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Anti-apoptotic effect by Bcl-2 in UVB-irradiated keratinocytes.
Takahashi, Hidetoshi,Honma, Masaru,Ishida-Yamamoto, Akemi,Namikawa, Kazuhiko,Miwa, Akiko,Okado, Haruo,Kiyama, Hiroshi,Iizuka, Hajime Korean Society of Photoscience 2002 Journal of Photosciences Vol.9 No.2
Bcl-2 is a member of large bcl-2 family and protects cells from apoptosis. Using bcl-2-expressing adenovirus vector (Ad-bc1-2), we investigated the effect of bc1-2 on UVB-induced apoptosis. Adenovirus vector efficiently introduced bc1-2 gene in cultured normal mouse keratinocytes (NMK cells); almost all NMK cells (lx10$^{6}$ ) were transfected at Ixl0$^{8}$ PFU/ml. Bcl-2-transfected NMK cells were significantly resistant to UVB-induced apoptosis with the suppressive effect dependent on bcl-2-expression level. Following UVB irradiation caspase 8, 3, 9 activities were stimulated in NMK cells, while in bc1-2-transfected cells, only caspase 8, but not caspase 3 or 9 activities were stimulated. In order to investigate the effect of bc1-2 in vivo, topical application of Ad-bc1-2 on tape-stripped mouse skin was performed. Following the application, Bc1-2 was efficiently overexpressed in almost all viable keratinocytes. The expression was transient with the maximal expression of Bc1-2 at 1st day following the application of lxl0$^{9}$ PFU in 200ml. The introduced Bc1-2 remained at least for 6 days. UVB irradiation (1250 J/m$^2$) induced apoptosis within 12 h and the maximal effect was observed at 24 h in control mouse skin. Bc1-2-transfected mice skin were resistant to UVB-induced apoptosis. Topical application of empty adenovirus vector alone had no effect on Bc1-2 expression or UVB-induced apoptosis. These results indicate that adenovirus vector is an efficient gene delivery system into keratinocytes and that Bcl-2 is a potent inhibitor of UVB-induced apoptosis both in vitro and in vivo.
Ammar, Youssef Ben,Matsubara, Takayoshi,Ito, Kazuo,Iizuka, Masaru,Limpaseni, Tipaporn,Pongsawasdi, Piamsook,Minamiura, Noshi 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.6
An $\alpha$-amylase (EC 3.2.1.1) was purified that catalyses the production of a high level of maltose from starch without the attendant production of glucose. The enzyme was produced extracellularly by thermophilic Streptomyces sp. that was isolated from Thailand's soil. Purification was achieved by alcohol precipiation, DEAE-Cellulose, and Gel filtration chromatographies. The purified enzyme exhibited maximum activity at pH 6-7 and $60^{\circ}C$. It had a relative molecular mass of 45 kDa, as determined by SDS-PAGE. The hydrolysis products from starch had $\alpha$-anomeric forms, as determined by $^1H$-NMR. This maltose-forming $\alpha$-amylase completely hydrolyzed the soluble starch to produce a high level of maltose, representing up to 90%. It hydrolyzed maltotetrose and maltotriose to primarily produce maltose (82% and 62%, repectively) without the attendant production of glucose. The high maltose level as a final end-product from starch and maltooligosaccharides, and the unique action pattern of this enzyme, indicate an unusual maltose-forming system. After the addition of the enzyme in the bread-baking process, the bread's volume increased and kept its softness longer than when the bread had no enzyme.
Stabilization of Amylolytic Enzymes by Modification with Periodate-Oxidized Soluble Starch
Ann, Yong-Geun,Anindyawati, Trisaniti,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi 한국식품영양학회 1998 韓國食品營養學會誌 Vol.11 No.5
The stabilization of amylolytic enzyme such as β-amylase of barley, β-amylase of wheat, β-amylase of sweet potato, α-amylase of Bacillus licheniformis, α-amylase of Aspergillus sp. and α-glucosidase of Aspergillus awamori was attained by modification with periodate-oxidized soluble starch. The pH stability of modified enzyme was increased at pH 9 for β-amylase of sweet potato, pH 3∼5 and 8∼11 for β-amylase of barley, pH 2∼3 and 7∼12 for β-amylase of wheat and pH 6 for α-glucosidase of Aspergillus awamori. Thermal stability increased 17.6% for α-amylase of Aspergillus sp. at 60℃ for 10min, 30% for α-amylase of Bacillus licheniformis at 100℃ for 5min and 4.5% for α-amylase of sweet potato at 60℃ for 10min compared with those of native enzymes.
Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11
Matsubara, Takayoshi,Ammar, Youssef Ben,Anindyawati, Trisanti,Yamamoto, Satoru,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.4
Raw-starch-digesting $\alpha$-amylase (Amyl III) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT-11 using wheat bran in the medium. The purified Amyl III digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl III were maltotriose and maltose, although a small amount of glucose was produced. Amyl III acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl III on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl III and GA I was observed for the digestion of raw starch granules.
Degradation of Raw Starch Granules by α-Amylase Purified from Culture of Aspergillus awamori KT-11
( Takayoshi Matsubara ),( Youssef Ben Ammar ),( Trisanti Anindyawati ),( Satoru Yamamoto ),( Kazuo Ito ),( Masaru Iizuka ),( Noshi Minamiura ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.4
Raw-starch-digesting α-amylase (Amyl Ⅲ) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT 11 using wheat bran in the medium. The purified Amyl Ⅲ digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl Ⅲ were maltotriose and maltose, although a small amount of glucose was produced. Amyl Ⅲ acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl Ⅲ on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl Ⅲ and GA I was observed for the digestion of raw starch granules.
Matsubara, Takayoshi,Ammar, Youssef Ben,Anindyawati, Trisanti,Yamamoto, Satoru,Ito, Kazuo,Iizuka, Masaru,Minamiura, Noshi Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.4
Complementary DNAs encoding $\alpha$-amylases (Amyl I, Amyl III) and glucoamylase (GA I) were cloned from Aspergillus awamori KT-11 and their nucleotide sequences were determined. The sequence of Amyl III that was a raw starch digesting $\alpha$-amylase was found to consist of a 1,902 bp open reading frame encoding 634 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. On the other hand, the sequence of Amyl I, which cannot act on raw starch, consisted of a 1,500 bp ORF encoding 499 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. The sequence of GA I consisted of a 1,920 bp ORF that encoded 639 amino acids. The signal peptide was composed of 24 amino acids. The amino acid sequence of Amyl III from the N-terminus to the amino acid number 499 showed 63.3% homology with Amyl I. However, the amino acid sequence from the amino acid number 501 to C-terminus, including the raw-starch-affinity site and the TS region rich in threonine and serine, showed 66.9% homology with GA I.
( Takayoshi Matsubara ),( Youssef Ben Ammar ),( Trisanti Anindyawati ),( Satoru Yamamoto ),( Kazuo Ito ),( Masaru Iizuka ),( Noshi Minamiura ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.4
Complementary DNAs encoding α-amylases (Amyl I, Amyl Ⅲ) and glucoamylase (GA I) were cloned from Aspergillus awamori KT-11 and their nucleotide sequences were determined. The sequence of Amyl Ⅲ that was a raw starch digesting α-amylase was found to consist of a 1,902 bp open reading frame encoding 634 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. On the other hand, the sequence of Amyl I, which cannot act on raw starch, consisted of a 1,500 bp ORF encoding 499 amino acids. The signal peptide of the enzyme was composed of 21 amino acids. The sequence of GA I consisted of a 1,920 bp ORF that encoded 639 amino acids. The signal peptide was composed of 24 amino acids. The amino acid sequence of Amyl III from the N-terminus to the amino acid number 499 showed 633% homology with Amyl I. However, the amino acid sequence from the amino acid number 501 to C-terminus, including the rawstarch-affinity site and the TS region rich in threonine and serine, showed 66.9% homology with GA I.