Ignet

Gene Information

Gene symbol: ANG

Gene name: angiogenin, ribonuclease, RNase A family, 5

HGNC ID: 483

Synonyms: RNASE5

Related Genes

#	Gene Symbol	Number of hits
1	ACE	1 hits
2	ACE2	1 hits
3	AGT	1 hits
4	AGTR1	1 hits
5	AKT1	1 hits
6	BECN1	1 hits
7	BEST1	1 hits
8	CYBB	1 hits
9	MAPK3	1 hits
10	MME	1 hits
11	NOX5	1 hits
12	REN	1 hits

Related Sentences

#	PMID	Sentence
1	16234311	High glucose resulted in the activation of ERK1/2 and Akt/PKB.
2	16234311	ERK1/2 pathway inhibitor or the dominant negative mutant of Akt/PKB inhibited high glucose-induced protein synthesis.
3	16234311	The stimulatory effect of high glucose on ROS production, ERK1/2, and Akt/PKB activation was prevented by the antioxidants catalase, diphenylene iodonium, and N-acetylcysteine.
4	16234311	In addition, ANG II resulted in the activation of ERK1/2 and Akt/PKB and GEC hypertrophy.
5	16234311	Moreover, high glucose and ANG II exhibited additive effects on ERK1/2 and Akt/PKB activation as well as protein synthesis.
6	16234311	These data demonstrate that high glucose stimulates GEC hypertrophy through a ROS-dependent activation of ERK1/2 and Akt/PKB.
7	16234311	High glucose resulted in the activation of ERK1/2 and Akt/PKB.
8	16234311	ERK1/2 pathway inhibitor or the dominant negative mutant of Akt/PKB inhibited high glucose-induced protein synthesis.
9	16234311	The stimulatory effect of high glucose on ROS production, ERK1/2, and Akt/PKB activation was prevented by the antioxidants catalase, diphenylene iodonium, and N-acetylcysteine.
10	16234311	In addition, ANG II resulted in the activation of ERK1/2 and Akt/PKB and GEC hypertrophy.
11	16234311	Moreover, high glucose and ANG II exhibited additive effects on ERK1/2 and Akt/PKB activation as well as protein synthesis.
12	16234311	These data demonstrate that high glucose stimulates GEC hypertrophy through a ROS-dependent activation of ERK1/2 and Akt/PKB.
13	17429035	Intraglomerular ANG II has been linked to glomerular injury.
14	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
15	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
16	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
17	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
18	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
19	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
20	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
21	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
22	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
23	17429035	Intraglomerular ANG II has been linked to glomerular injury.
24	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
25	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
26	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
27	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
28	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
29	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
30	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
31	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
32	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
33	17429035	Intraglomerular ANG II has been linked to glomerular injury.
34	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
35	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
36	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
37	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
38	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
39	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
40	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
41	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
42	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
43	17429035	Intraglomerular ANG II has been linked to glomerular injury.
44	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
45	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
46	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
47	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
48	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
49	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
50	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
51	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
52	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
53	17429035	Intraglomerular ANG II has been linked to glomerular injury.
54	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
55	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
56	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
57	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
58	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
59	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
60	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
61	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
62	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
63	17429035	Intraglomerular ANG II has been linked to glomerular injury.
64	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
65	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
66	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
67	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
68	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
69	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
70	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
71	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
72	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
73	17429035	Intraglomerular ANG II has been linked to glomerular injury.
74	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
75	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
76	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
77	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
78	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
79	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
80	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
81	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
82	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
83	17429035	Intraglomerular ANG II has been linked to glomerular injury.
84	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
85	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
86	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
87	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
88	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
89	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
90	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
91	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
92	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
93	17429035	Intraglomerular ANG II has been linked to glomerular injury.
94	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
95	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
96	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
97	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
98	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
99	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
100	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
101	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
102	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
103	17429035	Intraglomerular ANG II has been linked to glomerular injury.
104	17429035	However, little is known about the contribution of podocytes (POD) to intraglomerular ANG II homeostasis.
105	17429035	Immortalized mouse POD were incubated with 1-2 microM ANG I, ANG II, or the renin substrate ANG-(1-14) for different time intervals and coincubated in parallel with various inhibitors.
106	17429035	POD incubated with 1 microM ANG I primarily formed ANG-(1-9) and ANG-(1-7).
107	17429035	In contrast, MES incubated with ANG I primarily generated ANG II.
108	17429035	Modest angiotensin-converting enzyme (ACE) activity was also detected in POD, although only after cells were incubated with 2 microM ANG I.
109	17429035	In addition, we observed that POD degraded ANG II into ANG III and ANG-(1-7).
110	17429035	An aminopeptidase A inhibitor inhibited ANG III formation, and an ACE2 inhibitor led to ANG II accumulation.
111	17429035	Furthermore, we found that POD converted ANG-(1-14) to ANG I and ANG-(1-7).
112	17429035	These findings demonstrate that POD express a functional intrinsic renin-angiotensin system characterized by neprilysin, aminopeptidase A, ACE2, and renin activities, which predominantly lead to ANG-(1-7) and ANG-(1-9) formation, as well as ANG II degradation.
113	20007350	Comparative effect of direct renin inhibition and AT1R blockade on glomerular filtration barrier injury in the transgenic Ren2 rat.
114	20007350	Renin is the rate-limiting step in angiotensin (ANG II) generation.
115	20007350	Recent work suggests renin inhibition improves proteinuria comparable to ANG type 1 receptor (AT1R) blockade (ARB).
116	20007350	Structural and functional alterations were accompanied by increased renal cortical ANG II, AT1R, as well as NADPH oxidase subunit (Nox2) expression compared with SD controls.
117	20007350	Comparative effect of direct renin inhibition and AT1R blockade on glomerular filtration barrier injury in the transgenic Ren2 rat.
118	20007350	Renin is the rate-limiting step in angiotensin (ANG II) generation.
119	20007350	Recent work suggests renin inhibition improves proteinuria comparable to ANG type 1 receptor (AT1R) blockade (ARB).
120	20007350	Structural and functional alterations were accompanied by increased renal cortical ANG II, AT1R, as well as NADPH oxidase subunit (Nox2) expression compared with SD controls.
121	20007350	Comparative effect of direct renin inhibition and AT1R blockade on glomerular filtration barrier injury in the transgenic Ren2 rat.
122	20007350	Renin is the rate-limiting step in angiotensin (ANG II) generation.
123	20007350	Recent work suggests renin inhibition improves proteinuria comparable to ANG type 1 receptor (AT1R) blockade (ARB).
124	20007350	Structural and functional alterations were accompanied by increased renal cortical ANG II, AT1R, as well as NADPH oxidase subunit (Nox2) expression compared with SD controls.
125	20484657	ANG II promotes autophagy in podocytes.
126	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
127	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
128	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
129	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
130	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
131	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
132	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
133	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
134	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
135	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
136	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
137	20484657	ANG II promotes autophagy in podocytes.
138	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
139	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
140	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
141	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
142	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
143	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
144	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
145	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
146	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
147	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
148	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
149	20484657	ANG II promotes autophagy in podocytes.
150	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
151	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
152	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
153	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
154	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
155	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
156	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
157	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
158	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
159	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
160	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
161	20484657	ANG II promotes autophagy in podocytes.
162	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
163	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
164	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
165	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
166	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
167	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
168	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
169	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
170	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
171	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
172	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
173	20484657	ANG II promotes autophagy in podocytes.
174	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
175	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
176	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
177	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
178	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
179	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
180	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
181	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
182	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
183	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
184	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
185	20484657	ANG II promotes autophagy in podocytes.
186	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
187	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
188	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
189	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
190	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
191	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
192	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
193	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
194	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
195	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
196	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
197	20484657	ANG II promotes autophagy in podocytes.
198	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
199	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
200	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
201	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
202	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
203	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
204	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
205	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
206	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
207	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
208	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
209	20484657	ANG II promotes autophagy in podocytes.
210	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
211	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
212	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
213	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
214	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
215	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
216	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
217	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
218	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
219	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
220	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
221	20484657	ANG II promotes autophagy in podocytes.
222	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
223	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
224	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
225	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
226	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
227	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
228	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
229	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
230	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
231	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
232	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
233	20484657	ANG II promotes autophagy in podocytes.
234	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
235	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
236	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
237	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
238	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
239	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
240	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
241	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
242	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
243	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
244	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
245	20484657	ANG II promotes autophagy in podocytes.
246	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
247	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
248	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
249	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
250	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
251	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
252	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
253	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
254	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
255	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
256	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
257	20484657	ANG II promotes autophagy in podocytes.
258	20484657	Podocytes are an integral and important constituent of the glomerular filtration barrier (GFB) and are exposed to a higher concentrations of ANG II in diseased states; consequently, podocytes may accumulate oxidized proteins and damaged mitochondria.
259	20484657	In the present study, we evaluated the effect of ANG II on the podocyte autophagic process, which is likely to be triggered in order to degrade unwanted proteins and damaged organelles.
260	20484657	To quantitate the occurrence of autophagy, electron microscopic studies were carried out on control and ANG II-treated conditionally immortalized mouse podocytes (CIMPs).
261	20484657	ANG II-treated cells showed a fivefold greater number of autophagosomes/field compared with control cells.
262	20484657	This proautophagic effect of ANG II was inhibited by pretreatment with 3-methyladenine, an inhibitor of autophagy.
263	20484657	ANG II also enhanced podocyte expression of autophagic genes such as LC3-2 and beclin-1.
264	20484657	Since oxidative stress is often associated with the induction of autophagy, we examined the effect of ANG II on podocyte reactive oxygen species (ROS) generation.
265	20484657	ANG II enhanced podocyte ROS generation in a time-dependent manner.
266	20484657	To determine whether there is a causal relationship between ANG II-induced oxidative stress and induction of autophagy, we evaluated the effect of antioxidants on ANG II-induced autophagy.
267	20484657	As expected, the proautophagic effect of ANG II was inhibited by antioxidants.
268	20484657	We conclude that ANG II promotes podocyte autophagy through the generation of ROS.
269	22461301	Formation of ANG II from ANG I was largely abolished by an ANG-converting enzyme (ACE) inhibitor, whereas ANG-(1-7) formation was decreased by a prolylendopeptidase (PEP) inhibitor, but not by a neprilysin inhibitor.
270	22461301	Cleavage of ANG II resulted in partial conversion to ANG-(1-7), a process that was attenuated by an ACE2 inhibitor, as well as by an inhibitor of PEP and prolylcarboxypeptidase.
271	22461301	These results indicate that hGEnCs possess prominent ACE activity, but modest ANG II-metabolizing activity compared with that of podocytes.
272	22461301	PEP, ACE2, prolylcarboxypeptidase, APN, and aspartyl aminopeptidase are also enzymes contained in hGEnCs that participate in membrane-bound ANG peptide cleavage.