BIOCHEMICAL STUDIES ON THE FUNCTIONS OF CYTOPLASMIC ACTIN IN NON-MUSCLE CELLS

石浦, 正寛; イシウラ, マサヒロ

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04384_Dissertation	pdf	なし	2.61 MB	101	2015.03.16	論文/Dissertation
04384_Abstract	pdf	なし	74.4 KB	45	2014.06.19	要旨/Abstract

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タイトル	BIOCHEMICAL STUDIES ON THE FUNCTIONS OF CYTOPLASMIC ACTIN IN NON-MUSCLE CELLS
タイトル	非筋細胞におけるアクチン機能の生化学的研究
著者	NRID 1000020132730 1000020132730 著者名石浦, 正寛 ; イシウラ, マサヒロ
内容	Ishiura, Masahiro; Okada, Yoshio. THE ROLE OF ACTIN IN TEMPERATURE-DEPENDENT GEL-SOL TRANSFORMATION OF EXTRACTS OF EHRLICH ASCITES TUMOR CELLS. Journal of Cell Biology. 1979. 80(2), p.465-480.
抄録	Ehrlich ascites tumor cell extracts form a gel when warmed to 25 degrees C at pH 7.0 in sucrose solution, and the gel rapidly becomes a sol when cooled to 0 degrees C. This gel-sol transformation was studied quantitatively by determining the volume or the total protein of pellets of gel obtained by low-speed centrifugation. The gelation depended on nucleotide triphosphates, Mg2+, KCl, and a reducing agent. Gelation was inhibited reversibly by 0.5 microM free Ca2+, and 25--50 ng/ml of either cytochalasin B or D, but it was not affected by 10 mM colchicine. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that the gel was composed of six major proteins with mol wt greater than 300,000, 270,000, 89,000, 51,000, 48,000, and 42,000 daltons. The last component was identified as cell actin because it had the same molecular weight as muscle actin and bound with muscle myosin and tropomyosin. The role of actin in gelation was studied by use of actin-inhibitors. Gelation was inhibited by a chemically modified subfragment-1 of myosin, which binds with F-actin even in the presence of ATP, and by bovine pancreatic DNase I, which tightly binds with G- actin. Muscle G-actin neutralized the inhibitory effect of DNase I when added at an equimolar ratio to the latter, and it also restored gelation after its inhibition by DNase I. These findings suggest that gelation depends on actin. However, the extracts showed temperature- dependent, cytochalasin-sensitive, and Ca2+-regulated gelation as did the original extracts when the cell actin in the extracts was replaced by muscle actin, suggesting that components other than cell actin might be responsible for these characteristics of the gelation.
学位名	理学博士
学位授与年月日	1978-09-30
学位授与機関	大阪大学
研究科	理学
専攻	生理学
学位授与番号	甲第02117号
学位記番号	04384
言語	英語
ハンドルURL	https://hdl.handle.net/11094/2926
アクセス権	open access
権利情報	Copyright: Rockefeller University Press
出版タイプ	Version of Record
カテゴリ	博士論文本文あり / 理学研究科 / 1978年度
カテゴリ	博士論文 / 理学研究科 / 1978年度

資源タイプ	博士論文
ローカル資源タイプ	博士論文本文あり
ローカル資源タイプ	博士論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	大阪大学, 1978, 博士論文
DC.title	BIOCHEMICAL STUDIES ON THE FUNCTIONS OF CYTOPLASMIC ACTIN IN NON-MUSCLE CELLS
DC.title	非筋細胞におけるアクチン機能の生化学的研究
DC.creator	石浦, 正寛
DC.creator	イシウラ, マサヒロ
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DC.description	Ishiura, Masahiro; Okada, Yoshio. THE ROLE OF ACTIN IN TEMPERATURE-DEPENDENT GEL-SOL TRANSFORMATION OF EXTRACTS OF EHRLICH ASCITES TUMOR CELLS. Journal of Cell Biology. 1979. 80(2), p.465-480.
DCTERMS.abstract	Ehrlich ascites tumor cell extracts form a gel when warmed to 25 degrees C at pH 7.0 in sucrose solution, and the gel rapidly becomes a sol when cooled to 0 degrees C. This gel-sol transformation was studied quantitatively by determining the volume or the total protein of pellets of gel obtained by low-speed centrifugation. The gelation depended on nucleotide triphosphates, Mg2+, KCl, and a reducing agent. Gelation was inhibited reversibly by 0.5 microM free Ca2+, and 25--50 ng/ml of either cytochalasin B or D, but it was not affected by 10 mM colchicine. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that the gel was composed of six major proteins with mol wt greater than 300,000, 270,000, 89,000, 51,000, 48,000, and 42,000 daltons. The last component was identified as cell actin because it had the same molecular weight as muscle actin and bound with muscle myosin and tropomyosin. The role of actin in gelation was studied by use of actin-inhibitors. Gelation was inhibited by a chemically modified subfragment-1 of myosin, which binds with F-actin even in the presence of ATP, and by bovine pancreatic DNase I, which tightly binds with G- actin. Muscle G-actin neutralized the inhibitory effect of DNase I when added at an equimolar ratio to the latter, and it also restored gelation after its inhibition by DNase I. These findings suggest that gelation depends on actin. However, the extracts showed temperature- dependent, cytochalasin-sensitive, and Ca2+-regulated gelation as did the original extracts when the cell actin in the extracts was replaced by muscle actin, suggesting that components other than cell actin might be responsible for these characteristics of the gelation.
DCTERMS.issued' scheme='DCTERMS.W3CDTF	1978-09-30
DC.rights	Copyright: Rockefeller University Press
DC.format	application/pdf
DC.format	application/pdf
citation_title	BIOCHEMICAL STUDIES ON THE FUNCTIONS OF CYTOPLASMIC ACTIN IN NON-MUSCLE CELLS
citation_title	非筋細胞におけるアクチン機能の生化学的研究
citation_author	石浦, 正寛
citation_author	イシウラ, マサヒロ
citation_language	英語
citation_public_url	https://hdl.handle.net/11094/2926
citation_date	1978-09-30

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