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dc.contributor.authorPatel, Trushar R.
dc.contributor.authorNikodemus, Denise
dc.contributor.authorBesong, Tabot M.D.
dc.contributor.authorReuten, Raphael
dc.contributor.authorMeier, Markus
dc.contributor.authorHarding, Stephen E.
dc.contributor.authorWinzor, Donald J.
dc.contributor.authorKoch, Manuel
dc.contributor.authorStetefeld, Jörg
dc.date.accessioned2015-08-25T13:19:59Z
dc.date.available2015-08-25T13:19:59Z
dc.date.issued2015-07-26
dc.identifier.citationPatel 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.
dc.identifier.issn0945053X
dc.identifier.pmid26215696
dc.identifier.doi10.1016/j.matbio.2015.06.005
dc.identifier.urihttp://hdl.handle.net/10754/575931
dc.description.abstractLaminins 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.
dc.description.sponsorshipTRP 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).
dc.language.isoen
dc.publisherElsevier BV
dc.relation.urlhttp://linkinghub.elsevier.com/retrieve/pii/S0945053X15001237
dc.rightsArchived with thanks to Matrix Biology
dc.subjectAnalytical ultracentrifugation
dc.subjectCD spectroscopy
dc.subjectDynamic light scattering
dc.subjectExtracellular matrix
dc.subjectLaminin short arms
dc.subjectProtein self-association
dc.subjectSurface plasmon resonance
dc.titleBiophysical analysis of a lethal laminin alpha-1 mutation reveals altered self-interaction
dc.typeArticle
dc.contributor.departmentFunctional Nanomaterials Lab (FuNL)
dc.contributor.departmentKAUST Solar Center (KSC)
dc.identifier.journalMatrix Biology
dc.eprint.versionPost-print
dc.contributor.institutionDepartment of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba R3T 2N2, Canada
dc.contributor.institutionSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom
dc.contributor.institutionInstitute for Dental Research and Oral Musculoskeletal Biology and Center for Biochemistry, Medical Faculty, University of Cologne, Cologne 50931, Germany
dc.contributor.institutionNational Center for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington LE12 5RD, United Kingdom
dc.contributor.institutionSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personBesong, Tabot M.D.
refterms.dateFOA2016-07-26T00:00:00Z
dc.date.published-online2015-07-26
dc.date.published-print2016-01


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