Development of novel magnetic nano-carriers for high-performance affinity purification

Nishio, Kosuke; Masaike, Yuka; Ikeda, Motohisa; Narimatsu, Hiroki; Gokon, Nobuyuki; Tsubouchi, Shingo; Hatakeyama, Mamoru; Sakamoto, Satoshi; Hanyu, Naohiro; Sandhu, Adarsh; Kawaguchi, Haruma; Abe, Masanori; Handa, Hiroshi

doi:10.1016/j.colsurfb.2008.01.013

Cited by 96 publications

(76 citation statements)

References 33 publications

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“…Magnetic FG beads are structurally unique; they contain large ferrite nanoparticles compared with conventional magnetic beads [8]. During analysis of competitive inhibition using parental naftopidil, representative SDS gel images showed several TG09-02-binding protein bands (Fig.…”

Section: Resultsmentioning

confidence: 99%

Identification of a new pharmacological activity of the phenylpiperazine derivative naftopidil: tubulin-binding drug

Ishii

Sugimura

2014

J Chem Biol

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The phenylpiperazine derivative naftopidil is an α 1 -adrenoceptor (AR) antagonist that has been used clinically to treat benign prostatic hyperplasia. In our drug repositioning research, naftopidil shows the unique growth-inhibitory effects. Naftopidil inhibits cell cycle progression not only in cancer cells, but also in fibroblasts and vascular endothelial cells. Naftopidil-inhibited cell cycle progression is independent of α 1 -AR expression in cells. Therefore, the antiproliferative effects of naftopidil may be due to the off-target effects of the drug. In this study, we attempted to identify the offtarget molecules of naftopidil using the magnetic nanobeads, ferrite glycidyl metharcrylate (FG) beads. Similar to naftopidil, its derivatives TG09-01 and TG09-02, which were introduced with amino groups for immobilizing to FG beads, inhibited cell growth in human HT29 colon adenocarcinoma cells. Both derivatives were associated with inhibition of cell cycle progression in HT29 cells. This observation is consistent with that seen with naftopidil. Using TG09-02-immobilized FG beads, α-and β-tubulins were identified as the specific binding proteins of naftopidil. The tubulin polymerization assay clearly indicated that naftopidil bound directly to tubulin and inhibited the polymerization of tubulin. Other phenylpiperazine derivatives, such as RS100329, BMY7378, and KN-62, also inhibited the polymerization of tubulin. These results suggest that phenylpiperazine derivatives including naftopidil may have broad spectrum of cellular cytotoxicity in various types of cells. In addition, the tubulin polymerization-inhibiting activity of phenylpiperazine derivatives may be a specific feature of the phenylpiperazine-based structure. These findings can allow us to design and synthesize new tubulin-binding drugs derived from naftopidil as a lead compound.

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Section: Resultsmentioning

confidence: 99%

Identification of a new pharmacological activity of the phenylpiperazine derivative naftopidil: tubulin-binding drug

Ishii

Sugimura

2014

J Chem Biol

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“…This approach involves ferromagnetic latex nanoparticles (''nanobeads'') coupled to multimerized DNA sequence motifs for rapid and sequence-selective enrichment of DNA-binding proteins. Relative to other supports such as sepharose, nanobeads have lower nonspecific binding (due to their nonporous, moderately hydrophilic surface), higher capacity (due to their smaller size), and will remain in suspension until high-speed centrifugation or magnetic separation (Shimizu et al 2000;Nishio et al 2008). We used nanobeads coupled to multimerized consensus or mutant simple octamer sequences to purify Oct1 from HeLa cells following IR or H 2 O 2 treatment.…”

Section: Resultsmentioning

confidence: 99%

A general mechanism for transcription regulation by Oct1 and Oct4 in response to genotoxic and oxidative stress

Kang¹,

Gemberling²,

Nakamura³

et al. 2009

Genes Dev.

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119

150

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Oct1 and Oct4 are homologous transcription factors with similar DNA-binding specificities. Here we show that Oct1 is dynamically phosphorylated in vivo following exposure of cells to oxidative and genotoxic stress. We further show that stress regulates the selectivity of both proteins for specific DNA sequences. Mutation of conserved phosphorylation target DNA-binding domain residues in Oct1, and Oct4 confirms their role in regulating binding selectivity. Using chromatin immunoprecipitation, we show that association of Oct4 and Oct1 with a distinct group of in vivo targets is inducible by stress, and that Oct1 is essential for a normal post-stress transcriptional response. Finally, using an unbiased Oct1 target screen we identify a large number of genes targeted by Oct1 specifically under conditions of stress, and show that several of these inducible Oct1 targets are also inducibly bound by Oct4 in embryonic stem cells following stress exposure. Oct1 and Oct4 (products of the Pou2f1 and Pou5f1 genes) are members of the POU (Pit-1, Oct1/2, Unc-86) domain transcription factor family (Herr et al. 1988;Ryan and Rosenfeld 1997). This family is defined by the presence of a bipartite DNA-binding domain in which two subdomains, covalently connected by a flexible linker, typically recognize DNA through major groove interactions on opposite sides of the helix (Klemm et al. 1994). The classical DNA recognition sequence is known as an octamer motif (59-ATGCAAAT-39, hereafter called a ''simple'' octamer). However, we demonstrated recently that native binding sites for Oct4 frequently exist in complex paired, overlapping, and nonconsensus configurations (Tantin et al. 2008).Oct4 is a master regulator of the stem cell state and has recently been shown to be one of three proteins sufficient to reprogram differentiated adult mouse and human cells to the embryonic stem (ES) cell lineage (Okita et al. 2007;Takahashi et al. 2007;Nakagawa et al. 2008). The biological function of Oct1 is more enigmatic. Oct1 is known to interact with regulatory sites in interleukin, immunoglobulin, and histone genes (Garrity et al. 1994;Zheng et al. 2003;Ushmorov et al. 2004;Murayama et al. 2006). Oct1 also moderately stimulates gene expression reporter constructs linked to target sequences in transient transfection assays (Sive et al. 1986;LeBowitz et al. 1988). However, we showed that Oct1 is nonessential for native H2B, IgH, and Igk expression (V.E. V.E.H. Wang et al. 2004). Oct1-deficient cells appear morphologically normal in light microscopy and divide at normal rates. Oct1-deficient mice die in mid-late gestation (embryonic days 12,5-18.5 [E12.5-E18.5]) (V.E.H. .We determined previously that Oct1 À/À mouse embryonic fibroblasts (MEFs) are hypersensitive to oxidative and genotoxic stress (Tantin et al. 2005). One explanation for this result is that constitutive products of Oct1-mediated transcription participate in stress response pathways. Support for an alternative hypothesis, namely that Oct1 directly senses cellular stress, comes from the f...

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“…The most important applications of magnetic carriers are in wastewater treatment, affinity chromatography, and immobilization of enzymes or other biomolecules 20,21 . The magnetic nano particles may be a better choice because the magnetic separation is easier and generally avoids loss of particles 22 .…”

Section: Introductionmentioning

confidence: 99%

Fabrication and Characterization of Core-Shell Magnetic Chitosan Nanoparticles as a Novel carrier for Immobilization of <i>Burkholderia cepacia</i> Lipase

et al. 2015

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Development of novel magnetic nano-carriers for high-performance affinity purification

Cited by 96 publications

References 33 publications

Identification of a new pharmacological activity of the phenylpiperazine derivative naftopidil: tubulin-binding drug

Identification of a new pharmacological activity of the phenylpiperazine derivative naftopidil: tubulin-binding drug

A general mechanism for transcription regulation by Oct1 and Oct4 in response to genotoxic and oxidative stress

Fabrication and Characterization of Core-Shell Magnetic Chitosan Nanoparticles as a Novel carrier for Immobilization of <i>Burkholderia cepacia</i> Lipase

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