h-89 and pimagedine

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

Other Studies

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

Article	Year
N(omega)-nitro-L-arginine inhibits inducible HSP-70 via Ca(2+), PKC, and PKA in human intestinal epithelial T84 cells. American journal of physiology. Gastrointestinal and liver physiology, 2002, Volume: 282, Issue:3 The nitric oxide (NO) synthase inhibitor N(omega)-nitro-L-arginine (L-NNA) inhibits heat stress (HS)-induced NO production and the inducible 70-kDa heat shock protein (HSP-70i) in many rodent organs. We used human intestinal epithelial T84 cells to characterize the inhibitory effect of L-NNA on HS-induced HSP-70i expression. Intracellular Ca(2+) concentration ([Ca(2+)](i)) was measured using fura-2, and protein kinase C (PKC), and PKA activities were determined. HS increased HSP-70i mRNA and protein in T84 cells exposed to 45 degrees C for 10 min and allowed to recover for 6 h. L-NNA treatment for 1 h before HS inhibited the induction of HSP-70i mRNA and protein, with an IC(50) of 0.0471 +/- 0.0007 microM. Because the HS-induced increase in HSP-70i mRNA and protein is Ca(2+) dependent, we measured [Ca(2+)](i) after treating cells with L-NNA. L-NNA at 100 microM significantly decreased resting [Ca(2+)](i). Likewise, treatment with 1 microM GF-109203X or H-89 (inhibitors of PKC and PKA, respectively) for 30 min also significantly decreased [Ca(2+)](i) and inhibited HS-induced increase in HSP-70i. GF-109203X- or H-89-treated cells failed to respond to L-NNA by further decreasing [Ca(2+)](i) and HSP-70i. L-NNA effectively blocked heat shock factor-1 (HSF1) translocation from the cytosol to the nucleus, a process requiring PKC phosphorylation. These results suggest that L-NNA inhibits HSP-70i by reducing [Ca(2+)](i) and decreasing PKC and PKA activity, thereby blocking HSF1 translocation from the cytosol to the nucleus. Topics: Calcium; Cell Nucleus; Chelating Agents; Colonic Neoplasms; Cyclic AMP-Dependent Protein Kinases; Cycloheximide; Cytosol; Dactinomycin; DNA-Binding Proteins; Egtazic Acid; Enzyme Inhibitors; Guanidines; Heat Shock Transcription Factors; Hot Temperature; HSP70 Heat-Shock Proteins; Humans; Indoles; Intestinal Mucosa; Intestines; Isoquinolines; Maleimides; Nitric Oxide; Nitric Oxide Synthase; Nitroarginine; Protein Kinase C; Protein Kinases; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Sulfonamides; Transcription Factors; Tumor Cells, Cultured	2002

Article

Year

N(omega)-nitro-L-arginine inhibits inducible HSP-70 via Ca(2+), PKC, and PKA in human intestinal epithelial T84 cells.

American journal of physiology. Gastrointestinal and liver physiology, 2002, Volume: 282, Issue:3

The nitric oxide (NO) synthase inhibitor N(omega)-nitro-L-arginine (L-NNA) inhibits heat stress (HS)-induced NO production and the inducible 70-kDa heat shock protein (HSP-70i) in many rodent organs. We used human intestinal epithelial T84 cells to characterize the inhibitory effect of L-NNA on HS-induced HSP-70i expression. Intracellular Ca(2+) concentration ([Ca(2+)](i)) was measured using fura-2, and protein kinase C (PKC), and PKA activities were determined. HS increased HSP-70i mRNA and protein in T84 cells exposed to 45 degrees C for 10 min and allowed to recover for 6 h. L-NNA treatment for 1 h before HS inhibited the induction of HSP-70i mRNA and protein, with an IC(50) of 0.0471 +/- 0.0007 microM. Because the HS-induced increase in HSP-70i mRNA and protein is Ca(2+) dependent, we measured [Ca(2+)](i) after treating cells with L-NNA. L-NNA at 100 microM significantly decreased resting [Ca(2+)](i). Likewise, treatment with 1 microM GF-109203X or H-89 (inhibitors of PKC and PKA, respectively) for 30 min also significantly decreased [Ca(2+)](i) and inhibited HS-induced increase in HSP-70i. GF-109203X- or H-89-treated cells failed to respond to L-NNA by further decreasing [Ca(2+)](i) and HSP-70i. L-NNA effectively blocked heat shock factor-1 (HSF1) translocation from the cytosol to the nucleus, a process requiring PKC phosphorylation. These results suggest that L-NNA inhibits HSP-70i by reducing [Ca(2+)](i) and decreasing PKC and PKA activity, thereby blocking HSF1 translocation from the cytosol to the nucleus.

Topics: Calcium; Cell Nucleus; Chelating Agents; Colonic Neoplasms; Cyclic AMP-Dependent Protein Kinases; Cycloheximide; Cytosol; Dactinomycin; DNA-Binding Proteins; Egtazic Acid; Enzyme Inhibitors; Guanidines; Heat Shock Transcription Factors; Hot Temperature; HSP70 Heat-Shock Proteins; Humans; Indoles; Intestinal Mucosa; Intestines; Isoquinolines; Maleimides; Nitric Oxide; Nitric Oxide Synthase; Nitroarginine; Protein Kinase C; Protein Kinases; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Sulfonamides; Transcription Factors; Tumor Cells, Cultured

2002