A novel cysteine protease HeLa DUB-1 responsible for cleaving the ubiquitin in human ovarian cancer cells
Autor: | Myung-Sun Kim, Hyung Min Chung, In-Cheol Kang, Kyong-Jai Yoo, Kwang-Hyun Baek |
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Rok vydání: | 2004 |
Předmět: |
Cancer Research
Proteases DNA Complementary Molecular Sequence Data Protein degradation Deubiquitinating enzyme HeLa Ubiquitin Humans Tissue Distribution Northern blot Amino Acid Sequence RNA Messenger Cloning Molecular Conserved Sequence biology Base Sequence Sequence Homology Amino Acid biology.organism_classification Cysteine protease Protein Structure Tertiary Cysteine Endopeptidases Oncology Biochemistry Apoptosis Uterine Neoplasms biology.protein Female Ubiquitin Thiolesterase HeLa Cells |
Zdroj: | International journal of oncology. 25(2) |
ISSN: | 1019-6439 |
Popis: | The regulation of ubiquitin-mediated protein degradation is becoming important for a number of cellular processes. Human HeLa DUB-1 cDNA, encoding a novel deubiquitinating enzyme, was isolated from ovarian cancer cells. It has 1,647 bp nucleotides and encodes a 548 amino acid polypeptide with the molecular weight of approximately 61 kDa. It contains the highly conserved Cys, Asp (I), His, and Asn/Asp (II) domains characteristic of the ubiquitin-specific processing proteases. Biochemical assay revealed that HeLa DUB-1 has deubiquitinating enzyme activity in vivo and in vitro. Northern blot analysis for HeLa DUB-1 showed the strong expression in human skeletal muscle and pancreas and to some extent in heart, placenta, lung, liver, and kidney. Interestingly, the expression was hardly seen in the brain. Localization study indicates that HeLa DUB-1 proteins are present in both the cytoplasm and nucleus. |
Databáze: | OpenAIRE |
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