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Cited by 94Cell death mechanisms and regulationTGF-β signaling in diseasesCancer-related Molecular Pathways

The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.

Activation of caspase-8 in transforming growth factor-β-induced apoptosis of human hepatoma cells

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Shima, Yuka, Nakao, Kazuhiko, Nakashima, Tomoki, Kawakami, Atsushi, Nakata, Keisuke, Hamasaki, Keisuke, Kato, Yuji, Eguchi, Katsumi, Ishii, Nobuko·1999·Hepatology
DOI 10.1002/hep.510300503
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Abstract

Transforming growth factor-β1 (TGF-β1) has been shown to induce apoptosis in normal or transformed hepatocytes. To elucidate the biochemical pathways leading to apoptosis induced by TGF-β1 in human hepatoma cells (HuH-7), we examined the expression of Bcl-2-related proteins and X-chromosome-linked inhibitor of apoptosis (XIAP), and activation of the caspase cascade following TGF-β1 treatment. Bcl-xL expression began to decline at 12 hours after TGF-β1 treatment and progressively decreased to very low levels in a time-dependent manner. Bax expression showed a little change throughout the experiment. On the other hand, activation of caspase-8 was clearly observed at 36 hours after TGF-β1 treatment, followed by activation of caspase-9, and caspase-3 was activated at 48 hours after treatment at which time apoptosis of HuH-7 cells was observed. TGF-β1 significantly decreased XIAP expression in HuH-7 cells. Addition of an inhibitor of caspase-8 or caspase-3 (IETD-FMK or DEVD-CHO) markedly inhibited TGF-β1-induced apoptosis of HuH-7 cells. Fas/Fas ligand (FasL) interactions in HuH-7 cells were not involved in the apoptotic process. Furthermore, epidermal growth factor (EGF) also completely inhibited TGF-β1-induced apoptosis of HuH-7 cells by inhibiting activation of the caspase cascade. Our results suggested that activation of caspase-3 initiated through caspase-8 activation is involved in the apoptotic process induced by TGF-β1 in HuH-7 cells. Our results also showed that down-regulation of the expression of Bcl-xL and XIAP by TGF-β1 may facilitate activation of caspase-3 in these cells.

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Crossref · 10.1002/hep.510300503

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1 of the 38 references couldn’t be matched to a known paper.

Research works printed but not linked: 3

  1. Lin, 1992, Cancer Res, 52, 385
  2. Oberhammer, 1991, Cancer Res, 51, 2478
  3. Nakabayashi, 1984, Gann, 75, 151

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Metadata

Authors
Shima, Y., Nakao, K., Nakashima, T., Kawakami, A., Nakata, K., Hamasaki, K., Kato, Y., Eguchi, K., & Ishii, N.
Affiliations
Nagasaki University (JP)
Corresponding author
Nakao, Kazuhiko
ORCID
Venue
Hepatology
Publisher
Ovid Technologies (Wolters Kluwer Health)
Published
1999-11
Volume
30
Issue
5
Pages
1215-1222
ISSN
0270-9139 (ISSN-L)
DOI
10.1002/hep.510300503
OpenAlex
W2084133394
Cited by
94
References
38
Citations by year
2024: 2 · 2023: 2 · 2022: 1 · 2020: 3 · 2019: 2 · 2017: 2 · 2016: 2 · 2014: 4 · 2013: 2 · 2012: 2
FWCI
3.45
Type
journal article
Language
en
Open access
Licence
doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 5783 d)
Locations
  • Hepatology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
  • Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Keywords
TGF-β1, apoptosis, caspase-8, caspase-3, caspase-9, Bcl-xL, XIAP, hepatoma cells, Huh7 cells, epidermal growth factor, Fas/Fas ligand, caspase inhibitors, Bcl-2 family proteins
MeSH terms
Cell Division, Enzyme Activation, Epidermal Growth Factor, Carcinoma, Hepatocellular, Humans, Kinetics, Liver Neoplasms, Oligopeptides, Time Factors, Tumor Cells, Cultured, Cysteine Proteinase Inhibitors, Gene Expression Regulation, Neoplastic, Transforming Growth Factor beta, Apoptosis, fas Receptor, Proto-Oncogene Proteins c-bcl-2, Caspases, In Situ Nick-End Labeling, bcl-X Protein, Caspase 3, Caspase 8, Caspase 9, Caspase Inhibitors

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