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3 results on '"Wan Ping Bay"'

1. Selenium Blue-α and -β: turning on the fluorescence of a pyrenyl fluorophore via oxidative cleavage of the Se–C bond by reactive oxygen species

Author

Ming Wah Wong, Dejian Huang, Wei Chen, and Wan Ping Bay

Subjects
chemistry.chemical_classification, Reactive oxygen species, Fluorophore, Organic Chemistry, Hypochlorite, chemistry.chemical_element, Photochemistry, Biochemistry, Fluorescence, Medicinal chemistry, chemistry.chemical_compound, chemistry, Drug Discovery, Pyrene, Oxidative cleavage, Selenium
Abstract

Rapid oxidation of nonfluorescent pyrenyl-CH 2 SeAr (Ar = o -nitrophenyl) by hypochlorite yielded pyrenyl-CH 2 Cl and pyrenyl-CH 2 OH and turns on blue fluorescence, while slow oxidation of pyrenyl-CH 2 SeAr with excess H 2 O 2 leads to pyrenyl-CHO which emits a bluish-green fluorescence. The homolog, pyrenyl-CH 2 CH 2 SeAr′ (Ar′ = o -nitrophenyl) reacts slower with H 2 O 2 and ClO − giving the same product, vinyl pyrene.

Published
2012
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2. RNF13, a RING finger protein, mediates endoplasmic reticulum stress-induced apoptosis through the inositol-requiring enzyme (IRE1α)/c-Jun NH2-terminal kinase pathway

Author

Xiaofeng Gu, Chung Kai Wong, Yi Zhang, Linkang Zhou, Wan Ping Bay, Peng Li, Victor C. Yu, De Li, Yang Liu, Zhongde Ye, and Muhammad Arshad

Subjects
Cell signaling, RNA Splicing, Ubiquitin-Protein Ligases, Apoptosis, Regulatory Factor X Transcription Factors, Biology, Protein Serine-Threonine Kinases, Endoplasmic Reticulum, Biochemistry, Cell Line, Chlorocebus aethiops, Endoribonucleases, medicine, Staurosporine, Animals, Humans, RNA, Messenger, Phosphorylation, Molecular Biology, Transcription factor, Endoplasmic reticulum, JNK Mitogen-Activated Protein Kinases, Cell Biology, Endoplasmic Reticulum Stress, Cell biology, DNA-Binding Proteins, Enzyme Activation, Unfolded protein response, Apoptotic signaling pathway, Signal transduction, Apoptosis Regulatory Proteins, RING Finger Domains, Protein Processing, Post-Translational, medicine.drug, Protein Binding, Signal Transduction, Transcription Factors
Abstract

Disturbance of homeostasis at endoplasmic reticulum (ER) causes stress to cells that in turn triggers an adaptive signaling pathway termed unfolded protein response for the purpose of restoring normal cellular physiology or initiating signaling events leading to apoptosis. Identification of those genes that are involved in the unfolded protein response-mediated apoptotic signaling pathway would be valuable toward elucidating the molecular mechanism underlying the relationship between ER stress and apoptosis. We initiated a genetic screen by using the retroviral insertion mutation system to search for genes whose inactivation confers resistance to apoptosis induction by staurosporine. Using this approach, RING finger protein 13 (RNF13) was identified. Interestingly, RNF13 is highly enriched in ER. RNF13 knockdown cells are resistant to apoptosis and JNK activation triggered by ER stress. Conversely, overexpression of RNF13 induces JNK activation and caspase-dependent apoptosis. The RING and transmembrane domains of RNF13 are both required for its effects on JNK activation and apoptosis. Moreover, systematic analysis of the involvement of individual signaling components in the ER stress pathway using knockdown approach reveals that RNF13 acts upstream of the IRE1α-TRAF2 signaling axis for JNK activation and apoptosis. Finally, RNF13 co-immunoprecipitates with IRE1α, and the intact RING domain is also required for mediating its interaction. Together, our data support a model that RNF13 is a critical mediator for facilitating ER stress-induced apoptosis through the activation of the IRE1α-TRAF2-JNK signaling pathway.

Published
2013

3. RNF13, a RING Finger Protein, Mediates Endoplasmic Reticulum Stress-induced Apoptosis through the Inositol-requiring Enzyme (IRE1α)/c-Jun NH2-terminal Kinase Pathway.

Author

Arshad, Muhammad, Zhongde Ye, Xiaofeng Gu, Chung Kai Wong, Yang Liu, De Li, Linkang Zhou, Yi Zhang, Wan Ping Bay, Yu, Victor C., and Peng Li

Subjects
*HOMEOSTASIS, *ENDOPLASMIC reticulum, *APOPTOSIS, *STAUROSPORINE, *MEMBRANE proteins
Abstract

Disturbance of homeostasis at endoplasmic reticulum (ER) causes stress to cells that in turn triggers an adaptive signaling pathway termed unfolded protein response for the purpose of restoring normal cellular physiology or initiating signaling events leading to apoptosis. Identification of those genes that are involved in the unfolded protein response-mediated apoptotic signaling pathway would be valuable toward elucidating the molecular mechanism underlying the relationship between ER stress and apoptosis. We initiated a genetic screen by using the retroviral insertion mutation system to search for genes whose inactivation confers resistance to apoptosis induction by staurosporine. Using this approach, RING finger protein 13 (RNF13) was identified. Interestingly, RNF13 is highly enriched in ER. RNF13 knockdown cells are resistant to apoptosis and JNK activation triggered by ER stress. Conversely, overexpression of RNF13 induces JNK activation and caspase-dependent apoptosis. The RING and transmembrane domains of RNF13 are both required for its effects on JNK activation and apoptosis. Moreover, systematic analysis of the involvement of individual signaling components in the ER stress pathway using knockdown approach reveals that RNF13 acts upstream of the IRE1α- TRAF2 signaling axis for JNK activation and apoptosis. Finally, RNF13 co-immunoprecipitates with IRE1α, and the intact RING domain is also required for mediating its interaction. Together, our data support a model that RNF13 is a critical mediator for facilitating ER stress-induced apoptosis through the activation of the IRE1α-TRAF2-JNK signaling pathway. [ABSTRACT FROM AUTHOR]

Published
2013
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