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    Biophysical analysis of a lethal laminin alpha-1 mutation reveals altered self-interaction

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    Type
    Article
    Authors
    Patel, Trushar R. cc
    Nikodemus, Denise
    Besong, Tabot M.D. cc
    Reuten, Raphael
    Meier, Markus
    Harding, Stephen E.
    Winzor, Donald J.
    Koch, Manuel
    Stetefeld, Jörg
    KAUST Department
    Functional Nanomaterials Lab (FuNL)
    KAUST Solar Center (KSC)
    Date
    2015-07-26
    Online Publication Date
    2015-07-26
    Print Publication Date
    2016-01
    Permanent link to this record
    http://hdl.handle.net/10754/575931
    
    Metadata
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    Abstract
    Laminins are key basement membrane molecules that influence several biological activities and are linked to a number of diseases. They are secreted as heterotrimeric proteins consisting of one α, one β, and one γ chain, followed by their assembly into a polymer-like sheet at the basement membrane. Using sedimentation velocity, dynamic light scattering, and surface plasmon resonance experiments, we studied self-association of three laminin (LM) N-terminal fragments α-1 (hLM α-1 N), α-5 (hLM α-5 N) and β-3 (hLM β-3 N) originating from the short arms of the human laminin αβγ heterotrimer. Corresponding studies of the hLM α-1 N C49S mutant, equivalent to the larval lethal C56S mutant in zebrafish, have shown that this mutation causes enhanced self-association behavior, an observation that provides a plausible explanation for the inability of laminin bearing this mutation to fulfill functional roles in vivo, and hence for the deleterious pathological consequences of the mutation on lens function.
    Citation
    Patel TR, Nikodemus D, Besong TMD, Reuten R, Meier M, et al. (2015) Biophysical analysis of a lethal laminin alpha-1 mutation reveals altered self-interaction. Matrix Biology. Available: http://dx.doi.org/10.1016/j.matbio.2015.06.005.
    Sponsors
    TRP was the recipient of a Canadian Institutes of Health Research postdoctoral fellowship and is currently supported by the Marie Skłodowska-Curie Fellowship. JS holds a Canada Research Chair in Structure Biology. This investigation was supported in part by the Multiple Sclerosis Society of Canada and by the Canadian Institute of Health Research (RPA-109759).
    Publisher
    Elsevier BV
    Journal
    Matrix Biology
    DOI
    10.1016/j.matbio.2015.06.005
    PubMed ID
    26215696
    Additional Links
    http://linkinghub.elsevier.com/retrieve/pii/S0945053X15001237
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.matbio.2015.06.005
    Scopus Count
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    Articles; KAUST Solar Center (KSC)

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