title: Taurine exerts robust protection against hypoxia and oxygen/glucose deprivation in human neuroblastoma cell culture.
abstract: Stroke is one of the leading causes of mortality and disability worldwide. There is no effective treatment for stroke despite extensive research. Taurine is a free amino acid which is present at high concentrations in a range of organs including the brain, heart, and retina in mammalian systems. It had been shown that taurine can significantly increase cell survival under stroke conditions using both in vivo and in vitro models. Recently, we have found that several agents including granulocyte colony-stimulating factor (G-CSF), a stem cell enhancer and facilitator;S-methyl-N-diethylthiolcarbamate sulfoxide (DETC-MeSO), an NMDA receptor partial antagonist; sulindac, a potent antioxidant; and taurine, a neuroprotectant and calcium regulator, are effective in protecting against stroke-induced neuronal injury when used alone or in combination in both animal and tissue/cell culture models. In this chapter, we demonstrate that taurine can protect human neuroblastoma cells measured by ATP assay under conditions of hypoxia or oxygen/glucose deprivation (OGD). In addition, we found that taurine exerts its protective function by suppressing the OGD-induced upregulation of endoplasmic reticulum (ER) stress markers and proapoptotic proteins. A model depicting the mode of action of taurine in protecting neuroblastoma cells under OGD conditions is presented.
authors: Department of Biomedical Science, Florida Atlantic University, Boca Raton, FL 33431, USA. chenpochih1979@gmail.com
authors: Po-Chih
authors: PC
authors: Chen
authors: Chunliu
authors: C
authors: Pan
authors: Payam M
authors: PM
authors: Gharibani
authors: Howard
authors: H
authors: Prentice
authors: Jang-Yen
authors: JY
authors: Wu
mesh_terms: D051701:Activating Transcription Factor 4 / Q000378:metabolism; D051017:Apoptosis Regulatory Proteins / Q000378:metabolism; D015687:Cell Hypoxia / Q000187:drug effects; D002470:Cell Survival / Q000187:drug effects; D019610:Cytoprotection / Q000187:drug effects*; D004268:DNA-Binding Proteins / Q000378:metabolism; D004722:Endoribonucleases / Q000378:metabolism; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism; D005947:Glucose / Q000172:deficiency*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008954:Models, Biological; D009447:Neuroblastoma / Q000378:metabolism / Q000473:pathology*; D018696:Neuroprotective Agents / Q000494:pharmacology* / Q000627:therapeutic use; D010100:Oxygen / Q000378:metabolism*; D054645:Protein Phosphatase 1; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D000071701:Regulatory Factor X Transcription Factors; D013312:Stress, Physiological / Q000187:drug effects; D013654:Taurine / Q000494:pharmacology*; D014157:Transcription Factors / Q000378:metabolism; D014407:Tumor Cells, Cultured
chemical_list: C497109:ATF4 protein, human; D051017:Apoptosis Regulatory Proteins; C438378:BBC3 protein, human; D004268:DNA-Binding Proteins; D015852:Eukaryotic Initiation Factor-2; D008565:Membrane Proteins; D018696:Neuroprotective Agents; D011518:Proto-Oncogene Proteins; D000071701:Regulatory Factor X Transcription Factors; D014157:Transcription Factors; D051701:Activating Transcription Factor 4; D013654:Taurine; C403982:ERN2 protein, human; D017346:Protein Serine-Threonine Kinases; D004722:Endoribonucleases; C087519:PPP1R15A protein, human; D054645:Protein Phosphatase 1; D005947:Glucose; D010100:Oxygen