Search

Your search keyword '"Sakuragawa N"' showing total 508 results
Start Over Author "Sakuragawa N"
508 results on '"Sakuragawa N"'

7. Concise review: isolation and characterization of cells from human term placenta: outcome of the first international Workshop on Placenta Derived Stem Cells

Author

Parolini, O, Alviano, F, Bagnara, G P, Bilic, G, Bühring, H J, Evangelista, M, Hennerbichler, S, Liu, B, Magatti, M, Mao, N, Miki, T, Marongiu, F, Nakajima, H, Nikaido, T, Portmann-Lanz, C B, Sankar, V, Soncini, M, Stadler, G, Surbek, D, Takahashi, T A, Redl, H, Sakuragawa, N, Wolbank, S, Zeisberger, S M, Zisch, A H, Storm, S C, Parolini, O, Alviano, F, Bagnara, G P, Bilic, G, Bühring, H J, Evangelista, M, Hennerbichler, S, Liu, B, Magatti, M, Mao, N, Miki, T, Marongiu, F, Nakajima, H, Nikaido, T, Portmann-Lanz, C B, Sankar, V, Soncini, M, Stadler, G, Surbek, D, Takahashi, T A, Redl, H, Sakuragawa, N, Wolbank, S, Zeisberger, S M, Zisch, A H, and Storm, S C

Abstract

Placental tissue draws great interest as a source of cells for regenerative medicine because of the phenotypic plasticity of many of the cell types isolated from this tissue. Furthermore, placenta, which is involved in maintaining fetal tolerance, contains cells that display immunomodulatory properties. These two features could prove useful for future cell therapy-based clinical applications. Placental tissue is readily available and easily procured without invasive procedures, and its use does not elicit ethical debate. Numerous reports describing stem cells from different parts of the placenta, using nearly as numerous isolation and characterization procedures, have been published. Considering the complexity of the placenta, an urgent need exists to define, as clearly as possible, the region of origin and methods of isolation of cells derived from this tissue. On March 23-24, 2007, the first international Workshop on Placenta Derived Stem Cells was held in Brescia, Italy. Most of the research published in this area focuses on mesenchymal stromal cells isolated from various parts of the placenta or epithelial cells isolated from amniotic membrane. The aim of this review is to summarize and provide the state of the art of research in this field, addressing aspects such as cell isolation protocols and characteristics of these cells, as well as providing preliminary indications of the possibilities for use of these cells in future clinical applications

Published
2008

15. Hemostatic markers in Japanese patients undergoing anticoagulant therapy under thrombo-test monitoring

Author

Ikuma, H., primary, Wada, H., additional, Mori, Y., additional, Shimura, M., additional, Hiyoyama, K., additional, Nakasaki, T., additional, Nishikawa, M., additional, Onoda, K., additional, Yamada, N., additional, Ohta, T., additional, Nishioka, J., additional, Nobori, T., additional, Gabazza, E. C., additional, Sakuragawa, N., additional, and Shiku, H., additional

Published
1999
Full Text
View/download PDF

16. NPC1 gene mutations in Japanese patients with Niemann-Pick disease type C

Author

Yamamoto, T., primary, Nanba, E., additional, Ninomiya, H., additional, Higaki, K., additional, Zhang, H., additional, Akaboshi, S., additional, Watanabe, Y., additional, Takeshima, T., additional, Inui, K., additional, Okada, S., additional, Tanaka, A., additional, Sakuragawa, N., additional, Millat, G., additional, Vanier, M.T., additional, Morris, J.A., additional, Pentchev, P.G., additional, and Ohno, K., additional

Published
1999
Full Text
View/download PDF

27. Identification of new markers in Xp21 between DXS28 (C7) and DMD

Author

Worley, K.C., primary, Towbin, J.A., additional, Zhu, X.M., additional, Barker, D.F., additional, Ballabio, A., additional, Chamberlain, J., additional, Biesecker, L.G., additional, Blethen, S.L., additional, Brosnan, P., additional, Fox, J.E., additional, Rizzo, W.B., additional, Romeo, G., additional, Sakuragawa, N., additional, Seltzer, W.K., additional, Yamaguchi, S., additional, and McCabe, E.R.B., additional

Published
1992
Full Text
View/download PDF

35. Activation of heparin cofactor II by calcium spirulan.

Author

Hayakawa, Y, Hayashi, T, Lee, J B, Ozawa, T, and Sakuragawa, N

Abstract

Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate. Previous investigations have indicated that calcium spirulan (Ca-SP), a novel sulfated polysaccharide, enhanced the rate of inhibition of alpha-thrombin by HCII. In this study, we investigated the mechanism of the activation of HCII by Ca-SP. Interestingly, in the presence of Ca-SP, an N-terminal deletion mutant of HCII (rHCII-Delta74) inhibited alpha-thrombin, as native recombinant HCII (native rHCII) did. The second-order rate constant for the inhibition of alpha-thrombin by rHCII-Delta74 was 2.0 x 10(8) M(-1) min(-1) in the presence of 50 microgram/ml Ca-SP and 10, 000-fold higher than in the absence of Ca-SP. The rates of native rHCII and rHCII-Delta74 for the inhibition of gamma-thrombin were increased only 80- and 120-fold, respectively. Our results suggested that the anion-binding exosite I of alpha-thrombin was essential for the rapid inhibition reaction by HCII in the presence of Ca-SP and that the N-terminal acidic domain of HCII was not required. Therefore, we proposed a mechanism by which HCII was activated allosterically by Ca-SP and could interact with the anion-binding exosite I of thrombin not through the N-terminal acidic domain of HCII. The Arg(103) --> Leu mutant bound to Ca-SP-Toyopearl with normal affinity and inhibited alpha-thrombin in a manner similar to native rHCII. These results indicate that Arg(103) in HCII molecule is not critical for the interaction with Ca-SP.

Published
2000

42. Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability.

Author

Koide, T, Odani, S, Takahashi, K, Ono, T, and Sakuragawa, N

Abstract

Structural analyses of a hereditary abnormal antithrombin III, antithrombin III Toyama, which has normal progressive antithrombin activity but no heparin cofactor activity, have been carried out to elucidate the molecular abnormality causing recurrent thrombophlebitis of a patient and to identify an amino acid residue essential for the binding with heparin. Abnormal antithrombin III was reduced, S-pyridylethylated, and treated with cyanogen bromide. Eleven fragments were isolated by the combination of Sephadex G-50 gel filtration and reversed-phase HPLC and compared with those from normal antithrombin III. One large fragment (CN-III) that appeared to have a different amino acid composition from that of the corresponding fragment from normal antithrombin III was digested with trypsin, and the digests were separated by HPLC. The abnormal peptide was identified by comparing the peptide map with that from normal antithrombin III. Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama. One base mutation, C leads to T, in the 5' terminal position of the arginine-47 genetic codon (CGT) is probably responsible for this substitution. These results also suggest that arginine-47 is an essential amino acid residue for the binding with heparin.

Published
1984
Full Text
View/download PDF

46. Effects of dimethylsulfoxide on sphingomyelinase in cultured human fibroblasts and correction of sphingomyelinase deficiency in fibroblasts from Niemann-Pick patients

Author

Eijiro Satoyoshi, Sakuragawa N, Y. Yoshida, M. Sato, Arima M, and I. Kamo

Subjects
Hydrolases, Biophysics, Sphingomyelinase deficiency, Human skin, Biochemistry, hemic and lymphatic diseases, Humans, Dimethyl Sulfoxide, Molecular Biology, Cells, Cultured, Skin, Niemann-Pick Diseases, integumentary system, biology, Cell growth, Chemistry, Phosphoric Diester Hydrolases, Sphingomyelinase activity, Cell Biology, Fibroblasts, Enzyme assay, Sphingomyelin Phosphodiesterase, Enzyme Induction, biology.protein, Sphingomyelin, Lysosomes, Cell Division
Abstract

The effects of dimethylsulfoxide (DMSO) on sphingomyelinase activity were studied using human skin fibroblasts from normal individuals and Niemann-Pick patients. Sphingomyelinase activity in normal fibroblasts increased up to 230% of controls by 2% DMSO while the cell growth was inhibited. Other lysosomal hydrolases showed a rather smaller extent of increment in activity. There was no direct effect of DMSO in cell-free system and no evidence of any activating factor of sphingomyelinase in homogenates. Sphingomyelinase deficiency in fibroblasts from a Niemann-Pick patient (type C) was corrected by 2% DMSO with regaining its enzyme activity.

Published
1985

Catalog

Books, media, physical & digital resources
See catalog results