PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20543077-8 2010 These results suggest that ALDH2 plays an important role in the bioactivation of GTN and nitrite in the pulmonary and systemic vascular beds and that the reduction of nitrite to vasoactive NO does not play an important role in mediating vasodilator responses to GTN in the intact chest rat. Nitroglycerin 81-84 aldehyde dehydrogenase 2 family member Rattus norvegicus 27-32 21757654-9 2011 GTN-induced decrease in Ser1177, increase in Thr495 phosphorylation or S-glutathionylation of eNOS, and decrease in mitochondrial aldehyde dehydrogenase expression were normalized by telmisartan. Nitroglycerin 0-3 aldehyde dehydrogenase 2 family member Rattus norvegicus 116-152 20543077-0 2010 Mitochondrial aldehyde dehydrogenase mediates vasodilator responses of glyceryl trinitrate and sodium nitrite in the pulmonary vascular bed of the rat. Nitroglycerin 71-90 aldehyde dehydrogenase 2 family member Rattus norvegicus 0-36 20543077-1 2010 It has been reported that mitochondrial aldehyde dehydrogenase (ALDH2) catalyzes the formation of glyceryl dinitrate and inorganic nitrite from glyceryl trinitrate (GTN), leading to an increase in cGMP and vasodilation in the coronary and systemic vascular beds. Nitroglycerin 144-163 aldehyde dehydrogenase 2 family member Rattus norvegicus 26-62 20543077-1 2010 It has been reported that mitochondrial aldehyde dehydrogenase (ALDH2) catalyzes the formation of glyceryl dinitrate and inorganic nitrite from glyceryl trinitrate (GTN), leading to an increase in cGMP and vasodilation in the coronary and systemic vascular beds. Nitroglycerin 144-163 aldehyde dehydrogenase 2 family member Rattus norvegicus 64-69 20543077-1 2010 It has been reported that mitochondrial aldehyde dehydrogenase (ALDH2) catalyzes the formation of glyceryl dinitrate and inorganic nitrite from glyceryl trinitrate (GTN), leading to an increase in cGMP and vasodilation in the coronary and systemic vascular beds. Nitroglycerin 165-168 aldehyde dehydrogenase 2 family member Rattus norvegicus 26-62 20543077-1 2010 It has been reported that mitochondrial aldehyde dehydrogenase (ALDH2) catalyzes the formation of glyceryl dinitrate and inorganic nitrite from glyceryl trinitrate (GTN), leading to an increase in cGMP and vasodilation in the coronary and systemic vascular beds. Nitroglycerin 165-168 aldehyde dehydrogenase 2 family member Rattus norvegicus 64-69 22465477-5 2012 The results with allopurinol and cyanamide suggest that only mitochondrial aldehyde dehydrogenase is involved in the bioactivation of GTN, sodium nitrite, and GSNO, whereas both pathways are involved in the bioactivation of nitrite anion in the intact rat. Nitroglycerin 134-137 aldehyde dehydrogenase 2 family member Rattus norvegicus 61-97 19576883-0 2009 Comparing the role of glutathione-S-transferase and mitochondrial aldehyde dehydrogenase in nitroglycerin biotransformation and the correlation with calcitonin gene-related peptide. Nitroglycerin 92-105 aldehyde dehydrogenase 2 family member Rattus norvegicus 52-88 19576883-1 2009 Both glutathione-S-transferase (GST) and mitochondrial aldehyde dehydrogenase (ALDH-2) have been reported to participate in the biotransformation of nitroglycerin. Nitroglycerin 149-162 aldehyde dehydrogenase 2 family member Rattus norvegicus 41-77 19576883-1 2009 Both glutathione-S-transferase (GST) and mitochondrial aldehyde dehydrogenase (ALDH-2) have been reported to participate in the biotransformation of nitroglycerin. Nitroglycerin 149-162 aldehyde dehydrogenase 2 family member Rattus norvegicus 79-85 19576883-13 2009 The present results suggest that both GST and ALDH-2 are involved in nitroglycerin action while ALDH-2 plays a major role, and the change of CGRP contents closely correlates with the biotransformation of nitroglycerin. Nitroglycerin 69-82 aldehyde dehydrogenase 2 family member Rattus norvegicus 46-52 17541025-1 2007 OBJECTIVE: Nitrate tolerance is likely attributable to an increased production of reactive oxygen species (ROS) leading to an inhibition of the mitochondrial aldehyde dehydrogenase (ALDH-2), representing the nitroglycerin (GTN) and pentaerythrityl tetranitrate (PETN) bioactivating enzyme, and to impaired nitric oxide bioactivity and signaling. Nitroglycerin 208-221 aldehyde dehydrogenase 2 family member Rattus norvegicus 144-180 17541025-1 2007 OBJECTIVE: Nitrate tolerance is likely attributable to an increased production of reactive oxygen species (ROS) leading to an inhibition of the mitochondrial aldehyde dehydrogenase (ALDH-2), representing the nitroglycerin (GTN) and pentaerythrityl tetranitrate (PETN) bioactivating enzyme, and to impaired nitric oxide bioactivity and signaling. Nitroglycerin 208-221 aldehyde dehydrogenase 2 family member Rattus norvegicus 182-188 17541025-1 2007 OBJECTIVE: Nitrate tolerance is likely attributable to an increased production of reactive oxygen species (ROS) leading to an inhibition of the mitochondrial aldehyde dehydrogenase (ALDH-2), representing the nitroglycerin (GTN) and pentaerythrityl tetranitrate (PETN) bioactivating enzyme, and to impaired nitric oxide bioactivity and signaling. Nitroglycerin 223-226 aldehyde dehydrogenase 2 family member Rattus norvegicus 144-180 17541025-1 2007 OBJECTIVE: Nitrate tolerance is likely attributable to an increased production of reactive oxygen species (ROS) leading to an inhibition of the mitochondrial aldehyde dehydrogenase (ALDH-2), representing the nitroglycerin (GTN) and pentaerythrityl tetranitrate (PETN) bioactivating enzyme, and to impaired nitric oxide bioactivity and signaling. Nitroglycerin 223-226 aldehyde dehydrogenase 2 family member Rattus norvegicus 182-188 16244377-2 2005 A commonly used NBV, glyceryl trinitrate (GTN) is bioactivated by mitochondrial, class 2 aldehyde dehydrogenase (ALDH2). Nitroglycerin 21-40 aldehyde dehydrogenase 2 family member Rattus norvegicus 113-118 17493633-16 2007 Furthermore, reduced ALDH-2 activity and expression leads to decreased NTG bioconversion. Nitroglycerin 71-74 aldehyde dehydrogenase 2 family member Rattus norvegicus 21-27 17102135-3 2007 We have recently shown that mitochondria are an important source of nitroglycerin-induced oxidants and that the nitroglycerin-bioactivating mitochondrial aldehyde dehydrogenase is oxidatively inactivated in the setting of tolerance. Nitroglycerin 112-125 aldehyde dehydrogenase 2 family member Rattus norvegicus 140-176 16244377-2 2005 A commonly used NBV, glyceryl trinitrate (GTN) is bioactivated by mitochondrial, class 2 aldehyde dehydrogenase (ALDH2). Nitroglycerin 42-45 aldehyde dehydrogenase 2 family member Rattus norvegicus 113-118 16244377-4 2005 The GTN bioactivation step, however, inac-tivates ALDH2 and may alter the metabolism of these aldehydes. Nitroglycerin 4-7 aldehyde dehydrogenase 2 family member Rattus norvegicus 50-55 16244377-7 2005 GTN (1 microM) inhibited ALDH2 activity (55 +/- 6% of control) and ablated ALDH3 activity. Nitroglycerin 0-3 aldehyde dehydrogenase 2 family member Rattus norvegicus 25-30 15331769-1 2004 Mitochondrial aldehyde dehydrogenase (ALDH-2) was recently identified to be essential for the bioactivation of glyceryl trinitrate (GTN). Nitroglycerin 111-130 aldehyde dehydrogenase 2 family member Rattus norvegicus 0-36 15331769-1 2004 Mitochondrial aldehyde dehydrogenase (ALDH-2) was recently identified to be essential for the bioactivation of glyceryl trinitrate (GTN). Nitroglycerin 111-130 aldehyde dehydrogenase 2 family member Rattus norvegicus 38-44 15331769-1 2004 Mitochondrial aldehyde dehydrogenase (ALDH-2) was recently identified to be essential for the bioactivation of glyceryl trinitrate (GTN). Nitroglycerin 132-135 aldehyde dehydrogenase 2 family member Rattus norvegicus 0-36 15331769-1 2004 Mitochondrial aldehyde dehydrogenase (ALDH-2) was recently identified to be essential for the bioactivation of glyceryl trinitrate (GTN). Nitroglycerin 132-135 aldehyde dehydrogenase 2 family member Rattus norvegicus 38-44 15331769-6 2004 In contrast, mitochondrial ALDH-2 esterase activity was not affected by PETN and its metabolites, whereas it was inhibited by benomyl, GTN applied in vitro and in vivo, and some sulfhydryl oxidants. Nitroglycerin 135-138 aldehyde dehydrogenase 2 family member Rattus norvegicus 27-33 15331769-7 2004 The bioactivation-related metabolism of GTN to glyceryl-1,2-dinitrate by isolated RAW macrophages was reduced by the ALDH-2 inhibitors benomyl and daidzin, as well as by GTN at concentrations >1 microM. Nitroglycerin 40-43 aldehyde dehydrogenase 2 family member Rattus norvegicus 117-123 15331769-8 2004 We conclude that mitochondrial ALDH-2, specifically its esterase activity, is required for the bioactivation of the organic nitrates with high vasodilator potency, such as GTN and PETN, but not for the less potent nitrates. Nitroglycerin 172-175 aldehyde dehydrogenase 2 family member Rattus norvegicus 31-37 15331769-9 2004 It is interesting that ALDH-2 esterase activity was inhibited by GTN only, not by the other nitrates tested. Nitroglycerin 65-68 aldehyde dehydrogenase 2 family member Rattus norvegicus 23-29 14573760-4 2003 However, the mitochondrial aldehyde dehydrogenase (ALDH2) is inhibited in GTN-tolerant tissues and produces NO2- from GTN, which is proposed to be converted to NO within mitochondria. Nitroglycerin 118-121 aldehyde dehydrogenase 2 family member Rattus norvegicus 13-49 14755345-2 2004 The extent to which ALDH-2 contributes to GTN tolerance (impaired relaxation to GTN) and cross-tolerance (impaired endothelium-dependent relaxation) in vivo remain to be elucidated. Nitroglycerin 80-83 aldehyde dehydrogenase 2 family member Rattus norvegicus 20-26 14755345-5 2004 Further, whereas in control vessels, multiple inhibitors and substrates of ALDH-2 reduced both GTN-stimulation of cGKI and GTN-induced vasodilation, these agents had little effect on tolerant vessels. Nitroglycerin 95-98 aldehyde dehydrogenase 2 family member Rattus norvegicus 75-81 14755345-5 2004 Further, whereas in control vessels, multiple inhibitors and substrates of ALDH-2 reduced both GTN-stimulation of cGKI and GTN-induced vasodilation, these agents had little effect on tolerant vessels. Nitroglycerin 123-126 aldehyde dehydrogenase 2 family member Rattus norvegicus 75-81 14755345-0 2004 Central role of mitochondrial aldehyde dehydrogenase and reactive oxygen species in nitroglycerin tolerance and cross-tolerance. Nitroglycerin 84-97 aldehyde dehydrogenase 2 family member Rattus norvegicus 16-52 14755345-1 2004 Recent studies suggest that mitochondrial aldehyde dehydrogenase (ALDH-2) plays a central role in the process of nitroglycerin (glyceryl trinitrate, GTN) biotransformation in vivo and that its inhibition accounts for mechanism-based tolerance in vitro. Nitroglycerin 113-126 aldehyde dehydrogenase 2 family member Rattus norvegicus 28-64 14755345-1 2004 Recent studies suggest that mitochondrial aldehyde dehydrogenase (ALDH-2) plays a central role in the process of nitroglycerin (glyceryl trinitrate, GTN) biotransformation in vivo and that its inhibition accounts for mechanism-based tolerance in vitro. Nitroglycerin 113-126 aldehyde dehydrogenase 2 family member Rattus norvegicus 66-72 14755345-1 2004 Recent studies suggest that mitochondrial aldehyde dehydrogenase (ALDH-2) plays a central role in the process of nitroglycerin (glyceryl trinitrate, GTN) biotransformation in vivo and that its inhibition accounts for mechanism-based tolerance in vitro. Nitroglycerin 128-147 aldehyde dehydrogenase 2 family member Rattus norvegicus 28-64 14755345-1 2004 Recent studies suggest that mitochondrial aldehyde dehydrogenase (ALDH-2) plays a central role in the process of nitroglycerin (glyceryl trinitrate, GTN) biotransformation in vivo and that its inhibition accounts for mechanism-based tolerance in vitro. Nitroglycerin 128-147 aldehyde dehydrogenase 2 family member Rattus norvegicus 66-72 14755345-1 2004 Recent studies suggest that mitochondrial aldehyde dehydrogenase (ALDH-2) plays a central role in the process of nitroglycerin (glyceryl trinitrate, GTN) biotransformation in vivo and that its inhibition accounts for mechanism-based tolerance in vitro. Nitroglycerin 149-152 aldehyde dehydrogenase 2 family member Rattus norvegicus 28-64 14755345-1 2004 Recent studies suggest that mitochondrial aldehyde dehydrogenase (ALDH-2) plays a central role in the process of nitroglycerin (glyceryl trinitrate, GTN) biotransformation in vivo and that its inhibition accounts for mechanism-based tolerance in vitro. Nitroglycerin 149-152 aldehyde dehydrogenase 2 family member Rattus norvegicus 66-72 14755345-2 2004 The extent to which ALDH-2 contributes to GTN tolerance (impaired relaxation to GTN) and cross-tolerance (impaired endothelium-dependent relaxation) in vivo remain to be elucidated. Nitroglycerin 42-45 aldehyde dehydrogenase 2 family member Rattus norvegicus 20-26 14573760-4 2003 However, the mitochondrial aldehyde dehydrogenase (ALDH2) is inhibited in GTN-tolerant tissues and produces NO2- from GTN, which is proposed to be converted to NO within mitochondria. Nitroglycerin 74-77 aldehyde dehydrogenase 2 family member Rattus norvegicus 13-49 14573760-4 2003 However, the mitochondrial aldehyde dehydrogenase (ALDH2) is inhibited in GTN-tolerant tissues and produces NO2- from GTN, which is proposed to be converted to NO within mitochondria. Nitroglycerin 74-77 aldehyde dehydrogenase 2 family member Rattus norvegicus 51-56 14573760-4 2003 However, the mitochondrial aldehyde dehydrogenase (ALDH2) is inhibited in GTN-tolerant tissues and produces NO2- from GTN, which is proposed to be converted to NO within mitochondria. Nitroglycerin 118-121 aldehyde dehydrogenase 2 family member Rattus norvegicus 51-56 14573760-7 2003 The in vivo protocol resulted in almost complete inhibition of ALDH2 activity and GTN biotransformation in hepatic mitochondria, indicating that long-term GTN exposure results in inactivation of the enzyme. Nitroglycerin 155-158 aldehyde dehydrogenase 2 family member Rattus norvegicus 63-68 14573760-10 2003 Immunoblot analysis indicated that the majority of vascular ALDH2 is present in the cytoplasm, suggesting that mitochondrial biotransformation of GTN by ALDH2 plays a minor role in the overall vascular biotransformation of GTN by this enzyme. Nitroglycerin 146-149 aldehyde dehydrogenase 2 family member Rattus norvegicus 153-158 14573760-10 2003 Immunoblot analysis indicated that the majority of vascular ALDH2 is present in the cytoplasm, suggesting that mitochondrial biotransformation of GTN by ALDH2 plays a minor role in the overall vascular biotransformation of GTN by this enzyme. Nitroglycerin 223-226 aldehyde dehydrogenase 2 family member Rattus norvegicus 60-65