h-89 and oxadin

h-89 has been researched along with oxadin* in 1 studies

Other Studies

1 other study(ies) available for h-89 and oxadin

ArticleYear
20-O-β-D-glucopyranosyl-20(S)-protopanaxadiol suppresses UV-Induced MMP-1 expression through AMPK-mediated mTOR inhibition as a downstream of the PKA-LKB1 pathway.
    Journal of cellular biochemistry, 2014, Volume: 115, Issue:10

    Various health effects have been attributed to the ginsenoside metabolite 20-O-β-D-glucopyranosyl-20(S)-protopanaxadiol (GPD); however, its effect on ultraviolet (UV)-induced matrix metalloproteinase (MMP)-1 expression and the mechanism underlying this effect are unknown. We examined the inhibitory effect of GPD on UV-induced MMP-1 expression and its mechanisms in human dermal fibroblasts (HDFs). GPD attenuated UV-induced MMP-1 expression in HDFs and suppressed the UV-induced phosphorylation of mammalian target of rapamycin (mTOR) and p70(S6K) without inhibiting the activity of phosphatidylinositol 3-kinase and Akt, which are well-known upstream kinases of mTOR. GPD augmented the phosphorylation of liver kinase B1 (LKB1) and adenosine monophosphate-activated protein kinase (AMPK), which are inhibitors of mTOR, to a greater extent than UV treatment alone. Similar to GPD, 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5'-monophosphate (AICAR), an activator of AMPK, augmented UV-induced AMPK phosphorylation to a greater extent than UV treatment alone, resulting in the inhibition of MMP-1 expression. AICAR also decreased the phosphorylation of mTOR and p70(S6K). However, compound C, an antagonist of AMPK, increased MMP-1 expression. In HDF cells with AMPK knock-down using shRNA, MMP-1 expression was increased. These results indicate that AMPK activation plays a key role in MMP-1 suppression. Additionally, the cAMP-dependent protein kinase (PKA) inhibitor, H-89, antagonized GPD-mediated MMP-1 suppression via the inhibition of LKB1. Our results suggest that the suppressive activity of GPD on UV-induced MMP-1 expression is due to the activation of AMPK as a downstream of the PKA-LKB1 pathway.

    Topics: Aminoimidazole Carboxamide; AMP-Activated Protein Kinase Kinases; AMP-Activated Protein Kinases; Cell Line; Cyclic AMP-Dependent Protein Kinases; Fibroblasts; Ginsenosides; Humans; Isoquinolines; Matrix Metalloproteinase 1; Oxazines; Phosphatidylinositol 3-Kinase; Phosphorylation; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins c-akt; Ribonucleotides; Ribosomal Protein S6 Kinases, 70-kDa; RNA Interference; RNA, Small Interfering; Sulfonamides; TOR Serine-Threonine Kinases; Ultraviolet Rays

2014