pIClnand Cytosolic F-Actin Constitute a Heteromeric Complex with a Constant Molecular Mass in Rat Skeletal Muscles

To elucidate the function of pIC1n, its localization in subcellular organellae was investigated. A specific polyclonal anti-pIC1n antibody detected the soluble 38-kDa plC1n exclusively in the cytosols of rat heart, lung, liver, spleen, skeletal muscle, testis, and brain, but not rat kidney, plC1n -a...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1999-10, Vol.126 (4), p.643-649
Main Authors: Li, Yuanyuan, Tao, Guozhong, Nagasawa, Hiroyuki, Tazawa, Hiroshi, Kobayashi, Akira, Itoh, Hideaki, Tashima, Yohtalou
Format: Article
Language:English
Subjects:
F-actin
native PAGE
pIC1n skeletal muscle
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Summary:To elucidate the function of pIC1n, its localization in subcellular organellae was investigated. A specific polyclonal anti-pIC1n antibody detected the soluble 38-kDa plC1n exclusively in the cytosols of rat heart, lung, liver, spleen, skeletal muscle, testis, and brain, but not rat kidney, plC1n -associated proteins in skeletal muscle were also analyzed. Native-gradient PAGE showed a single 340-kDa protein band reactive to anti-pIC1n antibody. This band also stained with anti-actin antibody. Two-dimensional PAGE and immunoprecipitation analysis indicated that all of the pIC1n was present in association with actin of a constant length: the molecular ratio of plcm to actin was roughly 1: 7. In addition, all actin in the cytosol fractions was found in association with pIC1n- These results suggest the possibility that skeletal muscle plC1n controls the length of cytosolic F-actin.
ISSN:0021-924X
DOI:10.1093/oxfordjournals.jbchem.a022497