Expression of Fas and Fas-related molecules in human hepatocellular carcinoma

Lee, Sug Hyung; Shin, Min Sun; Lee, Ho-Sun; Bae, Jeong Hun; Lee, Hun Kyung; Kim, Hong Sug; Kim, Su Young; Jang, Ja June; Joo, Mee; Kang, Yun Kyung; Park, Won Sang; Park, Jik Young; Oh, Ro Ra; Han, Seo Young; Lee, Jong Heun; Kim, Sang Ho; Lee, Jung Young; Yoo, Nam Jin

doi:10.1053/hupa.2001.22769

Cited by 98 publications

(61 citation statements)

References 39 publications

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“…Many observations have highlighted the role of the Fas/FasL system in chemotherapy-induced apoptosis of tumors by upregulation of Fas/APO-1 or its ligand [20]. Loss of Fas/APO-1 expression might be involved in the escape of liver cancer cells from the immune defense system and chemoresistance of HCC to chemotherapeutic agents [21]. Ligation of Fas by agonistic antibody or its mature ligand induces receptor oligomerization and formation of death-inducing signaling complex (DISC), followed by activation of caspase-8, then further activating a series caspase cascade resulting in cell apoptotic death [3,19].…”

Section: Discussionmentioning

confidence: 99%

Acacetin inhibits the proliferation of Hep G2 by blocking cell cycle progression and inducing apoptosis

Hsu

Kuo

Lin

2004

Biochemical Pharmacology

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Section: Discussionmentioning

confidence: 99%

Acacetin inhibits the proliferation of Hep G2 by blocking cell cycle progression and inducing apoptosis

Hsu

Kuo

Lin

2004

Biochemical Pharmacology

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“…PTPL1 expression was reported to inhibit Fas-mediated apoptosis in both pancreatic adenocarcinoma [45,46] and melanoma [47] cell lines thus acting as a survival mechanism in tumor cells expressing both Fas and FasL. Additional tumor models of ovarian cancer [48], colon cancer [49], head/ neck cancer [50], hepatocellular carcinoma [51], and hepatoblastoma [52] also showed a correlation between tumor cell survival in the presence of both Fas/FasL and expression of PTPL1. While some functional and correlative evidence exists for the regulation of Fas by PTPL1, at least one potential mechanism is explored below.…”

Section: Ptpl1 As a Tumor Promotermentioning

confidence: 93%

PTPL1: a large phosphatase with a split personality

Abaan

Toretsky

2008

Cancer Metastasis Rev

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Protein tyrosine phosphatase, PTPL1, (also known as PTPN13, FAP-1, PTP-BAS, PTP1E) is a non-receptor type PTP and, at 270 kDa, is the largest phosphatase within this group. In addition to the well-conserved PTP domain, PTPL1 contains at least 7 putative macromolecular interaction domains. This structural complexity indicates that PTPL1 may modulate diverse cellular functions, perhaps exerting both positive and negative effects. In accordance with this idea, while certain studies suggest that PTPL1 can act as a tumor-promoting gene other experimental studies have suggested that PTPL1 may function as a tumor suppressor. The role of PTPL1 in the cancer cell is therefore likely to be both complex and context dependent with possible roles including the modulation of growth, stress-response, and cytoskeletal remodeling pathways. Understanding the nature of molecular complexes containing PTPL1, its interaction partners, substrates, regulation and subcellular localization are key to unraveling the complex personality of this protein phosphatase.

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“…Activated Fas recruits the adaptor protein Fas-associated death domain protein (FADD) that cleaves procaspase-8 and initiates an active form of caspase-8, which activates the downstream effector caspase-3 that leads to apoptosis (31). Several studies have shown that FasL expression is implicated in HCC and that it is enhanced in regions with infiltrating inflammatory cells on the margins of the cancerous tissue (18)(19)(20). Moreover, in vivo studies have shown that injection of sFasL can induce tumor cell apoptosis and hepatocyte apoptosis, which cause liver failure (23,24).…”

Section: Discussionmentioning

confidence: 99%

“…After cross-linking, the pro-apoptotic property of sFasL is restored. Several studies have shown that FasL expression is implicated in HCC and is enhanced in regions with infiltrating inflammatory cells on the margins of the cancerous tissue (18)(19)(20). In vitro studies have revealed that the capacity of naturally processed sFasL to induce apoptosis is less potent than that of cell surface FasL, possibly due to decreased capability to cross-link Fas (21,22).…”

Section: Introductionmentioning

confidence: 99%