S-Nitrosylation at Cysteine 498 of c-Src Tyrosine Kinase Regulates Nitric Oxide-mediated Cell Invasion

Rahman, Mohammad Aminur; Senga, Takeshi; Ito, Satoko; Hyodo, Toshinori; Hasegawa, Hitoki; Hamaguchi, Michinari

doi:10.1074/jbc.m109.059782

Cited by 101 publications

(112 citation statements)

References 29 publications

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“…It has previously been reported by this group that the enhancement of cell invasion caused by nitric oxide stimulation is mediated by Src and FAK kinase activation in MCF-7 breast cancer cells (23). To expand on these findings, the current study aimed to examine the role Src and FAK serve in the IL-1β-mediated cell invasion of MCF-7 cells, and identify whether Src and FAK kinase are involved in MMP-9 production and cell invasion.…”

Section: Introductionmentioning

confidence: 99%

Interleukin-1β activates focal adhesion kinase and Src to induce matrix metalloproteinase-9 production and invasion of MCF-7 breast cancer cells

2016

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Abstract. Interleukin-1β (IL-1b) is a pleiotropic cytokine that is important in tumor progression and invasion. Matrix metalloproteinase-9 (MMP-9), which is a secreted matrix-degrading enzyme, is one of the key regulators of tumor invasion and metastasis. The current report indicated that IL-1b promotes MMP-9 production and cell invasion in non-metastatic MCF-7 breast cancer cells. IL-1b activated focal adhesion kinase (FAK) and proto-oncogene tyrosine-protein kinase Src (Src). Moreover, inhibiting the Src/FAK pathway reduced the IL-1b-induced production of MMP-9 and cell invasion. To investigate the functional role of FAK in MMP-9 production cell lines expressing mutant FAK in FAK knock-out mouse fibroblasts were generated. In wild-type FAK-expressing cells, MMP-9 production was induced by IL-1b stimulation. By contrast, IL-1b-induced MMP-9 production was abrogated in FAK knock-out, FAK Y397F, FAK Y925F, and kinase dead mutant-expressing cells. Therefore the results of the current study indicate that FAK and Src kinases are activated by IL-1b and play a critical role in MMP-9 production and tumor cell invasion.

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Section: Introductionmentioning

confidence: 99%

Interleukin-1β activates focal adhesion kinase and Src to induce matrix metalloproteinase-9 production and invasion of MCF-7 breast cancer cells

2016

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“…Cadherin junctions can be noted from connections between cells, and changes in them are associated with rupture of cancer cells and metastases Wang and Shang, 2012). Free radicals are derived from some estrogen hormones such as the radical Panoxyl of beta -estradiol (Rahman et al, 2010).…”

Section: Oxidative Stress and Breast Cancermentioning

confidence: 99%

Roles of Oxidative Stress in the Development and Progression of Breast Cancer

Nourazarian¹,

Kangari²,

Salmaninejad³

2014

Asian Pacific Journal of Cancer Prevention

152

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Oxidative stress is caused by an imbalance in the redox status of the body. In such a state, increase of free radicals in the body can lead to tissue damage. One of the most important species of free radicals is reactive oxygen species (ROS) produced by various metabolic pathways, including aerobic metabolism in the mitochondrial respiratory chain. It plays a critical role in the initiation and progression of various types of cancers. ROS affects different signaling pathways, including growth factors and mitogenic pathways, and controls many cellular processes, including cell proliferation, and thus stimulates the uncontrolled growth of cells which encourages the development of tumors and begins the process of carcinogenesis. Increased oxidative stress caused by reactive species can reduce the body's antioxidant defense against angiogenesis and metastasis in cancer cells. These processes are main factors in the development of cancer. Bimolecular reactions cause free radicals in which create such compounds as malondialdehyde (MDA) and hydroxyguanosine. These substances can be used as indicators of cancer. In this review, free radicals as oxidizing agents, antioxidants as the immune system, and the role of oxidative stress in cancer, particularly breast cancer, have been investigated in the hope that better identification of the factors involved in the occurrence and spread of cancer will improve the identification of treatment goals.

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“…Under dynamic regulation by the NO signaling pathway, S-nitrosylation of a protein can modify its activity or function. For example, it has been reported that S-nitrosylation is important for regulating the catalytic activity of various kinases, including G protein-coupled receptor kinase 2, Akt/protein kinase B, Src kinase, inhibitory B kinase, or Ca 2ϩ /calmodulin-dependent protein kinase II (Reynaert et al, 2004;Yasukawa et al, 2005;Whalen et al, 2007;Song et al, 2008;Rahman et al, 2010). Whereas NO signaling pathway is one of the key regulators in a wide array of neurodevelopmental processes, including neuronal differentiation, neuronal survival, and synaptic plasticity (Guix et al, 2005), deregulation of this pathway has been implicated in the pathogenesis of neurological disorders such as Alzheimer's disease, Parkinson's disease, and stroke (Chung, 2006).…”

Section: Introductionmentioning

confidence: 99%

S-Nitrosylation of Cyclin-Dependent Kinase 5 (Cdk5) Regulates Its Kinase Activity and Dendrite Growth During Neuronal Development

Zhang¹,

Yu²,

Tsang³

et al. 2010

J. Neurosci.

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Precise regulation of cyclin-dependent kinase 5 (Cdk5), a member of the cyclin-dependent kinase family, is critical for proper neuronal development and functions. Cdk5 is activated through its association with the neuron-specific activator p35 or p39. Nonetheless, how its kinase activity is regulated in neurons is not well understood. In this study, we found that Cdk5 activity is regulated by S-nitrosylation, a post-translational modification of protein that affects a plethora of neuronal functions. S-nitrosylation of Cdk5 occurs at Cys83, which is one of the critical amino acids within the ATP-binding pocket of the kinase. Upon S-nitrosylation, Cdk5 exhibits reduced kinase activity, whereas mutation of Cys83 to Ala on Cdk5 renders the kinase refractory to such inhibition. Importantly, S-nitrosylated Cdk5 can be detected in the mouse brain, and blocking the S-nitrosylation of Cdk5 in cultured hippocampal neurons enhances dendritic growth and branching. Together, our findings reveal an important role of S-nitrosylation in regulating Cdk5 kinase activity and dendrite growth in neurons during development.

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S-Nitrosylation at Cysteine 498 of c-Src Tyrosine Kinase Regulates Nitric Oxide-mediated Cell Invasion

Cited by 101 publications

References 29 publications

Interleukin-1β activates focal adhesion kinase and Src to induce matrix metalloproteinase-9 production and invasion of MCF-7 breast cancer cells

Interleukin-1β activates focal adhesion kinase and Src to induce matrix metalloproteinase-9 production and invasion of MCF-7 breast cancer cells

Roles of Oxidative Stress in the Development and Progression of Breast Cancer

S-Nitrosylation of Cyclin-Dependent Kinase 5 (Cdk5) Regulates Its Kinase Activity and Dendrite Growth During Neuronal Development

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