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Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation.

Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. Research Abstract Details 

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  • Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. Abstract Text:

    takanori aokiTakanori Aoki,daisuke satoDaisuke Sato,yingyi liYingyi Li,takahisa takinoTakahisa Takino,hisashi miyamoriHisashi Miyamori,hiroshi satoHiroshi Sato,

    Apolipoprotein E (apoE) in a human fetal brain cDNA library was identified, using the expression cloning method, as a gene product that formed a complex with latent matrix metalloproteinase (MMP)-2. Co-expression of membrane-type MMP-1 (MT1-MMP) with apoE in HEK293T cells reduced the amount of apoE secreted into the culture medium, whereas cell-associated apoE core protein was not affected. Incubation of native apoE protein with recombinant MT1-MMP resulted in the cleavage of apoE. Recombinant apoE protein fused to glutathione S-transferase (apoE-GST) was cleaved by MT1-MMP at the following peptide bonds; T(85)-M(86), K(93)-S(94), R(246)-L(247), A(255)-E(256) and G(296)-L(297). HT1080 cells transfected with the apoE gene, which express endogenous MT1-MMP, secreted a low level of apoE protein and its cleaved fragments, and treatment with MMP inhibitor BB94 induced accumulation of apoE and retardation of cell proliferation. Addition of apoE-GST protein to the culture of HEK293T cells suppressed cell proliferation, and stable transfection of the MT1-MMP gene partly abrogated the suppression. These results suggest that cleavage of apoE protein by MT1-MMP abrogates apoE-mediated suppression of cell proliferation.

    Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. Publishing Authors By Initials

    t aokiT Aoki,d satoD Sato,y liY Li,t takinoT Takino,h miyamoriH Miyamori,h satoH Sato,

    For similar thiophenes research abstracts see: thiophenes research

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    Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 137

    Page Numbers: 95-9

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jan

    YEAR: 2005

    Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. Keywords Mesh Terms:

    KEYWORDS: Thiophenes

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. Information

    Substance Name: Metalloendopeptidases

    Registry Number: EC 3.4.24.-

    Grant and Affiliation Information for Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation.

    AFFILIATION: Department of Molecular Virology and Oncology, Cancer Research Institute, Kanazawa University, 13-1 Takara-machi, Kanazawa 920-0934, Japan.

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: J Biochem

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