pICln and Cytosolic F-Actin Constitute a Heteromeric Complex with a Constant Molecular Mass in Rat Skeletal Muscles.
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概要
- 論文の詳細を見る
To elucidate the function of pICln, its localization in subcellular organellae was investigated. A specific polyclonal anti-pICln antibody detected the soluble 38-kDa pICln exclusively in the cytosols of rat heart, lung, liver, spleen, skeletal muscle, testis, and brain, but not rat kidney. pICln-associated proteins in skeletal muscle were also analyzed. Native-gradient PAGE showed a single 340-kDa protein band reactive to anti-pICln antibody. This band also stained with anti-actin antibody. Two-dimensional PAGE and immunoprecipitation analysis indicated that all of the pICln was present in association with actin of a constant length: the molecular ratio of pICln to actin was roughly 1:7. In addition, all actin in the cytosol fractions was found in association with pICln. These results suggest the possibility that skeletal muscle pICln controls the length of cytosolic F-actin.
- 社団法人 日本生化学会の論文
著者
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Tazawa Hiroshi
Department Of Orthopaedic Surgery Akita University School Of Medicine
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LI Yuanyuan
Second Department of Biochemistry Akita University School of Medicine
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TAO Guozhong
Second Department of Biochemistry Akita University School of Medicine
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ITOH Hideaki
Second Department of Biochemistry Akita University School of Medicine
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TASHIMA Yohtalou
Second Department of Biochemistry Akita University School of Medicine
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Nagasawa Hiroyuki
Department Of Industrial Engineering College Of Engineering Osaka Prefecture University
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KOBAYASHI Akira
Second Department of Internal Medicine, Nagoya University School of Medicine
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- pICln and Cytosolic F-Actin Constitute a Heteromeric Complex with a Constant Molecular Mass in Rat Skeletal Muscles.