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582 results on '"Futaki, S."'

1. The Transcriptional Landscape of the Mammalian Genome

Author

Carninci, P., Kasukawa, T., Katayama, S., Gough, J., Frith, M. C., Maeda, N., Oyama, R., Ravasi, T., Lenhard, B., Wells, C., Kodzius, R., Shimokawa, K., Bajic, V. B., Brenner, S. E., Batalov, S., Forrest, A. R. R., Zavolan, M., Davis, M. J., Wilming, L. G., Aidinis, V., Allen, J. E., Ambesi-Impiombato, A., Apweiler, R., Aturaliya, R. N., Bailey, T. L., Bansal, M., Baxter, L., Beisel, K. W., Bersano, T., Bono, H., Chalk, A. M., Chiu, K. P., Choudhary, V., Christoffels, A., Clutterbuck, D. R., Crowe, M. L., Dalla, E., Dalrymple, B. P., de Bono, B., Della Gatta, G., di Bernardo, D., Down, T., Engstrom, P., Fagiolini, M., Faulkner, G., Fletcher, C. F., Fukushima, T., Furuno, M., Futaki, S., Gariboldi, M., Georgii-Hemming, P., Gingeras, T. R., Gojobori, T., Green, R. E., Gustincich, S., Harbers, M., Hayashi, Y., Hensch, T. K., Hirokawa, N., Hill, D., Huminiecki, L., Iacono, M., Ikeo, K., Iwama, A., Ishikawa, T., Jakt, M., Kanapin, A., Katoh, M., Kawasawa, Y., Kelso, J., Kitamura, H., Kitano, H., Kollias, G., Krishnan, S. P. T., Kruger, A., Kummerfeld, S. K., Kurochkin, I. V., Lareau, L. F., Lazarevic, D., Lipovich, L., Liu, J., Liuni, S., McWilliam, S., Babu, M. Madan, Madera, M., Marchionni, L., Matsuda, H., Matsuzawa, S., Miki, H., Mignone, F., Miyake, S., Morris, K., Mottagui-Tabar, S., Mulder, N., Nakano, N., Nakauchi, H., Ng, P., Nilsson, R., Nishiguchi, S., Nishikawa, S., Nori, F., Ohara, O., Okazaki, Y., Orlando, V., Pang, K. C., Pavan, W. J., Pavesi, G., Pesole, G., Petrovsky, N., Piazza, S., Reed, J., Reid, J. F., Ring, B. Z., Ringwald, M., Rost, B., Ruan, Y., Salzberg, S. L., Sandelin, A., Schneider, C., Schöbach, C., Sekiguchi, K., Semple, C. A. M., Seno, S., Sessa, L., Sheng, Y., Shibata, Y., Shimada, H., Shimada, K., Silva, D., Sinclair, B., Sperling, S., Stupka, E., Sugiura, K., Sultana, R., Takenaka, Y., Taki, K., Tammoja, K., Tan, S. L., Tang, S., Taylor, M. S., Tegner, J., Teichmann, S. A., Ueda, H. R., van Nimwegen, E., Verardo, R., Wei, C. L., Yagi, K., Yamanishi, H., Zabarovsky, E., Zhu, S., Zimmer, A., Hide, W., Bult, C., Grimmond, S. M., Teasdale, R. D., Liu, E. T., Brusic, V., Quackenbush, J., Wahlestedt, C., Mattick, J. S., Hume, D. A., Kai, C., Sasaki, D., Tomaru, Y., Fukuda, S., Kanamori-Katayama, M., Suzuki, M., Aoki, J., Arakawa, T., Iida, J., Imamura, K., Itoh, M., Kato, T., Kawaji, H., Kawagashira, N., Kawashima, T., Kojima, M., Kondo, S., Konno, H., Nakano, K., Ninomiya, N., Nishio, T., Okada, M., Plessy, C., Shibata, K., Shiraki, T., Suzuki, S., Tagami, M., Waki, K., Watahiki, A., Okamura-Oho, Y., Suzuki, H., and Kawai, J.

Published
2005

9. Modular Redesign of a Cationic Lytic Peptide To Promote the Endosomal Escape of Biomacromolecules

Author

Azuma, Y., Imai, H., Kawaguchi, Y., Nakase, I., Kimura, Hiroshi, and Futaki, S.

Subjects
Cytosol/metabolism, 0301 basic medicine, Peptides/chemistry/*metabolism/pharmacology, Peptide, 01 natural sciences, chemistry.chemical_compound, Cytosol, Coordination Complexes, Nickel, Dextrans/chemistry/metabolism, Cytotoxicity, chemistry.chemical_classification, Microscopy, Confocal, Cations/chemistry, Nickel/chemistry, Dextrans, General Medicine, Endocytosis, Dipicolylamine, Lytic cycle, Drug delivery, Intercellular Signaling Peptides and Proteins, peptides, Cell Survival/drug effects, Endosomes/*metabolism, Endosome, Cell Survival, Endosomes, 010402 general chemistry, Catalysis, 03 medical and health sciences, Cations, Humans, Fluorescent Dyes/chemistry, cytotoxicity, Fluorescent Dyes, tridentate ligands, 010405 organic chemistry, drug delivery, membranes, General Chemistry, Coordination Complexes/chemistry, 0104 chemical sciences, 030104 developmental biology, chemistry, Liposomes/metabolism, Liposomes, Biophysics, Peptides, HeLa Cells
Abstract

Endocytosis is an important route for the intracellular delivery of biomacromolecules, wherein their inefficient endosomal escape into the cytosol remains a major barrier. Based on the understanding that endosomal membranes are negatively charged, we focused on the potential of cationic lytic peptides for developing endosomolysis agents to release such entrapped molecules. As such, a venom peptide, Mastoparan X, was employed and redesigned to serve as a delivery tool. Appending a tri-glutamate unit to the N-terminus attenuates the cytotoxicity of Mastoparan X by about 40 fold, while introduction of a NiII -dipicolylamine complex enhances cellular uptake of the peptide by about 17 fold. Using the optimized peptide, various fluorescently labeled macromolecules were successfully delivered to the cytosol, enabling live-cell imaging of acetylated histones.

Published
2018
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24. Design and tuning of a cell-penetrating albumin derivative as a versatile nanovehicle for intracellular drug delivery

Author

Ichimizu, S., Watanabe, H., Maeda, H., Hamasaki, K., Nakamura, Y., Chuang, Victor, Kinoshita, R., Nishida, K., Tanaka, R., Enoki, Y., Ishima, Y., Kuniyasu, A., Kobashigawa, Y., Morioka, H., Futaki, S., Otagiri, M., Maruyama, T., Ichimizu, S., Watanabe, H., Maeda, H., Hamasaki, K., Nakamura, Y., Chuang, Victor, Kinoshita, R., Nishida, K., Tanaka, R., Enoki, Y., Ishima, Y., Kuniyasu, A., Kobashigawa, Y., Morioka, H., Futaki, S., Otagiri, M., and Maruyama, T.

Abstract

© 2018 Human serum albumin (HSA) is a superior carrier for delivering extracellular drugs. However, the development of a cell-penetrating HSA remains a great challenge due to its low membrane permeability. We report herein on the design of a series of palmitoyl-poly-arginine peptides (CPPs) and an evaluation of their cell-penetrating effects after forming a complex with HSA for use in intracellular drug delivery. The palmitoyl CPPs forms a stable complex with HSA by anchoring itself to the high affinity palmitate binding sites of HSA. Among the CPPs evaluated, a cyclic polypeptide composed of D-dodecaarginines, palmitoyl-cyclic-(D-Arg) 12 was the most effective for facilitating the cellular uptake of HSA by HeLa cells. Such a superior cell-penetrating capability is primarily mediated by macropinocytosis. The effect of the CPP on pharmacological activity was examined using three drugs loaded in HSA via three different methods: a) an HSA-paclitaxel complex, b) an HSA-doxorubicin covalent conjugate and c) an HSA-thioredoxin fusion protein. The results showed that cell-penetrating efficiency was increased with a corresponding and significant enhancement in pharmacological activity. In conclusion, palmitoyl-cyclic-(D-Arg) 12 /HSA is a versatile cell-penetrating drug delivery system with great potential for use as a nano-carrier for a wide diversity of pharmaceutical applications.

Published
2018

25. Enhanced expression of nidogen 1 around the nest of basal cell carcinoma compared with that around squamous cell carcinoma.

Author

Hirakawa, Y., Futaki, S., Tanizaki, H., Furukawa, F., Maemura, K., Kondo, Y., and Moriwaki, S.

Subjects
*BASAL cell carcinoma, *SQUAMOUS cell carcinoma, *PRECANCEROUS conditions, *ACTINIC keratosis, *NESTS, *EPIDERMIS
Abstract

Basal cell carcinoma (BCC) is a malignant skin tumor originating from cells of the epidermal basal layer and adnexal epithelium, especially in sun-exposed areas. Unlike squamous cell carcinoma (SCC), BCC has a propensity to grow only locally possibly due to differences in the surrounding microenvironment including the basement membrane (BM) and stroma. To investigate the components constituting the BM and surrounding connective tissue in BCC and SCC, we analyzed the expression of BM proteins, nidogen 1 (NID1) and type IV collagen (COL4). We compared the immunohistochemical expressions of NID1 and COL4 among tumor specimens from BCC, SCC and its precancerous condition, actinic keratosis (AK), (n = 5 each condition). The expressions of NID1 and COL4 were both decreased around the tumor nest of SCC. In contrast, the expressions of both NID1 and COL4 around the nest of BCC were much higher than in the peri-lesional normal skin not only at the BM, but also in the surrounding stromal tissue. Our findings imply that the surrounding stromal cells of BCC, but not SCC or AK, excessively produce NID1 and COL4, which may be involved in preventing BCC cells from destroying the BM and invading the dermis. [ABSTRACT FROM AUTHOR]

Published
2019
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29. Effects of Na+/H+ exchangers inhibitors on subcellular localization of endocytic organelles and intracellular dynamics of protein transduction domains HIV-TAT peptide and octaarginine

Author

Fretz, M.M., Jin, X., Conibere, R., Penning, N.A., Al-Taei, S., Storm, G., Futaki, S., Takeuchi, T., Nakase, I., Jones, A.T., Advanced drug delivery systems/drug targeting, and Dep Farmaceutische wetenschappen

Subjects
Pharmacology, Medical technology, Farmacie(FARM), Biomedische technologie en medicijnen
Published
2006

37. Effects of Na+/H+ exchangers inhibitors on subcellular localization of endocytic organelles and intracellular dynamics of protein transduction domains HIV-TAT peptide and octaarginine

Author

Advanced drug delivery systems/drug targeting, Dep Farmaceutische wetenschappen, Fretz, M.M., Jin, X., Conibere, R., Penning, N.A., Al-Taei, S., Storm, G., Futaki, S., Takeuchi, T., Nakase, I., Jones, A.T., Advanced drug delivery systems/drug targeting, Dep Farmaceutische wetenschappen, Fretz, M.M., Jin, X., Conibere, R., Penning, N.A., Al-Taei, S., Storm, G., Futaki, S., Takeuchi, T., Nakase, I., and Jones, A.T.

Published
2006

44. Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase. Effects of exogenous amines on the slow formation of intermediates

Author

Futaki S, Ueno H, Alvaro Martinez-del-Pozo, Ma, Pospischil, Jm, Manning, Ringe D, Stoddard B, Tanizawa K, Yoshimura T, and Soda K

Subjects
Binding Sites, Base Sequence, Protein Conformation, Circular Dichroism, Glutamine, Lysine, Molecular Sequence Data, Recombinant Proteins, D-Alanine Transaminase, Kinetics, Spectrophotometry, Pyridoxal Phosphate, Escherichia coli, Mutagenesis, Site-Directed, Oligonucleotide Probes, Transaminases
Abstract

In bacterial D-amino acid transaminase, Lys-145, which binds the coenzyme pyridoxal 5'-phosphate in Schiff base linkage, was changed to Gln-145 by site-directed mutagenesis (K145Q). The mutant enzyme had 0.015% the activity of the wild-type enzyme and was capable of forming a Schiff base with D-alanine; this external aldimine was formed over a period of minutes depending upon the D-alanine concentration. The transformation of the pyridoxal-5'-phosphate form of the enzyme to the pyridoxamine-5'-phosphate form (i.e. the half-reaction of transamination) occurred over a period of hours with this mutant enzyme. Thus, information on these two steps in the reaction and on the factors that influence them can readily be obtained with this mutant enzyme. In contrast, these reactions with the wild-type enzyme occur at much faster rates and are not easily studied separately. The mutant enzyme shows distinct preference for D- over L-alanine as substrates but it does so about 50-fold less effectively than the wild-type enzyme. Thus, Lys-145 probably acts in concert with the coenzyme and other functional side chain(s) to lead to efficient and stereochemically precise transamination in the wild-type enzyme. The addition of exogenous amines, ethanolamine or methyl amine, increased the rate of external aldimine formation with D-alanine and the mutant enzyme but the subsequent transformation to the pyridoxamine-5'-phosphate form of the enzyme was unaffected by exogenous amines. The wild-type enzyme displayed a large negative trough in the circular dichroic spectrum at 420 nm, which was practically absent in the mutant enzyme. However, addition of D-alanine to the mutant enzyme generated this negative Cotton effect (due to formation of the external aldimine with D-alanine). This circular dichroism band gradually collapsed in parallel with the transformation to the pyridoxamine-5'-phosphate enzyme. Further studies on this mutant enzyme, which displays the characteristics of the wild-type enzyme but at attenuated rates, may yield information on the factors controlling the stereochemistry of the reaction as well as on the catalytic steps of the transaminase pathway.

Published
1990

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