gedunin and Parkinson-Disease

gedunin has been researched along with Parkinson-Disease* in 1 studies

Other Studies

1 other study(ies) available for gedunin and Parkinson-Disease

Article	Year
Hsp90 Co-chaperone p23 contributes to dopaminergic mitochondrial stress via stabilization of PHD2: Implications for Parkinson's disease. Neurotoxicology, 2018, Volume: 65 The heat shock factor 90 (hsp90) complex has long been associated with neuropathological phenotypes linked to Parkinson's disease (PD) and its inhibition is neuroprotective in disease models. Hsp90 is conventionally believed to act by suppressing induction of hsp70. Here, we report a novel hsp70-independent mechanism by which Hsp90 may also contribute to PD-associated neuropathology. We previously reported that inhibition of the enzyme prolyl hydroxylase domain 2 (PHD2) in conjunction with increases in hypoxia-inducible factor 1 alpha (HIF1α) results in protection of vulnerable dopaminergic substantia nigra pars compacta (DAergic SNpc) neurons in in vitro and in vivo models of PD. We discovered an increased interaction between PHD2 and the p23:Hsp90 chaperone complex in response to mitochondrial stress elicited by the mitochondrial neurotoxin 1-methyl-4-phenylpyridine (MPP Topics: 1-Methyl-4-phenylpyridinium; Animals; Cells, Cultured; Dopaminergic Neurons; Gene Knockdown Techniques; HSP90 Heat-Shock Proteins; Hypoxia-Inducible Factor-Proline Dioxygenases; Limonins; Mitochondria; Molecular Chaperones; Neuroprotective Agents; Parkinson Disease; Procollagen-Proline Dioxygenase; Rats	2018

Article

Year

Hsp90 Co-chaperone p23 contributes to dopaminergic mitochondrial stress via stabilization of PHD2: Implications for Parkinson's disease.

Neurotoxicology, 2018, Volume: 65

The heat shock factor 90 (hsp90) complex has long been associated with neuropathological phenotypes linked to Parkinson's disease (PD) and its inhibition is neuroprotective in disease models. Hsp90 is conventionally believed to act by suppressing induction of hsp70. Here, we report a novel hsp70-independent mechanism by which Hsp90 may also contribute to PD-associated neuropathology. We previously reported that inhibition of the enzyme prolyl hydroxylase domain 2 (PHD2) in conjunction with increases in hypoxia-inducible factor 1 alpha (HIF1α) results in protection of vulnerable dopaminergic substantia nigra pars compacta (DAergic SNpc) neurons in in vitro and in vivo models of PD. We discovered an increased interaction between PHD2 and the p23:Hsp90 chaperone complex in response to mitochondrial stress elicited by the mitochondrial neurotoxin 1-methyl-4-phenylpyridine (MPP

Topics: 1-Methyl-4-phenylpyridinium; Animals; Cells, Cultured; Dopaminergic Neurons; Gene Knockdown Techniques; HSP90 Heat-Shock Proteins; Hypoxia-Inducible Factor-Proline Dioxygenases; Limonins; Mitochondria; Molecular Chaperones; Neuroprotective Agents; Parkinson Disease; Procollagen-Proline Dioxygenase; Rats

2018