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2 results on '"Heeyoung Seok"'

1. Comparative Study of Apoptosis Induced by H2O2 and NO: Limitation of Apoptosis Induced by NO Due to Slower Recovery of Activity of NOModified Caspase

Author

Song Yub Shin, Heeyoung Seok, Jung Sup Lee, Pratap Karki, Il-Seon Park, Byungyun Cho, and Ja Eun Kim

Subjects
Apoptosis, Caspase 3, Nitric Oxide, Biochemistry, Jurkat cells, Jurkat Cells, Structural Biology, Humans, Inducer, Caspase, chemistry.chemical_classification, biology, Intrinsic apoptosis, Cytochromes c, Hydrogen Peroxide, General Medicine, Caspase Inhibitors, Cell biology, Enzyme Activation, Enzyme, UVB-induced apoptosis, chemistry, Caspases, biology.protein
Abstract

Both H(2)O(2) and NO can act as apoptogens, triggering apoptosis in many cells. They are also well known inhibitors of caspases, essential enzymes in apoptosis. The differences between these two agents as apoptosis inducers and how caspases mediate apoptosis with these inhibitory agents is still unclear. Consistent with the previous reports, these two agents induced apoptosis accompanied by caspase activation with limitation of all apoptotic events for NO. It was found that NO-modified caspase-3 showed a slower recovery of its activity in the presence of the reducing agents compared to that of H(2)O(2) modification. This is one possible cause of the limited apoptosis in the case of NO.

Published
2006

2. Biochemical Characterization of Apoptotic Cleavage of KH-Type Splicing Regulatory Protein (KSRP) / Far Upstream Element-Binding Protein 2 (FBP2)

Author

Minseok Cheon, II-Seon Park, Heeyoung Seok, and Jinsun Cho

Subjects
Regulation of gene expression, biology, Caspase 3, Intrinsic apoptosis, RNA-Binding Proteins, Apoptosis, General Medicine, Cleavage (embryo), Biochemistry, Cysteine protease, Rats, Substrate Specificity, Structural Biology, Caspases, RNA splicing, Proteome, Trans-Activators, Tumor Cells, Cultured, biology.protein, Animals, Humans, Caspase
Abstract

Caspases, Asp-specific cysteine protease, cleave proteins upon apoptosis. To identify and characterize new caspase substrate in the nucleus, the proteome of the rat liver extracts was analyzed after the treatment with caspases. One of the identified proteins was KSRP / FBP2 that is preferentially cleaved by caspase-3 and -7 at two sites after Asp102 and Asp183. The second site was cleaved only in the protein produced in cells, but not in in vitro translated protein. These results indicate that more than the primary sequence may be important for the recognition by caspases.

Published
2002

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