Recombinant alpha-fetoprotein C-terminal fragment: The new recombinant vector for targeted delivery

Посыпанова, Г. А.; Gorokhovets, Neonila V.; Макаров, Владимир Александрович; Savvateeva, Lyudmila V.; Kireeva, Natalya N; Северин, С Е; Северин, Е. С.

doi:10.1080/10611860801927721

Cited by 27 publications

(19 citation statements)

References 19 publications

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“…); whereas the 18-and 31-kD proteins represent scavenger receptors (SRs) on all other types of endothelium regardless of location in the body [47,63]. The latter two scavenger-like receptors, already mentioned above, have been reported to bind chemically modified or [29] Note that AFP did not normally localize to the nucleus except in one study using fragmented AFP. AFP was not localized to the nucleus in any study employing full-length alpha-fetoprotein, see Posypanova [29].…”

Section: Afp-binding Proteins On Endothelial Cellsmentioning

confidence: 90%

“…The latter two scavenger-like receptors, already mentioned above, have been reported to bind chemically modified or [29] Note that AFP did not normally localize to the nucleus except in one study using fragmented AFP. AFP was not localized to the nucleus in any study employing full-length alpha-fetoprotein, see Posypanova [29]. AFP-receptor antibody clones were not used to detect the receptor, but rather polyclonal antibodies were employed a Positive staining=fluorescence throughout cytoplasm b A human AFP fragment consisting of the third domain and a portion of the second domain (amino acids #357-590) did localize in the cell nucleus (see text)…”

Section: Afp-binding Proteins On Endothelial Cellsmentioning

confidence: 93%

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Review of the putative cell-surface receptors for alpha-fetoprotein: identification of a candidate receptor protein family

Mizejewski

2010

Tumor Biol.

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The identification of a receptor for alpha-fetoprotein (AFP) has long been sought in the field of medicine. The uptake and endocytosis of AFP by rat tumor cells in 1984 sparked a series of confirmatory reports and the original studies were then extended to include multiple tumor types in rats, mice, and humans. The following year, French investigators partially characterized the binding properties of the AFP receptor, but they were not able to purify the receptor. It was not until 1991-1992 that an AFP receptor was partially purified and characterized from both human monocytes and breast cancer cells. By 1993, a monoclonal antibody had been raised against the AFP receptor produced from a breast cancer extract with claims that the receptor was a widespread (universal) oncofetal biomarker for cancer. However, that receptor has yet to be cloned and/or purified due to its complex multimeric binding interactions and associations. The present report will review the literature of the multiple putative AFP receptors described to date, the cellular uptake and endocytosis of AFP, and the biochemical characterization of these putative cell-surface proteins. In addition, evidence derived from computer modeling, proteolytic degradation patterns, and amino acid sequence analysis will be presented in a proposed identification of a family of multi-ligand binding receptors; this family fits many, if not most, of the criteria required for an AFP receptor. The purposed receptor protein family is tentatively identified as the Scavenger receptors which comprise several classes of single- and double-pass integral transmembrane proteins. Present data do not support the concept that the AFP receptor is a "universal" tumor receptor and/or biomarker.

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Section: Afp-binding Proteins On Endothelial Cellsmentioning

confidence: 90%

Section: Afp-binding Proteins On Endothelial Cellsmentioning

confidence: 93%

Review of the putative cell-surface receptors for alpha-fetoprotein: identification of a candidate receptor protein family

Mizejewski

2010

Tumor Biol.

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“…These data prove the efficacy of the vector coated NP system for the delivery of pacli taxel in the chosen experimental conditions (the incu bation of the cells with NPs for 2 h). The experimental conditions were selected according to our previous results, which demonstrated that the level of the receptor mediated endocytosis of the rAFP3D pep tide fragment reached the maximum during the first several hours of incubation with tumor cells [10]. Therefore, the enhanced cytotoxic activity of vector coated NP is a result of the more efficient intracellular transport of these NP by receptor mediated endocy tosis when compared with the nonspecific endocytic uptake of the control NP without a vector and the pas sive diffusion of free paclitaxel.…”

Section: Resultsmentioning

confidence: 99%

“…), but they do not exist in normal tissue cells; for this reason, RAFP is considered a uni versal tumor marker [7,8]. Our previous studies have reported that the efficiency of rAFP3D binding to the RAFPs of cancer cells were equivalent to those seen with full size AFPs [9,10]. Similarly, the application of rAFP3D as a vector molecule within cisplatin con jugates resulted in the enhancement in the specificity of cisplatin delivery into tumor cells [9].…”

Section: Introductionmentioning

confidence: 98%

Antitumor activity of targeted nanosome delivery systems based on poly(lactic-co-glycolic acid) nanoparticles, paclitaxel, and a recombinant alpha-fetoprotein fragment

et al. 2012

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Biodegradable polymeric nanoparticles conjugated with targeting vector molecules have become prospective agents to improve the effectiveness of chemotherapeutic cancer treatment. This approach reduces the systemic toxicity of the drugs and increases the specificity of their uptake by cancer cells. A method has been developed to obtain complex nanoparticles loaded with the antitumor drug paclitaxel and a C terminal fragment of recombinant oncofetal alpha fetoprotein serving as a vector molecule, the in vitro cytotoxic activity of complex nanoparticles for MCF 7 human breast adenocarcinoma cells and resistant MDR1 + cells of the MCF 7 Adr subline was shown to be higher than the cytotoxicity of the free drug and drug loaded nano particles without the vector molecule. Moreover, the toxicity of complex paclitaxel loaded nanoparticles against lymphocytes was low, which confirmed the selectivity of nanoparticle action. In summary, these results demonstrate that the strategy of active targeting of nanoparticles can efficiently enhance the antitumor activity of paclitaxel and it can solve the problem of reversing the multidrug resistance (MDR) of tumor cells.

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“…Recombinant AFP plasmids containing domain 1 and domain 2 were made in accordance with Morinaga et al (1983) [domain 1: amino acids position 1-197, domain 2: amino acids position 198-389], and domain 3 was produced with amino acid positions 357-590 [5]. The N-terminal of recombinant D1-AFP and D2-AFP contain an extra 14 amino acid peptide (MASMTGGQQMGRDP) while D3-AFP contains additional 2 amino acids (MA).…”

Section: Resultsmentioning

confidence: 99%

Immunoregulatory effects of AFP domains on monocyte-derived dendritic cell function

Setiyono¹,

Budiyati²,

Purwantomo³

et al. 2011

BMC Immunol

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BackgroundAlpha-fetoprotein (AFP) is a tumor-associated glycoprotein that functions in regulation of both ontogenic and oncogenic growth. Recent study showed that AFP can induce apoptosis or impair monocyte-derived dendritic cell (MDDC) function. However, it is still unclear which AFP domain (D-AFP) plays major role in this function.ResultsAs expected monocytes cultured in the presence of Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) and Interleukin-4 (IL-4) developed into MDDC. Up-regulation of HLA-DR and CD11c as well as loss of CD14 molecules could be observed. Full length AFP (FL-AFP), domain 2 AFP (D2-AFP) and D3-AFP, but not D1-AFP, significantly inhibited the expression of HLA-DRhigh/CD11chigh and CD80+/CD86high molecules. In contrast, CD83 expression was substantially down-regulated in all samples. Expression of CD40 was significantly suppressed by FL-AFP but not by any D-AFPs. Finally, both FL-AFP and D-AFP impaired the MDDC ability to secrete IL-12 (p70).ConclusionsD2- and D3- but not D1-AFP extensively suppresses the MDDC function. All the recombinant AFP proteins impaired the ability of MDDC to secrete IL-12.

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Recombinant alpha-fetoprotein C-terminal fragment: The new recombinant vector for targeted delivery

Cited by 27 publications

References 19 publications

Review of the putative cell-surface receptors for alpha-fetoprotein: identification of a candidate receptor protein family

Review of the putative cell-surface receptors for alpha-fetoprotein: identification of a candidate receptor protein family

Antitumor activity of targeted nanosome delivery systems based on poly(lactic-co-glycolic acid) nanoparticles, paclitaxel, and a recombinant alpha-fetoprotein fragment

Immunoregulatory effects of AFP domains on monocyte-derived dendritic cell function

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