Downregulation of FGL2/prothrombinase delays HCCLM6 xenograft tumour growth and decreases tumour angiogenesis

@article{Liu2012DownregulationOF,
  title={Downregulation of FGL2/prothrombinase delays HCCLM6 xenograft tumour growth and decreases tumour angiogenesis},
  author={Yanling Liu and Li Xu and Q. Zeng and Jingli Wang and Ming Wang and Dong Xi and Xiaojing Wang and Daofeng Yang and Xiaoping Luo and Qin Ning},
  journal={Liver International},
  year={2012},
  volume={32}
}
Fibrinogen‐like protein 2 (FGL2), which directly generates thrombin from prothrombin without activation of the conventional coagulation cascade, was shown to be overexpressed in various human malignant tumours. 
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The Duality of Fgl2 - Secreted Immune Checkpoint Regulator Versus Membrane-Associated Procoagulant: Therapeutic Potential and Implications
TLDR
This article will provide a comprehensive review of the currently known biological properties of Fgl2, which provides a compelling rationale for FGL2 expression to not only be considered as a disease biomarker but also as a therapeutic target.
The cell-membrane prothrombinase, fibrinogen-like protein 2, promotes angiogenesis and tumor development.
Soluble fibrinogen like protein 2 (sFGL2), the novel effector molecule for immunoregulation
TLDR
This mini-review focuses primarily on the recent literature with respect to the signaling mechanism of sFGL2 in immunomodulation, and discusses the clinical implications of s fibrinogen-like protein 2 in transplantation, hepatitis, autoimmunity, and tumors.
Coagulation and angiogenic gene expression profiles are defined by molecular subgroups of medulloblastoma: evidence for growth factor‐thrombin cross‐talk
TLDR
This data indicates that there is a link between molecular subtype and the network of vascular regulators expressed in MB, and this work aims to establish a causal link between WNT, SHH, Group 3 and Group 4 and molecular disease subtypes.
Adenovirus‐mediated artificial microRNA against human fibrinogen like protein 2 inhibits hepatocellular carcinoma growth
TLDR
An adenoviral vector expressing an artificial microRNA (miRNA) against hFGL2 (Ad‐hfgl2‐mi RNA) was used to evaluate the effect of FGL2 knockdown on cell proliferation and tumor growth of HCCLM6 xenografts.
The Role of Fibrinogen-Like Protein 2 on Immunosuppression and Malignant Progression in Glioma
TLDR
FGL2 facilitates glioma progression from low to high grade and holds therapeutic promise for halting malignant transformation in gliomas, and inhibiting FGL2 expression had a therapeutic effect.
FGL2 prothrombinase contributes to the early stage of coronary microvascular obstruction through a fibrin-dependent pathway.
Overexpression of fibrinogen-like protein 2 induces epithelial-to-mesenchymal transition and promotes tumor progression in colorectal carcinoma
TLDR
It is suggested that F GL2 plays an important oncogenic role in CRC aggressiveness by inducing EMT, and FGL2 could be employed as a novel prognostic marker and effective therapeutic target for CRC.
Physiological functions and clinical implications of fibrinogen-like 2: A review.
TLDR
Light is shed on development of sFGL2 as an alternative immunosuppressive agent for organ transplantation or as a biomarker for predicting disease progression, monitoring therapeutic effects, and targeting FGL2 for repression in ameliorating fulminant viral hepatitis.
Stroma-derived Fibrinogen-like Protein 2 Activates Cancer-associated Fibroblasts to Promote Tumor Growth in Lung Cancer
TLDR
It is demonstrated that Fgl2 induced an activated and pro-tumorigenic phenotype of cancer-associated fibroblasts (CAFs) which are the principal source of CXCL12 in the tumor microenvironment (TME).
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References

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TLDR
The hfg12 contributes to the hypercoagulability in cancer and may induce tumor angiogenesis and metastasis via cytokine induction.
Endothelial Induction of fgl2 Contributes to Thrombosis during Acute Vascular Xenograft Rejection1
TLDR
Induction of fgl2 on the vascular endothelium plays a role in the pathogenesis of AVR-associated thrombosis and may yield novel strategies by which to overcome AVR and extend xenograft survival.
The Fgl2/fibroleukin prothrombinase contributes to immunologically mediated thrombosis in experimental and human viral hepatitis.
TLDR
Data indicate a critical role for Fgl2/fibroleukin in the pathophysiology of experimental and human viral hepatitis.
Role of Fibrinogen-Like Protein 2 Prothrombinase/Fibroleukin in Experimental and Human Allograft Rejection1
TLDR
It is suggested that fgl2 accounts for the fibrin deposition seen in both experimental and human allograft rejection and provide a rationale for targeting fGL2 as adjunctive therapy to treat allografted rejection.
Cytokine-Induced Hepatic Apoptosis Is Dependent on FGL2/Fibroleukin: The Role of Sp1/Sp3 and STAT1/PU.1 Composite cis Elements
TLDR
It is demonstrated that IFN-γ and TNF-α induce hepatocyte apoptosis in vivo, which is dependent on induction of fgl2, and defines the molecular basis of transcription of fGL2 in vitro.
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TLDR
Thrombin plays an important role in OPN‐mediated aggressive phenotype of HCC through activation of integrin β1‐FAK signaling, and is an independent poor prognostic factor for HCC.
Expression and significance of fgl2 prothrombinase in cardiac microvascular endothelial cells of rats with type 2 diabetes
TLDR
In rats with type 2 diabetes, microthrombosis due to fgl2 contributes to the impairment of cardiac diastolic or systolic function and morphological changes.
The fgl2 prothrombinase/fibroleukin gene is required for lipopolysaccharide-triggered abortions and for normal mouse reproduction.
TLDR
Physiological expression of fgl2 in fetal trophoblast may prevent occult loss in early pregnancy, along with other coagulation factors, but fgl 2 expression is required for LPS to induce abortion pathology.
Kinetic Analysis of a Unique Direct Prothrombinase, fgl2, and Identification of a Serine Residue Critical for the Prothrombinase Activity1
TLDR
Direct evidence is provided that fgl2 cleaves prothrombin to thrombin consistent with serine protease activity and requires calcium, phospholipids, and factor Va for its full activity.
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