 1 (ASK1) and P38 without obvious influence on ROS level.
156	24378334	This effect was associated with strong suppression of oxidative stress-sensitive kinase apoptosis signal-regulating kinase 1 (ASK1) and P38 without obvious influence on ROS level.
157	24378334	Further analyses revealed that AMPK promoted thioredoxin (Trx) binding to ASK1.
158	24378334	Further analyses revealed that AMPK promoted thioredoxin (Trx) binding to ASK1.
159	24378334	Further analyses revealed that AMPK promoted thioredoxin (Trx) binding to ASK1.
160	24378334	Consistently, AMPK potently suppressed the expression of thioredoxin-interacting protein (TXNIP), a negative regulator of Trx, whereas it significantly enhanced the activity of Trx reductases that convert oxidized Trx to reduced form.
161	24378334	Consistently, AMPK potently suppressed the expression of thioredoxin-interacting protein (TXNIP), a negative regulator of Trx, whereas it significantly enhanced the activity of Trx reductases that convert oxidized Trx to reduced form.
162	24378334	Consistently, AMPK potently suppressed the expression of thioredoxin-interacting protein (TXNIP), a negative regulator of Trx, whereas it significantly enhanced the activity of Trx reductases that convert oxidized Trx to reduced form.
163	24378334	In further support of a key role of Trx, downregulation or inhibition of Trx exaggerated but downregulation of TXNIP attenuated the cell injury.
164	24378334	In further support of a key role of Trx, downregulation or inhibition of Trx exaggerated but downregulation of TXNIP attenuated the cell injury.
165	24378334	In further support of a key role of Trx, downregulation or inhibition of Trx exaggerated but downregulation of TXNIP attenuated the cell injury.
166	24338821	Genome-wide association studies indicate that expression of acetyl-CoA carboxylase (ACC) 2, a key enzyme of fatty acid oxidation (FAO), is associated with proteinuria in type 2 diabetes.
167	24338821	Genome-wide association studies indicate that expression of acetyl-CoA carboxylase (ACC) 2, a key enzyme of fatty acid oxidation (FAO), is associated with proteinuria in type 2 diabetes.
168	24338821	Here, we show that stimulation of FAO by aminoimidazole-4-carboxamide-1β-D-ribofuranoside (AICAR) or by adiponectin, activators of the low-energy sensor AMP-activated protein kinase (AMPK), protects from palmitic acid-induced podocyte death.
169	24338821	Here, we show that stimulation of FAO by aminoimidazole-4-carboxamide-1β-D-ribofuranoside (AICAR) or by adiponectin, activators of the low-energy sensor AMP-activated protein kinase (AMPK), protects from palmitic acid-induced podocyte death.
170	24338821	Conversely, inhibition of carnitine palmitoyltransferase (CPT-1), the rate-limiting enzyme of FAO and downstream target of AMPK, augments palmitic acid toxicity and impedes the protective AICAR effect.
171	24338821	Conversely, inhibition of carnitine palmitoyltransferase (CPT-1), the rate-limiting enzyme of FAO and downstream target of AMPK, augments palmitic acid toxicity and impedes the protective AICAR effect.
172	24068196	Moreover, renal AMPK activity, which was decreased by HFD, was recovered following the administration of metformin; in addition, fatty acid oxidation was increased by the inhibition of ACC.
173	24068196	Moreover, renal AMPK activity, which was decreased by HFD, was recovered following the administration of metformin; in addition, fatty acid oxidation was increased by the inhibition of ACC.
174	24068196	These results indicate that metformin exerts beneficial effects on obesity-induced renal injury by regulating systemic inflammation, insulin resistance and the renal AMPK/ACC pathway.
175	24068196	These results indicate that metformin exerts beneficial effects on obesity-induced renal injury by regulating systemic inflammation, insulin resistance and the renal AMPK/ACC pathway.
176	23557706	High glucose (HG) induces apoptosis of podocytes, inhibits AMP-activated protein kinase (AMPK) activation, inactivates tuberin, and activates mTOR.
177	23557706	High glucose (HG) induces apoptosis of podocytes, inhibits AMP-activated protein kinase (AMPK) activation, inactivates tuberin, and activates mTOR.
178	23557706	High glucose (HG) induces apoptosis of podocytes, inhibits AMP-activated protein kinase (AMPK) activation, inactivates tuberin, and activates mTOR.
179	23557706	HG also increases the levels of Nox4 and Nox1 and NADPH oxidase activity.
180	23557706	HG also increases the levels of Nox4 and Nox1 and NADPH oxidase activity.
181	23557706	HG also increases the levels of Nox4 and Nox1 and NADPH oxidase activity.
182	23557706	Inhibition of mTOR by low-dose rapamycin decreases HG-induced Nox4 and Nox1, NADPH oxidase activity, and podocyte apoptosis.
183	23557706	Inhibition of mTOR by low-dose rapamycin decreases HG-induced Nox4 and Nox1, NADPH oxidase activity, and podocyte apoptosis.
184	23557706	Inhibition of mTOR by low-dose rapamycin decreases HG-induced Nox4 and Nox1, NADPH oxidase activity, and podocyte apoptosis.
185	23557706	Inhibition of mTOR had no effect on AMPK or tuberin phosphorylation, indicating that mTOR is downstream of these signaling molecules.
186	23557706	Inhibition of mTOR had no effect on AMPK or tuberin phosphorylation, indicating that mTOR is downstream of these signaling molecules.
187	23557706	Inhibition of mTOR had no effect on AMPK or tuberin phosphorylation, indicating that mTOR is downstream of these signaling molecules.
188	23557706	In isolated glomeruli of OVE26 mice, there is a similar decrease in the activation of AMPK and tuberin and activation of mTOR with increase in Nox4 and NADPH oxidase activity.
189	23557706	In isolated glomeruli of OVE26 mice, there is a similar decrease in the activation of AMPK and tuberin and activation of mTOR with increase in Nox4 and NADPH oxidase activity.
190	23557706	In isolated glomeruli of OVE26 mice, there is a similar decrease in the activation of AMPK and tuberin and activation of mTOR with increase in Nox4 and NADPH oxidase activity.
191	23557706	Our data provide evidence for a novel function of mTOR in Nox4-derived reactive oxygen species generation and podocyte apoptosis that contributes to urinary albumin excretion in type 1 diabetes.
192	23557706	Our data provide evidence for a novel function of mTOR in Nox4-derived reactive oxygen species generation and podocyte apoptosis that contributes to urinary albumin excretion in type 1 diabetes.
193	23557706	Our data provide evidence for a novel function of mTOR in Nox4-derived reactive oxygen species generation and podocyte apoptosis that contributes to urinary albumin excretion in type 1 diabetes.
194	20181668	Specifically, AMPK has been identified as a regulator of several ion transporters of significance in renal physiology, including the cystic fibrosis transmembrane conductance regulator (CFTR), the epithelial sodium channel (ENaC), the Na(+)-K(+)-2Cl(-) cotransporter (NKCC), and the vacuolar H(+)-ATPase (V-ATPase).
195	20181668	Specifically, AMPK has been identified as a regulator of several ion transporters of significance in renal physiology, including the cystic fibrosis transmembrane conductance regulator (CFTR), the epithelial sodium channel (ENaC), the Na(+)-K(+)-2Cl(-) cotransporter (NKCC), and the vacuolar H(+)-ATPase (V-ATPase).
196	20181668	Specifically, AMPK has been identified as a regulator of several ion transporters of significance in renal physiology, including the cystic fibrosis transmembrane conductance regulator (CFTR), the epithelial sodium channel (ENaC), the Na(+)-K(+)-2Cl(-) cotransporter (NKCC), and the vacuolar H(+)-ATPase (V-ATPase).
197	20181668	Identified regulators of AMPK in the kidney include dietary salt, diabetes, adiponectin, and ischemia.
198	20181668	Identified regulators of AMPK in the kidney include dietary salt, diabetes, adiponectin, and ischemia.
199	20181668	Identified regulators of AMPK in the kidney include dietary salt, diabetes, adiponectin, and ischemia.
200	20181668	Activation of AMPK in response to adiponectin is described in podocytes, where it reduces albuminuria, and in tubular cells, where it reduces glycogen accumulation.
201	20181668	Activation of AMPK in response to adiponectin is described in podocytes, where it reduces albuminuria, and in tubular cells, where it reduces glycogen accumulation.
202	20181668	Activation of AMPK in response to adiponectin is described in podocytes, where it reduces albuminuria, and in tubular cells, where it reduces glycogen accumulation.
203	20150538	Mechanisms linking obesity, chronic kidney disease, and fatty liver disease: the roles of fetuin-A, adiponectin, and AMPK.
204	20150538	Recent studies identify mechanisms common to both diseases linked through an interorgan communication orchestrated by fetuin-A and adiponectin.
205	18941912	Adiponectin stimulates phosphorylation of AMP-activated protein kinase alpha in renal glomeruli.
206	18941912	Adiponectin stimulates phosphorylation of AMP-activated protein kinase alpha in renal glomeruli.
207	18941912	Adiponectin stimulates phosphorylation of AMP-activated protein kinase alpha in renal glomeruli.
208	18941912	Adiponectin stimulates phosphorylation of AMP-activated protein kinase alpha in renal glomeruli.
209	18941912	Adiponectin receptor ADIPOR1 activates the intracellular second messenger AMP-activated protein kinase (AMPK) that participates in the control of the oxidative stress and apoptosis.
210	18941912	Adiponectin receptor ADIPOR1 activates the intracellular second messenger AMP-activated protein kinase (AMPK) that participates in the control of the oxidative stress and apoptosis.
211	18941912	Adiponectin receptor ADIPOR1 activates the intracellular second messenger AMP-activated protein kinase (AMPK) that participates in the control of the oxidative stress and apoptosis.
212	18941912	Adiponectin receptor ADIPOR1 activates the intracellular second messenger AMP-activated protein kinase (AMPK) that participates in the control of the oxidative stress and apoptosis.
213	18941912	ADIPOR1 and catalytic AMPK sub-units alpha1 and alpha2 were revealed in normal rat glomeruli and incubation of freshly isolated rat glomeruli with either adiponectin or AICAR led to the activation by phosphorylation of catalytic AMPK.
214	18941912	ADIPOR1 and catalytic AMPK sub-units alpha1 and alpha2 were revealed in normal rat glomeruli and incubation of freshly isolated rat glomeruli with either adiponectin or AICAR led to the activation by phosphorylation of catalytic AMPK.
215	18941912	ADIPOR1 and catalytic AMPK sub-units alpha1 and alpha2 were revealed in normal rat glomeruli and incubation of freshly isolated rat glomeruli with either adiponectin or AICAR led to the activation by phosphorylation of catalytic AMPK.
216	18941912	ADIPOR1 and catalytic AMPK sub-units alpha1 and alpha2 were revealed in normal rat glomeruli and incubation of freshly isolated rat glomeruli with either adiponectin or AICAR led to the activation by phosphorylation of catalytic AMPK.
217	18941912	It is concluded that glomerular cells express a functional adiponectin receptor ADIPOR1 which, through activation of AMPK, may play important roles in the control of oxidative stress and cell survival within the glomerulus.
218	18941912	It is concluded that glomerular cells express a functional adiponectin receptor ADIPOR1 which, through activation of AMPK, may play important roles in the control of oxidative stress and cell survival within the glomerulus.
219	18941912	It is concluded that glomerular cells express a functional adiponectin receptor ADIPOR1 which, through activation of AMPK, may play important roles in the control of oxidative stress and cell survival within the glomerulus.
220	18941912	It is concluded that glomerular cells express a functional adiponectin receptor ADIPOR1 which, through activation of AMPK, may play important roles in the control of oxidative stress and cell survival within the glomerulus.