Ignet

Gene Information

Gene symbol: MAOA

Gene name: monoamine oxidase A

HGNC ID: 6833

Related Genes

#	Gene Symbol	Number of hits
1	AGTR1	1 hits
2	ALDH9A1	1 hits
3	AOC3	1 hits
4	CAT	1 hits
5	ITLN1	1 hits
6	MAOB	1 hits

Related Sentences

#	PMID	Sentence
1	14697891	MAO consists of two subtypes, MAO-A and MAO-B, depending on their substrates and sensitivity to inhibitors.
2	14697891	The function of MAO-A is highly dependent on the lipid constituent of mitochondrial membrane, whereas the function of MAO-B does not depend on the lipid status of mitochondrial membrane.
3	14697891	In the islet of Langerhans, MAO-A is observed in about 50% of the cells, whereas MAO-B is less abundant and located mainly in the periphery of pancreatic islets.
4	14697891	MAO consists of two subtypes, MAO-A and MAO-B, depending on their substrates and sensitivity to inhibitors.
5	14697891	The function of MAO-A is highly dependent on the lipid constituent of mitochondrial membrane, whereas the function of MAO-B does not depend on the lipid status of mitochondrial membrane.
6	14697891	In the islet of Langerhans, MAO-A is observed in about 50% of the cells, whereas MAO-B is less abundant and located mainly in the periphery of pancreatic islets.
7	14697891	MAO consists of two subtypes, MAO-A and MAO-B, depending on their substrates and sensitivity to inhibitors.
8	14697891	The function of MAO-A is highly dependent on the lipid constituent of mitochondrial membrane, whereas the function of MAO-B does not depend on the lipid status of mitochondrial membrane.
9	14697891	In the islet of Langerhans, MAO-A is observed in about 50% of the cells, whereas MAO-B is less abundant and located mainly in the periphery of pancreatic islets.
10	16154211	Brain MAO-A and MAO-B activity were both significantly increased in the stressed rats.
11	22124705	Correlation between total nitrite/nitrate concentrations and monoamine oxidase (types A and B) and semicarbazide-sensitive amine oxidase enzymatic activities in human mesenteric arteries from non-diabetic and type 2 diabetic patients.
12	22124705	The aim of this study was to determine the correlation between total nitrite/nitrate concentrations (NOx) and the kinetic parameters of monoamine oxidase enzymes (MAO-A and MAO-B) and semicarbazide-sensitive amine oxidase (SSAO) in human mesenteric arteries.
13	22124705	Segments of human inferior mesenteric arteries from non-diabetic (61.1 ± 8.9 years old, 7 males and 5 females, N = 12) and type 2 diabetic patients (65.8 ± 6.2 years old, 8 males and 4 females, N = 12) were used to determine NOx concentrations and the kinetic parameters of MAO-A, MAO-B and SSAO by the Griess reaction and by radiochemical assay, respectively.
14	22124705	In the non-diabetic group, there was a positive correlation between NOx concentrations and MAO-B parameters: Km (r = 0.612, P = 0.034) and Vmax (r = 0.593, P = 0.042), and a negative correlation with the SSAO parameters: Km (r = -0.625, P = 0.029) and Vmax (r = -0.754, P = 0.005).
15	22124705	Correlation between total nitrite/nitrate concentrations and monoamine oxidase (types A and B) and semicarbazide-sensitive amine oxidase enzymatic activities in human mesenteric arteries from non-diabetic and type 2 diabetic patients.
16	22124705	The aim of this study was to determine the correlation between total nitrite/nitrate concentrations (NOx) and the kinetic parameters of monoamine oxidase enzymes (MAO-A and MAO-B) and semicarbazide-sensitive amine oxidase (SSAO) in human mesenteric arteries.
17	22124705	Segments of human inferior mesenteric arteries from non-diabetic (61.1 ± 8.9 years old, 7 males and 5 females, N = 12) and type 2 diabetic patients (65.8 ± 6.2 years old, 8 males and 4 females, N = 12) were used to determine NOx concentrations and the kinetic parameters of MAO-A, MAO-B and SSAO by the Griess reaction and by radiochemical assay, respectively.
18	22124705	In the non-diabetic group, there was a positive correlation between NOx concentrations and MAO-B parameters: Km (r = 0.612, P = 0.034) and Vmax (r = 0.593, P = 0.042), and a negative correlation with the SSAO parameters: Km (r = -0.625, P = 0.029) and Vmax (r = -0.754, P = 0.005).
19	24012905	We explored the hypothesis that exposure of cardiomyocytes to AT-II caused activation of MAO-A and also of catalase and aldehyde dehydrogenase activities, enzymes involved in degrading MAO's end products.
20	24012905	In each group of cells, MAO, catalase and aldehyde dehydrogenase activities were measured radiochemically and spectrophotometrically.
21	24012905	The same enzymes were also measured in HL-1 immortalized cardiomyocytes not exposed and exposed to AT-II (100 nM for 18 h) in the absence and in the presence of irbesartan (1 μM), an AT1 antagonist.
22	24012905	MAO-A catalase and aldehyde dehydrogenase activities were found significantly higher in D, than in N cells.
23	24012905	MAO-A positively correlated with catalase activity in D cells.
24	24012905	MAO-A and aldehyde dehydrogenase but not catalase over-activation, were prevented in DLos cells.
25	24012905	Similarly, MAO-A activity, but not catalase and aldehyde dehydrogenase increased significantly in HL-1 cells acutely exposed to AT-II and this increase was prevented when irbesartan, an AT1 antagonist was present.
26	24012905	Over-activation of cardiomyocyte MAO-A activity is among acute (18 h) and short-term (2-weeks of diabetes) cardiac effects of AT-II and a novel target of AT1 antagonists, first line treatments of diabetic cardiomyopathy.
27	24012905	We explored the hypothesis that exposure of cardiomyocytes to AT-II caused activation of MAO-A and also of catalase and aldehyde dehydrogenase activities, enzymes involved in degrading MAO's end products.
28	24012905	In each group of cells, MAO, catalase and aldehyde dehydrogenase activities were measured radiochemically and spectrophotometrically.
29	24012905	The same enzymes were also measured in HL-1 immortalized cardiomyocytes not exposed and exposed to AT-II (100 nM for 18 h) in the absence and in the presence of irbesartan (1 μM), an AT1 antagonist.
30	24012905	MAO-A catalase and aldehyde dehydrogenase activities were found significantly higher in D, than in N cells.
31	24012905	MAO-A positively correlated with catalase activity in D cells.
32	24012905	MAO-A and aldehyde dehydrogenase but not catalase over-activation, were prevented in DLos cells.
33	24012905	Similarly, MAO-A activity, but not catalase and aldehyde dehydrogenase increased significantly in HL-1 cells acutely exposed to AT-II and this increase was prevented when irbesartan, an AT1 antagonist was present.
34	24012905	Over-activation of cardiomyocyte MAO-A activity is among acute (18 h) and short-term (2-weeks of diabetes) cardiac effects of AT-II and a novel target of AT1 antagonists, first line treatments of diabetic cardiomyopathy.
35	24012905	We explored the hypothesis that exposure of cardiomyocytes to AT-II caused activation of MAO-A and also of catalase and aldehyde dehydrogenase activities, enzymes involved in degrading MAO's end products.
36	24012905	In each group of cells, MAO, catalase and aldehyde dehydrogenase activities were measured radiochemically and spectrophotometrically.
37	24012905	The same enzymes were also measured in HL-1 immortalized cardiomyocytes not exposed and exposed to AT-II (100 nM for 18 h) in the absence and in the presence of irbesartan (1 μM), an AT1 antagonist.
38	24012905	MAO-A catalase and aldehyde dehydrogenase activities were found significantly higher in D, than in N cells.
39	24012905	MAO-A positively correlated with catalase activity in D cells.
40	24012905	MAO-A and aldehyde dehydrogenase but not catalase over-activation, were prevented in DLos cells.
41	24012905	Similarly, MAO-A activity, but not catalase and aldehyde dehydrogenase increased significantly in HL-1 cells acutely exposed to AT-II and this increase was prevented when irbesartan, an AT1 antagonist was present.
42	24012905	Over-activation of cardiomyocyte MAO-A activity is among acute (18 h) and short-term (2-weeks of diabetes) cardiac effects of AT-II and a novel target of AT1 antagonists, first line treatments of diabetic cardiomyopathy.
43	24012905	We explored the hypothesis that exposure of cardiomyocytes to AT-II caused activation of MAO-A and also of catalase and aldehyde dehydrogenase activities, enzymes involved in degrading MAO's end products.
44	24012905	In each group of cells, MAO, catalase and aldehyde dehydrogenase activities were measured radiochemically and spectrophotometrically.
45	24012905	The same enzymes were also measured in HL-1 immortalized cardiomyocytes not exposed and exposed to AT-II (100 nM for 18 h) in the absence and in the presence of irbesartan (1 μM), an AT1 antagonist.
46	24012905	MAO-A catalase and aldehyde dehydrogenase activities were found significantly higher in D, than in N cells.
47	24012905	MAO-A positively correlated with catalase activity in D cells.
48	24012905	MAO-A and aldehyde dehydrogenase but not catalase over-activation, were prevented in DLos cells.
49	24012905	Similarly, MAO-A activity, but not catalase and aldehyde dehydrogenase increased significantly in HL-1 cells acutely exposed to AT-II and this increase was prevented when irbesartan, an AT1 antagonist was present.
50	24012905	Over-activation of cardiomyocyte MAO-A activity is among acute (18 h) and short-term (2-weeks of diabetes) cardiac effects of AT-II and a novel target of AT1 antagonists, first line treatments of diabetic cardiomyopathy.
51	24012905	We explored the hypothesis that exposure of cardiomyocytes to AT-II caused activation of MAO-A and also of catalase and aldehyde dehydrogenase activities, enzymes involved in degrading MAO's end products.
52	24012905	In each group of cells, MAO, catalase and aldehyde dehydrogenase activities were measured radiochemically and spectrophotometrically.
53	24012905	The same enzymes were also measured in HL-1 immortalized cardiomyocytes not exposed and exposed to AT-II (100 nM for 18 h) in the absence and in the presence of irbesartan (1 μM), an AT1 antagonist.
54	24012905	MAO-A catalase and aldehyde dehydrogenase activities were found significantly higher in D, than in N cells.
55	24012905	MAO-A positively correlated with catalase activity in D cells.
56	24012905	MAO-A and aldehyde dehydrogenase but not catalase over-activation, were prevented in DLos cells.
57	24012905	Similarly, MAO-A activity, but not catalase and aldehyde dehydrogenase increased significantly in HL-1 cells acutely exposed to AT-II and this increase was prevented when irbesartan, an AT1 antagonist was present.
58	24012905	Over-activation of cardiomyocyte MAO-A activity is among acute (18 h) and short-term (2-weeks of diabetes) cardiac effects of AT-II and a novel target of AT1 antagonists, first line treatments of diabetic cardiomyopathy.
59	24012905	We explored the hypothesis that exposure of cardiomyocytes to AT-II caused activation of MAO-A and also of catalase and aldehyde dehydrogenase activities, enzymes involved in degrading MAO's end products.
60	24012905	In each group of cells, MAO, catalase and aldehyde dehydrogenase activities were measured radiochemically and spectrophotometrically.
61	24012905	The same enzymes were also measured in HL-1 immortalized cardiomyocytes not exposed and exposed to AT-II (100 nM for 18 h) in the absence and in the presence of irbesartan (1 μM), an AT1 antagonist.
62	24012905	MAO-A catalase and aldehyde dehydrogenase activities were found significantly higher in D, than in N cells.
63	24012905	MAO-A positively correlated with catalase activity in D cells.
64	24012905	MAO-A and aldehyde dehydrogenase but not catalase over-activation, were prevented in DLos cells.
65	24012905	Similarly, MAO-A activity, but not catalase and aldehyde dehydrogenase increased significantly in HL-1 cells acutely exposed to AT-II and this increase was prevented when irbesartan, an AT1 antagonist was present.
66	24012905	Over-activation of cardiomyocyte MAO-A activity is among acute (18 h) and short-term (2-weeks of diabetes) cardiac effects of AT-II and a novel target of AT1 antagonists, first line treatments of diabetic cardiomyopathy.