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Start Over Author "Ferdaus Hassan" Journal fems immunology & medical microbiology
2 results on '"Ferdaus Hassan"'

1. MnTBAP, a synthetic metalloporphyrin, inhibits production of tumor necrosis factor-α in lipopolysaccharide-stimulated RAW 264.7 macrophages cells via inhibiting oxidative stress-mediating p38 and SAPK/JNK signaling

Author

Yoshikazu Naiki, Isamu Mori, Takashi Yokochi, Gantsetseg Tumurkhuu, Tomoaki Yoshida, Shamima Islam, Naoki Koide, Jargalsaikhan Dagvadorj, and Ferdaus Hassan

Subjects
Microbiology (medical), MAPK/ERK pathway, MAP Kinase Kinase 4, Metalloporphyrins, p38 mitogen-activated protein kinases, Immunology, Biology, medicine.disease_cause, p38 Mitogen-Activated Protein Kinases, Microbiology, Cell Line, Mice, medicine, Animals, Immunologic Factors, Immunology and Allergy, Protein kinase A, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Tumor Necrosis Factor-alpha, Macrophages, NF-kappa B, General Medicine, Cell biology, Oxidative Stress, Infectious Diseases, Biochemistry, Second messenger system, Phosphorylation, Tumor necrosis factor alpha, Reactive Oxygen Species, Intracellular, Oxidative stress
Abstract

Antioxidants are able to inhibit inflammatory gene expression in response to lipopolysaccharide via down-regulating generation of intracellular reactive oxygen species (ROS) as second messengers. The effect of manganese (III) tetrakis (4-benzoic acid) porphyrin (MnTBAP), a synthetic metalloporphyrin with antioxidant activity, on tumor necrosis factor (TNF)-alpha production in lipopolysaccharide-stimulated RAW 264.7 macrophage cells was examined. MnTBAP prevented the generation of intracellular ROS in lipopolysaccharide-stimulated RAW 264.7 cells and further inhibited lipopolysaccharide-induced TNF-alpha production. MnTBAP exclusively prevented the phosphorylation of p38 mitogen-activated protein kinase (MAPK) and stress-activated protein kinase (SAPK/JNK) whereas it did not affect the phosphorylation and activation of nuclear factor-kappaB and extracellular signal regulated kinase 1/2. MnTBAP was suggested to inhibit lipopolysaccharide-induced TNF-alpha production by the prevention of intracellular ROS generation and subsequent inactivation of p38 MAPK and SAPK/JNK.

Published
2007
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2. Inhibition of extracellular signal-regulated kinase 1/2 augments nitric oxide production in lipopolysaccharide-stimulated RAW264.7 macrophage cells.

Author

Naoki Koide, Hiroyasu Ito, Mya Mya Mu, Tsuyoshi Sugiyama, Ferdaus Hassan, Shamima Islam, Isamu Mori, Tomoaki Yoshida, and Takashi Yokochi

Subjects
EXTRACELLULAR signal-regulated kinases, NITRIC-oxide synthases, LIPOPOLYSACCHARIDES, MACROPHAGES, MITOGEN-activated protein kinase kinase, KINASE inhibitors
Abstract

The present study was conducted to determine effects of U0126, a specific inhibitor of mitogen-activated kinase kinase 1/2, on production of nitric oxide (NO) in RAW264.7 macrophage cells. U0126 significantly enhanced NO production in lipopolysaccharide (LPS) but not CpG DNA or interferon-c-stimulated RAW264.7 cells. In contrast, U0124, a negative control for U0126, did not affect LPS-induced NO production. Further, a series of inhibitors of p38, phosphatidyl-inositol 3-kinase and Janus tyrosine kinase rather caused suppression in LPS-stimulated RAW264.7 cells. U0126 was found to definitely inhibit phosphorylation of extracellular signal-regulated kinase (Erk) 1/2 and augment the levels of inducible type of NO synthase. Antisense oligonucleotides of Erk1/2 also augmented LPS-induced NO production. Inactivation of Erk1/2 by U0126 furthermore inhibited LPS-induced activating protein- 1 activation, but not nuclear factor-jB activation. The results suggest that Erk1/2 might negatively regulate NO production in LPS-stimulated RAW264.7 cells. [ABSTRACT FROM AUTHOR]

Published
2005
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