Identification of FGF receptor-binding peptides for cancer gene therapy

Maruta, Fukuto; Parker, Alan L.; Fisher, Kerry D.; Hallissey, Michael; Ismail, Tariq; Rowlands, David; Chandler, Lois A.; Kerr, David; Seymour, Leonard W.

doi:10.1038/sj.cgt.7700470

Cited by 61 publications

(50 citation statements)

References 23 publications

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“…184 A study demonstrated that a heptapeptide sequence (MQLPLAT) is binding to FGFR with high affinity, 185 suggesting that peptide is also a ligand to FGFR. Hu et al 186 …”

mentioning

confidence: 99%

Ligand-based targeted therapy: a novel strategy for hepatocellular carcinoma

Li¹,

Zhang²,

Wang³

et al. 2016

IJN

118

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“…184 A study demonstrated that a heptapeptide sequence (MQLPLAT) is binding to FGFR with high affinity, 185 suggesting that peptide is also a ligand to FGFR. Hu et al 186 …”

mentioning

confidence: 99%

Ligand-based targeted therapy: a novel strategy for hepatocellular carcinoma

Li¹,

Zhang²,

Wang³

et al. 2016

IJN

118

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“…In vitro biopanning was carried out as described previously with slight modifications (10)(11)(12). Briefly, following subtractive clearance of the library using the normal cell line MMNK-1, 3 consecutive rounds of in vitro biopanning were carried out on the target human ICC RBE cells.…”

Section: Identification Of Peptide Motifs Binding To Human Cca Rbe Cellsmentioning

confidence: 99%

“…Biopanning was conducted for a total of 3 rounds for enrichment of peptides binding selectively and efficiently to CCA. Phage display, isolation, and sequencing of phage DNA were carried out as described previously (10,11).…”

Section: Cell Linesmentioning

confidence: 99%

“…More recently, peptide-presenting bacteriophage libraries that enable the selection of peptides that bind to selected cell types or ligands have been utilized (8). The biopanning technique has been shown to be a powerful tool for identifying specific ligands on target organs and tumors, as it enables forced evolution of very high-affinity targeting peptides through rounds of selection of living libraries of peptides presented on the surface of the bacteriophage particle (9)(10)(11)(12). This technique has classically been used to iteratively produce peptides binding purified cell surface markers (13,14), cultured cell lines (15,16), or tumor-bearing animals (17)(18)(19).…”

Section: Introductionmentioning

confidence: 99%

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COP35, a Cholangiocarcinoma-Binding Oligopeptide, Interacts with the Clathrin Heavy Chain Accompanied by GRP78

Kitahara

Masumoto

Parker

et al. 2011

Molecular Cancer Research

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Cholangiocarcinoma (CCA) is a common carcinoma of the liver, and the majority of patients with CCA have a poor prognosis due to the lack of effective nonsurgical therapies in addition to its rapid progression and inoperability at the time of diagnosis. The development of novel nonsurgical therapeutics that efficiently target CCA could significantly improve the prognosis for patients presenting with CCA. Here, we describe the iterative production and characterization of a novel peptide, designated COP35 (CCA-binding oligopeptide 35), which binds selectively to human CCA, identified by bacteriophage biopanning using the intrahepatic CCA cell line RBE and the normal cholangiocyte cell line MMNK-1. COP35 was found to augment the growth inhibitory effects of 5-fluorouracil (5-FU) against RBE cells. Utilizing pull-down assay and liquid chromatography, we identify the clathrin heavy chain accompanied by GRP78/BiP as a COP35-binding partner. In summary, we identify COP35 as a possible candidate for peptide-targeted therapies for CCA. Mol Cancer Res; 9(6); 688-701. Ó2011 AACR.

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“…[13][14][15][16][17] There is considerable interest, therefore, in the use of such peptides as Ag-targeting moieties, since they could greatly simplify vaccine development. A receptor attracting considerable interest for enhancing Ag-specific immunity by targeting of Ag to DCs is CD11c/CD18, which is expressed at high levels on murine DCs, and is often used as DC-specific marker.…”

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confidence: 99%

Ag‐bearing liposomes engrafted with peptides that interact with CD11c/CD18 induce potent Ag‐specific and antitumor immunity

Faham

Altin

2011

Intl Journal of Cancer

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Dendritic cells (DCs) play key role in eliciting antigen (Ag)-specific immune responses, and crucial to this is the uptake of Ag via surface receptors including the heterodimeric integrin CD11c/CD18. Here we report that CD11c/CD18-interacting peptides can be used as targeting moieties to deliver liposomal Ag to antigen presenting cells (APCs) and elicit Ag-specific and antitumor immunity. Two peptides of sequence related to human ICAM-4 and previously reported to bind CD11c/CD18, and a 12-mer cyclic peptide previously identified by phage display to bind CD11c/CD18, were produced synthetically, and tested for their ability to target liposomal Ag. The three peptides were designed to contain a shorter spacer to reduce steric hindrance, and a His-tag to enable engraftment onto liposomes incorporated with chelator lipid. Our results show that the three peptides, denoted as p17, p18 and p30, promote strong binding of liposomes to CD11c 1 and CD11b 1 cells in vitro and in vivo. Vaccination of mice with Ag-bearing liposomes engrafted with the peptides, particularly p18 and p30, induced Agspecific T cell priming and antibody production. Importantly, the vaccination of C57BL/6 mice with syngeneic B16-OVA-derived plasma membrane vesicles (PMVs) engrafted with p18 and p30 peptide showed dramatic antitumor responses, inhibiting tumor growth/metastasis in both the lung and subcutaneous tumor models, with a high proportion of the mice apparently being ''cured'' of their tumors. The engraftment of p18 and p30 peptides onto liposomes and PMVs, thus provides an effective means to target Ags to DCs in vivo, for the development of effective cancer vaccines and immunotherapies.The use of antigen-pulsed dendritic cells (DCs) has shown promise for developing cell-based cancer vaccines and immunotherapies. 1 DCs play a key role in eliciting Ag-specific immune responses, and crucial to this is the uptake of antigen (Ag) via a number of DC surface receptors such as Fc-receptors, C-type lectins, Toll-like receptors (TLRs) and integrin receptor CD11c/CD18. [2][3][4][5][6] The unique ability of DCs to prime naïve T cells makes them ideal targets for Ag-delivery and vaccine development. 7 To better exploit this potential, techniques have been used to target protein-Ag to DCs in vivo, potentially circumventing the need to manipulate DCs ex vivo for cancer immunotherapy. 8,9 Typical strategies involve conjugation of Ag to mAbs, ScFv or Fab fragments specific for a DC surface marker or Ag-uptake receptor. 4,6,10,11 To facilitate the delivery of multiple Ags simultaneously, we previously attached recombinant co-stimulatory molecules and ScFv to Ag-containing delivery vehicles such as liposomes and membrane vesicles. 8,12 The vaccination of mice with such constructs can elicit potent immune responses and inhibit tumor growth in tumor models. 12 However, mAbs, ScFvs, and recombinant proteins for use as DC-targeted conjugates, or as targeting moieties for liposomes, can be time-consuming and expensive to produce for clinical applications.The use of...

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Identification of FGF receptor-binding peptides for cancer gene therapy

Cited by 61 publications

References 23 publications

Ligand-based targeted therapy: a novel strategy for hepatocellular carcinoma

Ligand-based targeted therapy: a novel strategy for hepatocellular carcinoma

COP35, a Cholangiocarcinoma-Binding Oligopeptide, Interacts with the Clathrin Heavy Chain Accompanied by GRP78

Ag‐bearing liposomes engrafted with peptides that interact with CD11c/CD18 induce potent Ag‐specific and antitumor immunity

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