EVIDENCE FOR FIBRONECTIN DEGRADATION BY CALPAIN-II

N ELAMRANI, Denis Pierre Balcerzak, M SORIANO, J J BRUSTIS, P COTTIN, S POUSSARD, A DUCASTAING

    Research output: Contribution to journalArticle

    11 Citations (Scopus)

    Abstract

    Recent work supports the hypothesis that calpain II can be exteriorized. Indeed, this cysteine calcium-dependent proteinase was shown to be intercellularly, and, more particularly, associated to extracellular matrix components. Thereby, calpain II could be involved in hydrolysis of pericellular matrix components such as fibronectin, which is known to play an important role in cellular differentiation. Our in vitro studies provide evidence that fibronectin is a potential substrate for calpain II. On cultured cells, our findings show that calpain II is able, on the one hand, to cleave the fibrillar network of fibronectin secreted by fibroblasts, and, on the other, to decrease dramatically the fibronectin amount secreted by myoblasts just before fusion. Moreover, following this treatment, myoblasts become spherical due to the cleavage of this attachment factor. However, these cells, plated on an appropriate substrate are still able to differentiate. Our results suggest that calpain II is indeed involved in myoblast fusion via the fibronectin cleavage since it is well established that myogenic lineages lose this glycoprotein at the time of fusion.

    Original languageEnglish
    Pages (from-to)849-853
    Number of pages5
    JournalBiochemistry and Cell Biology
    Volume75
    Issue number10
    Publication statusPublished - 1993

    Keywords

    • CALPAIN-II
    • FIBRONECTIN
    • CULTURE IN-VITRO
    • MYOBLASTS
    • MUSCLE

    Cite this

    ELAMRANI, N., Balcerzak, D. P., SORIANO, M., BRUSTIS, J. J., COTTIN, P., POUSSARD, S., & DUCASTAING, A. (1993). EVIDENCE FOR FIBRONECTIN DEGRADATION BY CALPAIN-II. Biochemistry and Cell Biology, 75(10), 849-853.

    EVIDENCE FOR FIBRONECTIN DEGRADATION BY CALPAIN-II. / ELAMRANI, N ; Balcerzak, Denis Pierre; SORIANO, M ; BRUSTIS, J J ; COTTIN, P ; POUSSARD, S ; DUCASTAING, A .

    In: Biochemistry and Cell Biology, Vol. 75, No. 10, 1993, p. 849-853.

    Research output: Contribution to journalArticle

    ELAMRANI, N, Balcerzak, DP, SORIANO, M, BRUSTIS, JJ, COTTIN, P, POUSSARD, S & DUCASTAING, A 1993, 'EVIDENCE FOR FIBRONECTIN DEGRADATION BY CALPAIN-II', Biochemistry and Cell Biology, vol. 75, no. 10, pp. 849-853.
    ELAMRANI N, Balcerzak DP, SORIANO M, BRUSTIS JJ, COTTIN P, POUSSARD S et al. EVIDENCE FOR FIBRONECTIN DEGRADATION BY CALPAIN-II. Biochemistry and Cell Biology. 1993;75(10):849-853.
    ELAMRANI, N ; Balcerzak, Denis Pierre ; SORIANO, M ; BRUSTIS, J J ; COTTIN, P ; POUSSARD, S ; DUCASTAING, A . / EVIDENCE FOR FIBRONECTIN DEGRADATION BY CALPAIN-II. In: Biochemistry and Cell Biology. 1993 ; Vol. 75, No. 10. pp. 849-853.
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    abstract = "Recent work supports the hypothesis that calpain II can be exteriorized. Indeed, this cysteine calcium-dependent proteinase was shown to be intercellularly, and, more particularly, associated to extracellular matrix components. Thereby, calpain II could be involved in hydrolysis of pericellular matrix components such as fibronectin, which is known to play an important role in cellular differentiation. Our in vitro studies provide evidence that fibronectin is a potential substrate for calpain II. On cultured cells, our findings show that calpain II is able, on the one hand, to cleave the fibrillar network of fibronectin secreted by fibroblasts, and, on the other, to decrease dramatically the fibronectin amount secreted by myoblasts just before fusion. Moreover, following this treatment, myoblasts become spherical due to the cleavage of this attachment factor. However, these cells, plated on an appropriate substrate are still able to differentiate. Our results suggest that calpain II is indeed involved in myoblast fusion via the fibronectin cleavage since it is well established that myogenic lineages lose this glycoprotein at the time of fusion.",
    keywords = "CALPAIN-II, FIBRONECTIN, CULTURE IN-VITRO, MYOBLASTS, MUSCLE",
    author = "N ELAMRANI and Balcerzak, {Denis Pierre} and M SORIANO and BRUSTIS, {J J} and P COTTIN and S POUSSARD and A DUCASTAING",
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    AU - ELAMRANI, N

    AU - Balcerzak, Denis Pierre

    AU - SORIANO, M

    AU - BRUSTIS, J J

    AU - COTTIN, P

    AU - POUSSARD, S

    AU - DUCASTAING, A

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    N2 - Recent work supports the hypothesis that calpain II can be exteriorized. Indeed, this cysteine calcium-dependent proteinase was shown to be intercellularly, and, more particularly, associated to extracellular matrix components. Thereby, calpain II could be involved in hydrolysis of pericellular matrix components such as fibronectin, which is known to play an important role in cellular differentiation. Our in vitro studies provide evidence that fibronectin is a potential substrate for calpain II. On cultured cells, our findings show that calpain II is able, on the one hand, to cleave the fibrillar network of fibronectin secreted by fibroblasts, and, on the other, to decrease dramatically the fibronectin amount secreted by myoblasts just before fusion. Moreover, following this treatment, myoblasts become spherical due to the cleavage of this attachment factor. However, these cells, plated on an appropriate substrate are still able to differentiate. Our results suggest that calpain II is indeed involved in myoblast fusion via the fibronectin cleavage since it is well established that myogenic lineages lose this glycoprotein at the time of fusion.

    AB - Recent work supports the hypothesis that calpain II can be exteriorized. Indeed, this cysteine calcium-dependent proteinase was shown to be intercellularly, and, more particularly, associated to extracellular matrix components. Thereby, calpain II could be involved in hydrolysis of pericellular matrix components such as fibronectin, which is known to play an important role in cellular differentiation. Our in vitro studies provide evidence that fibronectin is a potential substrate for calpain II. On cultured cells, our findings show that calpain II is able, on the one hand, to cleave the fibrillar network of fibronectin secreted by fibroblasts, and, on the other, to decrease dramatically the fibronectin amount secreted by myoblasts just before fusion. Moreover, following this treatment, myoblasts become spherical due to the cleavage of this attachment factor. However, these cells, plated on an appropriate substrate are still able to differentiate. Our results suggest that calpain II is indeed involved in myoblast fusion via the fibronectin cleavage since it is well established that myogenic lineages lose this glycoprotein at the time of fusion.

    KW - CALPAIN-II

    KW - FIBRONECTIN

    KW - CULTURE IN-VITRO

    KW - MYOBLASTS

    KW - MUSCLE

    M3 - Article

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    SP - 849

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    JO - Biochemistry and Cell Biology

    JF - Biochemistry and Cell Biology

    SN - 0829-8211

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    ER -