esculetin and pyrazolanthrone

esculetin has been researched along with pyrazolanthrone* in 1 studies

Other Studies

1 other study(ies) available for esculetin and pyrazolanthrone

Article	Year
Esculetin induces mitochondria-mediated apoptosis in 3T3-L1 adipocytes. Apoptosis : an international journal on programmed cell death, 2006, Volume: 11, Issue:8 Adipose tissue mass is determined by the volume and the number of adipocytes and is subjected to homeostatic regulation involving cell death mechanisms. We investigated the effects of esculetin, a coumarin compound, on apoptotic signaling in 3T3-L1 adipocytes. Esculetin treatment induced an increase in expression of Bax with a concomitant decrease of Bcl-2 in a time-dependent manner. Esculetin treatment also resulted in translocation of cytochrome c from mitochondria to cytosol and cleavage of 116 kDa poly(ADP-ribose) polymerase (PARP)-1, resulting in the accumulation of an 85 kDa cleavage product in a caspase-dependent manner. Furthermore, esculetin selectively altered the phosphorylation state of members of the MAPK superfamily, causing dephosphorylation of extracellular signal-regulating kinase 1/2 (ERK1/2) and hyperphosphorylation of c-Jun-N-terminal kinase (JNK). In addition, an inhibitor of the JNK MAP kinase pathway, SP600125, reduced esculetin-induced cytochrome c release. These results indicate that esculetin mediated adipocyte apoptosis involves the mitochondrial pathway. Esculetin thus decreases adipocyte number by initiating this apoptotic process in 3T3-L1 adipocytes. Topics: 3T3-L1 Cells; Animals; Anthracenes; Apoptosis; Caspase 3; Cell Survival; Cytochromes c; JNK Mitogen-Activated Protein Kinases; Mice; Mitogen-Activated Protein Kinases; Poly (ADP-Ribose) Polymerase-1; Poly(ADP-ribose) Polymerases; Proto-Oncogene Proteins c-bcl-2; Umbelliferones	2006

Article

Year

Esculetin induces mitochondria-mediated apoptosis in 3T3-L1 adipocytes.

Apoptosis : an international journal on programmed cell death, 2006, Volume: 11, Issue:8

Adipose tissue mass is determined by the volume and the number of adipocytes and is subjected to homeostatic regulation involving cell death mechanisms. We investigated the effects of esculetin, a coumarin compound, on apoptotic signaling in 3T3-L1 adipocytes. Esculetin treatment induced an increase in expression of Bax with a concomitant decrease of Bcl-2 in a time-dependent manner. Esculetin treatment also resulted in translocation of cytochrome c from mitochondria to cytosol and cleavage of 116 kDa poly(ADP-ribose) polymerase (PARP)-1, resulting in the accumulation of an 85 kDa cleavage product in a caspase-dependent manner. Furthermore, esculetin selectively altered the phosphorylation state of members of the MAPK superfamily, causing dephosphorylation of extracellular signal-regulating kinase 1/2 (ERK1/2) and hyperphosphorylation of c-Jun-N-terminal kinase (JNK). In addition, an inhibitor of the JNK MAP kinase pathway, SP600125, reduced esculetin-induced cytochrome c release. These results indicate that esculetin mediated adipocyte apoptosis involves the mitochondrial pathway. Esculetin thus decreases adipocyte number by initiating this apoptotic process in 3T3-L1 adipocytes.

Topics: 3T3-L1 Cells; Animals; Anthracenes; Apoptosis; Caspase 3; Cell Survival; Cytochromes c; JNK Mitogen-Activated Protein Kinases; Mice; Mitogen-Activated Protein Kinases; Poly (ADP-Ribose) Polymerase-1; Poly(ADP-ribose) Polymerases; Proto-Oncogene Proteins c-bcl-2; Umbelliferones

2006