Ignet

Gene Information

Gene symbol: GLO1

Gene name: glyoxalase I

HGNC ID: 4323

Synonyms: GLOD1

Related Genes

#	Gene Symbol	Number of hits
1	AKR1B1	1 hits
2	AKT1	1 hits
3	ALDH9A1	1 hits
4	ALPI	1 hits
5	ASRGL1	1 hits
6	C21orf33	1 hits
7	C21orf63	1 hits
8	C4A	1 hits
9	C4B	1 hits
10	CAT	1 hits
11	CXCL12	1 hits
12	CXCR4	1 hits
13	EGF	1 hits
14	GC	1 hits
15	GLI1	1 hits
16	GSR	1 hits
17	HAGH	1 hits
18	HIF1A	1 hits
19	HLA-A	1 hits
20	IDDM2	1 hits
21	IL6	1 hits
22	INS	1 hits
23	LAT2	1 hits
24	NDUFB4	1 hits
25	NOS3	1 hits
26	PGR	1 hits
27	PKLR	1 hits
28	PPP1R3C	1 hits
29	SETD2	1 hits
30	SOD1	1 hits
31	SORD	1 hits
32	SSFA2	1 hits
33	TNFRSF10A	1 hits
34	TNFRSF25	1 hits
35	TRG	1 hits

Related Sentences

#	PMID	Sentence
1	1480818	Enzyme activities related to D- and L-lactate, such as pyruvate kinase, phosphofructokinase, aldolase, and glyoxalase I, were measured in the livers of these rats.
2	1757272	The gene for glyoxalase I (E.C. 4.4.1.5), Glo, has two alleles, Glo1 and Glo2, which are autosomally inherited in a co-dominant manner.
3	1757272	There was no correlation between Glo1 frequency and incidence of insulin-dependent diabetes mellitus (IDDM).
4	1757272	The gene for glyoxalase I (E.C. 4.4.1.5), Glo, has two alleles, Glo1 and Glo2, which are autosomally inherited in a co-dominant manner.
5	1757272	There was no correlation between Glo1 frequency and incidence of insulin-dependent diabetes mellitus (IDDM).
6	1921315	The marker genes are: plasma alkaline phosphatase-1 (Alp-1), catalase-1 (Cs-1), carboxylesterases (Es-1, Es-2, Es-14), glyoxalase I (Glo-1), group specific component (Gc), and haemoglobin-beta-chain (Hbb).
7	2725076	Human red blood cells were fractionated by density, which correlates with cell age, and the activities of glyoxalase I and glyoxalase II were determined for each fraction.
8	2725076	The activity of glyoxalase I and glyoxalase II both significantly increased during maturation of the red blood cells (P less than 0.001), except in the most dense, old cell fraction where both glyoxalase activities decreased.
9	2725076	Human red blood cells were fractionated by density, which correlates with cell age, and the activities of glyoxalase I and glyoxalase II were determined for each fraction.
10	2725076	The activity of glyoxalase I and glyoxalase II both significantly increased during maturation of the red blood cells (P less than 0.001), except in the most dense, old cell fraction where both glyoxalase activities decreased.
11	2776650	Glyoxalase I and glyoxalase II metabolise methylglyoxal to D-lactic acid, via the intermediate S-D-lactoylglutathione.
12	2776650	There were no significant differences in the activities of glyoxalase I and glyoxalase II between diabetic patients and controls.
13	2776650	For insulin-dependent patients only, those without retinopathy had a higher activity of glyoxalase II than those with retinopathy (P less than 0.05).
14	2776650	A group of age- and duration-matched insulin-dependent diabetic patients with retinopathy also had a higher activity of glyoxalase I compared with a group of diabetic patients without retinopathy (P less than 0.025).
15	2776650	Glyoxalase I and glyoxalase II metabolise methylglyoxal to D-lactic acid, via the intermediate S-D-lactoylglutathione.
16	2776650	There were no significant differences in the activities of glyoxalase I and glyoxalase II between diabetic patients and controls.
17	2776650	For insulin-dependent patients only, those without retinopathy had a higher activity of glyoxalase II than those with retinopathy (P less than 0.05).
18	2776650	A group of age- and duration-matched insulin-dependent diabetic patients with retinopathy also had a higher activity of glyoxalase I compared with a group of diabetic patients without retinopathy (P less than 0.025).
19	2776650	Glyoxalase I and glyoxalase II metabolise methylglyoxal to D-lactic acid, via the intermediate S-D-lactoylglutathione.
20	2776650	There were no significant differences in the activities of glyoxalase I and glyoxalase II between diabetic patients and controls.
21	2776650	For insulin-dependent patients only, those without retinopathy had a higher activity of glyoxalase II than those with retinopathy (P less than 0.05).
22	2776650	A group of age- and duration-matched insulin-dependent diabetic patients with retinopathy also had a higher activity of glyoxalase I compared with a group of diabetic patients without retinopathy (P less than 0.025).
23	3196289	The activities of glyoxalase I and glyoxalase II were not significantly changed, but the concentrations of the glyoxalase substrates, methylglyoxal and S-D-lactoylglutathione, and the percentage of glucotriose metabolized via the glyoxalase pathway, were significantly increased.
24	6586708	Three diabetic haplotypes were confirmed to occur frequently among affected sibs: (a) A1, B8, BFS, C2.1, C4AQO , C4B1 ,DR3, GLO2 ; (b) Aw30, Cw5 ,B18,BFF1,C2.1, C4A3 , C4BQO ,DR3, GLO2 ; (c) A2,Cw3, B15,BFS, C2.1, C4A3 , C4B3 , DR4,GLO1.
25	6955994	HLA-A, B, C, DR antigens, Bf, C4 and glyoxalase I (GLO) polymorphisms in French Basques with insulin-dependent diabetes mellitus (IDDM).
26	7859825	The activities of glyoxalase I and glyoxalase II and the concentration of methylglyoxal were determined in 26 human lenses.
27	7859825	The activity of glyoxalase I (mean +/- S.D.) was 15.62 +/- 3.90 U (g wet weight)-1 and the activity of glyoxalase II was 0.189 +/- 0.087 U (g wet weight)-1 (n = 26).
28	7859825	There was a significant negative correlation of both the activity of glyoxalase I and the activity of glyoxalase II with subject age but no correlation of methylglyoxal concentration with subject age.
29	7859825	The activities of glyoxalase I and glyoxalase II and the concentration of methylglyoxal were determined in 26 human lenses.
30	7859825	The activity of glyoxalase I (mean +/- S.D.) was 15.62 +/- 3.90 U (g wet weight)-1 and the activity of glyoxalase II was 0.189 +/- 0.087 U (g wet weight)-1 (n = 26).
31	7859825	There was a significant negative correlation of both the activity of glyoxalase I and the activity of glyoxalase II with subject age but no correlation of methylglyoxal concentration with subject age.
32	7859825	The activities of glyoxalase I and glyoxalase II and the concentration of methylglyoxal were determined in 26 human lenses.
33	7859825	The activity of glyoxalase I (mean +/- S.D.) was 15.62 +/- 3.90 U (g wet weight)-1 and the activity of glyoxalase II was 0.189 +/- 0.087 U (g wet weight)-1 (n = 26).
34	7859825	There was a significant negative correlation of both the activity of glyoxalase I and the activity of glyoxalase II with subject age but no correlation of methylglyoxal concentration with subject age.
35	8373434	Glyoxalase I and glyoxalase II activities were decreased in the liver and increased in skeletal muscle of diabetic rats and of Statil-treated diabetic rats, relative to normal controls.
36	8636255	Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
37	8636255	Levels of aldose reductase, glyoxalase I, and glyoxalase II in mononuclear and polymorphonuclear cells from insulin-dependent diabetes mellitus (IDDM) patients with long term diabetic complications were compared to levels in IDDM patients without complications and to those in nondiabetic controls.
38	8636255	Glyoxalase I and glyoxalase II were determined spectrophotometrically.
39	8636255	Aldose reductase in mononuclear cells from symptomatic IDDM patients is significantly elevated compared to that in asymptomatic IDDM patients (mean +/- SEM, 0.96 +/- 0.20 vs. 0.46 +/- 0.08 microgram/mg protein; P < 0.02).
40	8636255	Glyoxalase I in mononuclear and polymorphonuclear cells from symptomatic IDDM patients is significantly elevated compared to that in controls [mean for mononuclear cells, 0.46 +/- 0.03 vs. 0.37 +/- 0.03 mumol/min.mg (P < 0.05); mean for polymorphonuclear cells, 0.16 +/- 0.01 vs. 0.10 +/- 0.01 mumol/min.mg (P < 0.002)].
41	8636255	Glyoxalase II is significantly elevated only in polymorphonuclear cells from symptomatic IDDM patients compared to controls (mean, 0.13 +/- 0.01 vs. 0.063 +/- 0.016 mumol/min.mg; P < 0.005).
42	8636255	Aldose reductase, glyoxalase I, and glyoxalase II are involved in the metabolism of methylglyoxal, suggesting that methylglyoxal may play a role in the etiology of diabetic complications.
43	8636255	Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
44	8636255	Levels of aldose reductase, glyoxalase I, and glyoxalase II in mononuclear and polymorphonuclear cells from insulin-dependent diabetes mellitus (IDDM) patients with long term diabetic complications were compared to levels in IDDM patients without complications and to those in nondiabetic controls.
45	8636255	Glyoxalase I and glyoxalase II were determined spectrophotometrically.
46	8636255	Aldose reductase in mononuclear cells from symptomatic IDDM patients is significantly elevated compared to that in asymptomatic IDDM patients (mean +/- SEM, 0.96 +/- 0.20 vs. 0.46 +/- 0.08 microgram/mg protein; P < 0.02).
47	8636255	Glyoxalase I in mononuclear and polymorphonuclear cells from symptomatic IDDM patients is significantly elevated compared to that in controls [mean for mononuclear cells, 0.46 +/- 0.03 vs. 0.37 +/- 0.03 mumol/min.mg (P < 0.05); mean for polymorphonuclear cells, 0.16 +/- 0.01 vs. 0.10 +/- 0.01 mumol/min.mg (P < 0.002)].
48	8636255	Glyoxalase II is significantly elevated only in polymorphonuclear cells from symptomatic IDDM patients compared to controls (mean, 0.13 +/- 0.01 vs. 0.063 +/- 0.016 mumol/min.mg; P < 0.005).
49	8636255	Aldose reductase, glyoxalase I, and glyoxalase II are involved in the metabolism of methylglyoxal, suggesting that methylglyoxal may play a role in the etiology of diabetic complications.
50	8636255	Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
51	8636255	Levels of aldose reductase, glyoxalase I, and glyoxalase II in mononuclear and polymorphonuclear cells from insulin-dependent diabetes mellitus (IDDM) patients with long term diabetic complications were compared to levels in IDDM patients without complications and to those in nondiabetic controls.
52	8636255	Glyoxalase I and glyoxalase II were determined spectrophotometrically.
53	8636255	Aldose reductase in mononuclear cells from symptomatic IDDM patients is significantly elevated compared to that in asymptomatic IDDM patients (mean +/- SEM, 0.96 +/- 0.20 vs. 0.46 +/- 0.08 microgram/mg protein; P < 0.02).
54	8636255	Glyoxalase I in mononuclear and polymorphonuclear cells from symptomatic IDDM patients is significantly elevated compared to that in controls [mean for mononuclear cells, 0.46 +/- 0.03 vs. 0.37 +/- 0.03 mumol/min.mg (P < 0.05); mean for polymorphonuclear cells, 0.16 +/- 0.01 vs. 0.10 +/- 0.01 mumol/min.mg (P < 0.002)].
55	8636255	Glyoxalase II is significantly elevated only in polymorphonuclear cells from symptomatic IDDM patients compared to controls (mean, 0.13 +/- 0.01 vs. 0.063 +/- 0.016 mumol/min.mg; P < 0.005).
56	8636255	Aldose reductase, glyoxalase I, and glyoxalase II are involved in the metabolism of methylglyoxal, suggesting that methylglyoxal may play a role in the etiology of diabetic complications.
57	8636255	Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
58	8636255	Levels of aldose reductase, glyoxalase I, and glyoxalase II in mononuclear and polymorphonuclear cells from insulin-dependent diabetes mellitus (IDDM) patients with long term diabetic complications were compared to levels in IDDM patients without complications and to those in nondiabetic controls.
59	8636255	Glyoxalase I and glyoxalase II were determined spectrophotometrically.
60	8636255	Aldose reductase in mononuclear cells from symptomatic IDDM patients is significantly elevated compared to that in asymptomatic IDDM patients (mean +/- SEM, 0.96 +/- 0.20 vs. 0.46 +/- 0.08 microgram/mg protein; P < 0.02).
61	8636255	Glyoxalase I in mononuclear and polymorphonuclear cells from symptomatic IDDM patients is significantly elevated compared to that in controls [mean for mononuclear cells, 0.46 +/- 0.03 vs. 0.37 +/- 0.03 mumol/min.mg (P < 0.05); mean for polymorphonuclear cells, 0.16 +/- 0.01 vs. 0.10 +/- 0.01 mumol/min.mg (P < 0.002)].
62	8636255	Glyoxalase II is significantly elevated only in polymorphonuclear cells from symptomatic IDDM patients compared to controls (mean, 0.13 +/- 0.01 vs. 0.063 +/- 0.016 mumol/min.mg; P < 0.005).
63	8636255	Aldose reductase, glyoxalase I, and glyoxalase II are involved in the metabolism of methylglyoxal, suggesting that methylglyoxal may play a role in the etiology of diabetic complications.
64	8636255	Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study.
65	8636255	Levels of aldose reductase, glyoxalase I, and glyoxalase II in mononuclear and polymorphonuclear cells from insulin-dependent diabetes mellitus (IDDM) patients with long term diabetic complications were compared to levels in IDDM patients without complications and to those in nondiabetic controls.
66	8636255	Glyoxalase I and glyoxalase II were determined spectrophotometrically.
67	8636255	Aldose reductase in mononuclear cells from symptomatic IDDM patients is significantly elevated compared to that in asymptomatic IDDM patients (mean +/- SEM, 0.96 +/- 0.20 vs. 0.46 +/- 0.08 microgram/mg protein; P < 0.02).
68	8636255	Glyoxalase I in mononuclear and polymorphonuclear cells from symptomatic IDDM patients is significantly elevated compared to that in controls [mean for mononuclear cells, 0.46 +/- 0.03 vs. 0.37 +/- 0.03 mumol/min.mg (P < 0.05); mean for polymorphonuclear cells, 0.16 +/- 0.01 vs. 0.10 +/- 0.01 mumol/min.mg (P < 0.002)].
69	8636255	Glyoxalase II is significantly elevated only in polymorphonuclear cells from symptomatic IDDM patients compared to controls (mean, 0.13 +/- 0.01 vs. 0.063 +/- 0.016 mumol/min.mg; P < 0.005).
70	8636255	Aldose reductase, glyoxalase I, and glyoxalase II are involved in the metabolism of methylglyoxal, suggesting that methylglyoxal may play a role in the etiology of diabetic complications.
71	9486985	Glyoxalase-I catalyzes the conversion of MG to S-D-lactoylglutathione, which in turn is converted to D-lactate by glyoxalase-II.
72	9679550	It is comprised of two enzymes, glyoxalase I and glyoxalase II, and a catalytic amount of reduced glutathione (GSH) as cofactor.
73	9771022	This system consists of two enzymes, glyoxalase I and glyoxalase II.
74	11306074	Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications.
75	11306074	Thus, glutathione converts aldose reductase from an aldehyde reductase to a ketone reductase with methylglyoxal as substrate.
76	11306074	The relative importance of aldose reductase and glyoxalase-I in the metabolic disposal of methylglyoxal is highly dependent upon the concentration of glutathione, owing to the non-catalytic pre-enzymatic reaction between methylglyoxal and glutathione.
77	11306074	Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications.
78	11306074	Thus, glutathione converts aldose reductase from an aldehyde reductase to a ketone reductase with methylglyoxal as substrate.
79	11306074	The relative importance of aldose reductase and glyoxalase-I in the metabolic disposal of methylglyoxal is highly dependent upon the concentration of glutathione, owing to the non-catalytic pre-enzymatic reaction between methylglyoxal and glutathione.
80	12604221	Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase.
81	16085563	Troglitazone (TRG) is an anti-diabetic thiazolidinedione drug previously used to treat insulin-resistance in Type 2 diabetes.
82	16085563	We previously showed that TRG down regulates GLO1 gene expression in a number of cell types and reasoned that TRG might be a useful adjunct therapy to overcome DOX resistance.
83	16085563	Higher doses of TRG were found to alter histone H3:H2B ratios with a decreased ratio in DOX-sensitive and increased ratio in DOX-resistant lines.
84	16934871	Candidate genes of anxiety-related behavior in HAB/LAB rats and mice: focus on vasopressin and glyoxalase-I.
85	16934871	In both HAB/LAB rats and mice, the behavioral phenotype has been found to be significantly correlated with the expression of the neuropeptide arginine vasopressin (AVP) at the level of the hypothalamic paraventricular nucleus (PVN).
86	16934871	As shown exemplarily in HAB rats and LAB mice, single nucleotide polymorphisms (SNPs) in regulatory structures of the AVP gene underlie AVP-mediated phenotypic phenomena; in HAB rats, a SNP in the promoter of the AVP gene leads to reduced binding of the transcriptional repressor CBF-A, thus causing AVP overexpression and overrelease.
87	16934871	Conversely, in LAB mice, a SNP in the AVP gene seems to cause an amino acid exchange in the signal peptide, presumably leading to a deficit in bioavailable AVP likely to underlie the total hypo-anxiety of LAB mice in combination with signs of central diabetes insipidus.
88	16934871	Another feature of LAB mice is overexpression of glyoxalase-I.
89	16934871	Candidate genes of anxiety-related behavior in HAB/LAB rats and mice: focus on vasopressin and glyoxalase-I.
90	16934871	In both HAB/LAB rats and mice, the behavioral phenotype has been found to be significantly correlated with the expression of the neuropeptide arginine vasopressin (AVP) at the level of the hypothalamic paraventricular nucleus (PVN).
91	16934871	As shown exemplarily in HAB rats and LAB mice, single nucleotide polymorphisms (SNPs) in regulatory structures of the AVP gene underlie AVP-mediated phenotypic phenomena; in HAB rats, a SNP in the promoter of the AVP gene leads to reduced binding of the transcriptional repressor CBF-A, thus causing AVP overexpression and overrelease.
92	16934871	Conversely, in LAB mice, a SNP in the AVP gene seems to cause an amino acid exchange in the signal peptide, presumably leading to a deficit in bioavailable AVP likely to underlie the total hypo-anxiety of LAB mice in combination with signs of central diabetes insipidus.
93	16934871	Another feature of LAB mice is overexpression of glyoxalase-I.
94	18227068	Because hyperglycemia increases reactive oxygen species in a number of cell types, and because many of the defects responsible for impaired vasculogenesis involve HIF1-regulated genes, we hypothesized that HIF1 function is impaired in diabetes because of reactive oxygen species-induced modification of HIF1alpha by the glyoxalase 1 (GLO1) substrate methylglyoxal.
95	18227068	In hypoxic fibroblasts cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the EPC mobilizing chemokine stromal cell-derived factor-1 (SDF-1) and of vascular epidermal growth factor, which modulates growth and differentiation of recruited EPCs.
96	18227068	In hypoxic EPCs cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the SDF-1 receptor CXCR4, and endothelial nitric-oxide synthase, an enzyme essential for EPC mobilization.
97	18227068	Because hyperglycemia increases reactive oxygen species in a number of cell types, and because many of the defects responsible for impaired vasculogenesis involve HIF1-regulated genes, we hypothesized that HIF1 function is impaired in diabetes because of reactive oxygen species-induced modification of HIF1alpha by the glyoxalase 1 (GLO1) substrate methylglyoxal.
98	18227068	In hypoxic fibroblasts cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the EPC mobilizing chemokine stromal cell-derived factor-1 (SDF-1) and of vascular epidermal growth factor, which modulates growth and differentiation of recruited EPCs.
99	18227068	In hypoxic EPCs cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the SDF-1 receptor CXCR4, and endothelial nitric-oxide synthase, an enzyme essential for EPC mobilization.
100	18227068	Because hyperglycemia increases reactive oxygen species in a number of cell types, and because many of the defects responsible for impaired vasculogenesis involve HIF1-regulated genes, we hypothesized that HIF1 function is impaired in diabetes because of reactive oxygen species-induced modification of HIF1alpha by the glyoxalase 1 (GLO1) substrate methylglyoxal.
101	18227068	In hypoxic fibroblasts cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the EPC mobilizing chemokine stromal cell-derived factor-1 (SDF-1) and of vascular epidermal growth factor, which modulates growth and differentiation of recruited EPCs.
102	18227068	In hypoxic EPCs cultured in high glucose, overexpression of GLO1 prevented reduced expression of both the SDF-1 receptor CXCR4, and endothelial nitric-oxide synthase, an enzyme essential for EPC mobilization.
103	18720345	The intake of these compounds significantly and dose-dependently decreased the levels of plasma glycated hemoglobin (HbA1c), renal carboxymethyllysine and urinary glycated albumin (p < 0.05).
104	18720345	SEC or SPC intake significantly and dose-dependently diminished renal aldose reductase (AR) activity and enhanced glyoxalase I (GLI) activity (p < 0.05); also significantly decreased renal sorbitol and fructose concentrations (p < 0.05).
105	18720345	The intake of SEC or SPC significantly lowered renal VEGF level (p < 0.05), and caused dose-dependent downregulation in AR mRNA expression, and upregulation in GLI mRNA expression (p < 0.05).
106	19687346	Moreover, glyoxalase I and II, enzymes that detoxify MG, and glutathione reductase, which generates reduced glutathione, a cofactor for glyoxalase, are also reduced in preeclampsia.
107	20632216	The activities of superoxide dismutase, catalase and glyoxalase I were assayed.
108	20632216	Catalase and glyoxalase I had a decrease in their activities.
109	20632216	The activities of superoxide dismutase, catalase and glyoxalase I were assayed.
110	20632216	Catalase and glyoxalase I had a decrease in their activities.
111	21378371	The activities of catalase, superoxide dismutase, and glyoxalase I were also assessed.
112	21439372	Oral administration of resveratrol to diabetic rats showed a significant normalization on the levels of creatinine clearance, plasma adiponectin, C-peptide and renal superoxide anion, hydroxyl radical, nitric oxide, TNF-α, IL-1β, IL-6 and NF-κB p65 subunit and activities of renal aspartate transaminase, alanine transaminase and alkaline phosphatase in comparison with diabetic rats.
113	21439372	The altered activities of renal aldose reductase, sorbitol dehydrogenase and glyoxalase-I and elevated level of serum advanced glycation end products in diabetic rats were also reverted back to near normalcy.
114	21439372	Further, resveratrol treatment revealed a significant improvement in superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase and glutathione reductase activities and vitamins C and E, and reduced glutathione levels, with a significant decline in lipid peroxides, hydroperoxides and protein carbonyls levels in diabetic kidneys.
115	21456600	PCA treatments at 2 and 4% significantly lowered renal activity and mRNA expression of aldose reductase and sorbitol dehydrogenase (p < 0.05), and PCA treatments only at 4% significantly enhanced renal glyoxalase I mRNA expression (p < 0.05).
116	21456600	PCA treatments also dose-dependently decreased the renal level of type-IV collagen, fibronectin, and transforming growth factor-β1 (p < 0.05), as well as dose-dependently diminished renal protein kinase C (PKC) activity (p < 0.05); however, PCA treatments only at 4% suppressed renal mRNA expression of PKC-α and PKC-beta (p < 0.05).
117	23819326	Group C+DM2 was characterized by higher levels ofbody mass index, insulinemia, estradiolemia, interleukin 6 in serum, and glyoxalase I activity in mononuclears.
118	23879009	Influencing the transduction mechanisms primarily through activation of protein kinase activated by 5'AMP (AMPK) regulates the activity of the AMPK/mTOR signaling pathway.
119	23879009	Metformin has antiproliferative properties; reduces the VEGF levels, causing a reduction in tumor vasculature; causes an increase in progesterone receptor, which increases the response to hormonal therapy; inhibits the expression of glyoxalase I, mediating resistance to chemotherapy; decreases in the concentration of human telomerase; reduces the activity of Akt and Erk kinases, key regulators of metabolism and progression of tumors and also inhibits the formation of metastases.