Viscoelastic behavior of human lamin A proteins in the context of dilated cardiomyopathy
Lamins are intermediate filament proteins of type V constituting a nuclear lamina or filamentous meshwork which lines the nucleoplasmic side of the inner nuclear membrane. This protein mesh provides a supporting scaffold for the nuclear envelope and tethers interphase chromosome to the nuclear perip...
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| description | Lamins are intermediate filament proteins of type V constituting a nuclear lamina or filamentous meshwork which lines the nucleoplasmic side of the inner nuclear membrane. This protein mesh provides a supporting scaffold for the nuclear envelope and tethers interphase chromosome to the nuclear periphery. Mutations of mainly A-type lamins are found to be causative for at least 11 human diseases collectively termed as laminopathies majority of which are characterised by aberrant nuclei with altered structural rigidity, deformability and poor mechanotransduction behaviour. But the investigation of viscoelastic behavior of lamin A continues to elude the field. In order to address this problem, we hereby present the very first report on viscoelastic properties of wild type human lamin A and some of its mutants linked with Dilated cardiomyopathy (DCM) using quantitative rheological measurements. We observed a dramatic strain-softening effect on lamin A network as an outcome of the strain amplitude sweep measurements which could arise from the large compliance of the quasi-cross-links in the network or that of the lamin A rods. In addition, the drastic stiffening of the differential elastic moduli on superposition of rotational and oscillatory shear stress reflect the increase in the stiffness of the laterally associated lamin A rods. These findings present a preliminary insight into distinct biomechanical properties of wild type lamin A protein and its mutants which in turn revealed interesting differences. |
| doi_str_mv | 10.1371/journal.pone.0083410 |
| format | Article |
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This protein mesh provides a supporting scaffold for the nuclear envelope and tethers interphase chromosome to the nuclear periphery. Mutations of mainly A-type lamins are found to be causative for at least 11 human diseases collectively termed as laminopathies majority of which are characterised by aberrant nuclei with altered structural rigidity, deformability and poor mechanotransduction behaviour. But the investigation of viscoelastic behavior of lamin A continues to elude the field. In order to address this problem, we hereby present the very first report on viscoelastic properties of wild type human lamin A and some of its mutants linked with Dilated cardiomyopathy (DCM) using quantitative rheological measurements. We observed a dramatic strain-softening effect on lamin A network as an outcome of the strain amplitude sweep measurements which could arise from the large compliance of the quasi-cross-links in the network or that of the lamin A rods. In addition, the drastic stiffening of the differential elastic moduli on superposition of rotational and oscillatory shear stress reflect the increase in the stiffness of the laterally associated lamin A rods. These findings present a preliminary insight into distinct biomechanical properties of wild type lamin A protein and its mutants which in turn revealed interesting differences.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0083410</identifier><identifier>PMID: 24386194</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Aberration ; Biology ; Biomechanics ; Biophysics ; Cardiomyopathy ; Cardiomyopathy, Dilated - genetics ; Cardiomyopathy, Dilated - metabolism ; Cardiomyopathy, Dilated - pathology ; Cell Line ; Congestive cardiomyopathy ; Crosslinking ; Deformability ; Deformation mechanisms ; Dilated cardiomyopathy ; Elasticity ; Formability ; Gene Expression ; Genetic aspects ; Genomics ; Human behavior ; Humans ; Hypotheses ; Intermediate filament proteins ; Lamin Type A - chemistry ; Lamin Type A - genetics ; Lamin Type A - metabolism ; Lamin Type A - ultrastructure ; Lamins ; Mechanical properties ; Mechanotransduction ; Medicine ; Membrane proteins ; Microscopy ; Modulus of elasticity ; Mutants ; Mutation ; Nuclear physics ; Nuclei ; Protein Folding ; Proteins ; Rheological properties ; Rigidity ; Rods ; Shear Strength ; Shear stress ; Stem cells ; Stiffening ; Stiffness ; Studies ; Tethers ; Viscoelasticity ; Viscosity ; Xenopus</subject><ispartof>PloS one, 2013-12, Vol.8 (12), p.e83410-e83410</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Banerjee et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Banerjee et al 2013 Banerjee et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-5b2daa3258dfc4e25a04d883463e71c3648c099f31ce8c336ab9199b84a504b3</citedby><cites>FETCH-LOGICAL-c758t-5b2daa3258dfc4e25a04d883463e71c3648c099f31ce8c336ab9199b84a504b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3875444/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3875444/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24386194$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Das, Anindita</contributor><creatorcontrib>Banerjee, Avinanda</creatorcontrib><creatorcontrib>Rathee, Vikram</creatorcontrib><creatorcontrib>Krishnaswamy, Rema</creatorcontrib><creatorcontrib>Bhattacharjee, Pritha</creatorcontrib><creatorcontrib>Ray, Pulak</creatorcontrib><creatorcontrib>Sood, Ajay K</creatorcontrib><creatorcontrib>Sengupta, Kaushik</creatorcontrib><title>Viscoelastic behavior of human lamin A proteins in the context of dilated cardiomyopathy</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Lamins are intermediate filament proteins of type V constituting a nuclear lamina or filamentous meshwork which lines the nucleoplasmic side of the inner nuclear membrane. This protein mesh provides a supporting scaffold for the nuclear envelope and tethers interphase chromosome to the nuclear periphery. Mutations of mainly A-type lamins are found to be causative for at least 11 human diseases collectively termed as laminopathies majority of which are characterised by aberrant nuclei with altered structural rigidity, deformability and poor mechanotransduction behaviour. But the investigation of viscoelastic behavior of lamin A continues to elude the field. In order to address this problem, we hereby present the very first report on viscoelastic properties of wild type human lamin A and some of its mutants linked with Dilated cardiomyopathy (DCM) using quantitative rheological measurements. We observed a dramatic strain-softening effect on lamin A network as an outcome of the strain amplitude sweep measurements which could arise from the large compliance of the quasi-cross-links in the network or that of the lamin A rods. In addition, the drastic stiffening of the differential elastic moduli on superposition of rotational and oscillatory shear stress reflect the increase in the stiffness of the laterally associated lamin A rods. These findings present a preliminary insight into distinct biomechanical properties of wild type lamin A protein and its mutants which in turn revealed interesting differences.</description><subject>Aberration</subject><subject>Biology</subject><subject>Biomechanics</subject><subject>Biophysics</subject><subject>Cardiomyopathy</subject><subject>Cardiomyopathy, Dilated - genetics</subject><subject>Cardiomyopathy, Dilated - metabolism</subject><subject>Cardiomyopathy, Dilated - pathology</subject><subject>Cell Line</subject><subject>Congestive cardiomyopathy</subject><subject>Crosslinking</subject><subject>Deformability</subject><subject>Deformation mechanisms</subject><subject>Dilated cardiomyopathy</subject><subject>Elasticity</subject><subject>Formability</subject><subject>Gene Expression</subject><subject>Genetic aspects</subject><subject>Genomics</subject><subject>Human behavior</subject><subject>Humans</subject><subject>Hypotheses</subject><subject>Intermediate filament proteins</subject><subject>Lamin Type A - chemistry</subject><subject>Lamin Type A - genetics</subject><subject>Lamin Type A - metabolism</subject><subject>Lamin Type A - ultrastructure</subject><subject>Lamins</subject><subject>Mechanical properties</subject><subject>Mechanotransduction</subject><subject>Medicine</subject><subject>Membrane proteins</subject><subject>Microscopy</subject><subject>Modulus of elasticity</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Nuclear physics</subject><subject>Nuclei</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Rheological properties</subject><subject>Rigidity</subject><subject>Rods</subject><subject>Shear Strength</subject><subject>Shear stress</subject><subject>Stem cells</subject><subject>Stiffening</subject><subject>Stiffness</subject><subject>Studies</subject><subject>Tethers</subject><subject>Viscoelasticity</subject><subject>Viscosity</subject><subject>Xenopus</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNkluL1DAUx4so7kW_gWhBEH2YMWnSpnkRhsXLwMKCLotv4TRNpxnSZjZJF-fbb-p0l6nsg-Qhycnv_E_OJUneYLTEhOHPWzu4HsxyZ3u1RKgkFKNnySnmJFsUGSLPj84nyZn3W4RyUhbFy-Qko_GAOT1Nft9oL60y4IOWaaVauNPWpbZJ26GDPjXQ6T5dpTtng9K9T-MttCqVtg_qTxjBWhsIqk4luFrbbm93ENr9q-RFA8ar19N-nlx_-3p98WNxefV9fbG6XEiWl2GRV1kNQLK8rBtJVZYDonUZkymIYliSgpYScd4QLFUpCSmg4pjzqqSQI1qR8-TdQXZnrBdTTbzAlGUI05zwSKwPRG1hK3ZOd-D2woIWfw3WbQS4mLxRguaKg2I1ZKimFcuqjFLIGlk1jEhSjVpfpmhD1alaqj44MDPR-UuvW7Gxd4KULKeURoGPk4Czt4PyQXSx_soY6JUdxn9zVHBGMIvo-3_Qp7ObqA3EBHTf2BhXjqJiRRnjhDGGI7V8goqrVp2OrVSNjvaZw6eZw9TuDQzei_Wvn__PXt3M2Q9HbKvAhNZbMwRtez8H6QGUznrvVPNYZIzEOP8P1RDj_Itp_qPb2-MGPTo9DDy5B6OZAFQ</recordid><startdate>20131230</startdate><enddate>20131230</enddate><creator>Banerjee, Avinanda</creator><creator>Rathee, Vikram</creator><creator>Krishnaswamy, Rema</creator><creator>Bhattacharjee, Pritha</creator><creator>Ray, Pulak</creator><creator>Sood, Ajay K</creator><creator>Sengupta, Kaushik</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20131230</creationdate><title>Viscoelastic behavior of human lamin A proteins in the context of dilated cardiomyopathy</title><author>Banerjee, Avinanda ; Rathee, Vikram ; Krishnaswamy, Rema ; Bhattacharjee, Pritha ; Ray, Pulak ; Sood, Ajay K ; Sengupta, Kaushik</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-5b2daa3258dfc4e25a04d883463e71c3648c099f31ce8c336ab9199b84a504b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Aberration</topic><topic>Biology</topic><topic>Biomechanics</topic><topic>Biophysics</topic><topic>Cardiomyopathy</topic><topic>Cardiomyopathy, Dilated - genetics</topic><topic>Cardiomyopathy, Dilated - metabolism</topic><topic>Cardiomyopathy, Dilated - pathology</topic><topic>Cell Line</topic><topic>Congestive cardiomyopathy</topic><topic>Crosslinking</topic><topic>Deformability</topic><topic>Deformation mechanisms</topic><topic>Dilated cardiomyopathy</topic><topic>Elasticity</topic><topic>Formability</topic><topic>Gene Expression</topic><topic>Genetic aspects</topic><topic>Genomics</topic><topic>Human behavior</topic><topic>Humans</topic><topic>Hypotheses</topic><topic>Intermediate filament proteins</topic><topic>Lamin Type A - chemistry</topic><topic>Lamin Type A - genetics</topic><topic>Lamin Type A - metabolism</topic><topic>Lamin Type A - ultrastructure</topic><topic>Lamins</topic><topic>Mechanical properties</topic><topic>Mechanotransduction</topic><topic>Medicine</topic><topic>Membrane proteins</topic><topic>Microscopy</topic><topic>Modulus of elasticity</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Nuclear physics</topic><topic>Nuclei</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Rheological properties</topic><topic>Rigidity</topic><topic>Rods</topic><topic>Shear Strength</topic><topic>Shear stress</topic><topic>Stem cells</topic><topic>Stiffening</topic><topic>Stiffness</topic><topic>Studies</topic><topic>Tethers</topic><topic>Viscoelasticity</topic><topic>Viscosity</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Banerjee, Avinanda</creatorcontrib><creatorcontrib>Rathee, Vikram</creatorcontrib><creatorcontrib>Krishnaswamy, Rema</creatorcontrib><creatorcontrib>Bhattacharjee, Pritha</creatorcontrib><creatorcontrib>Ray, Pulak</creatorcontrib><creatorcontrib>Sood, Ajay K</creatorcontrib><creatorcontrib>Sengupta, Kaushik</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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This protein mesh provides a supporting scaffold for the nuclear envelope and tethers interphase chromosome to the nuclear periphery. Mutations of mainly A-type lamins are found to be causative for at least 11 human diseases collectively termed as laminopathies majority of which are characterised by aberrant nuclei with altered structural rigidity, deformability and poor mechanotransduction behaviour. But the investigation of viscoelastic behavior of lamin A continues to elude the field. In order to address this problem, we hereby present the very first report on viscoelastic properties of wild type human lamin A and some of its mutants linked with Dilated cardiomyopathy (DCM) using quantitative rheological measurements. We observed a dramatic strain-softening effect on lamin A network as an outcome of the strain amplitude sweep measurements which could arise from the large compliance of the quasi-cross-links in the network or that of the lamin A rods. In addition, the drastic stiffening of the differential elastic moduli on superposition of rotational and oscillatory shear stress reflect the increase in the stiffness of the laterally associated lamin A rods. These findings present a preliminary insight into distinct biomechanical properties of wild type lamin A protein and its mutants which in turn revealed interesting differences.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24386194</pmid><doi>10.1371/journal.pone.0083410</doi><tpages>e83410</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2013-12, Vol.8 (12), p.e83410-e83410 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1472014539 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Aberration Biology Biomechanics Biophysics Cardiomyopathy Cardiomyopathy, Dilated - genetics Cardiomyopathy, Dilated - metabolism Cardiomyopathy, Dilated - pathology Cell Line Congestive cardiomyopathy Crosslinking Deformability Deformation mechanisms Dilated cardiomyopathy Elasticity Formability Gene Expression Genetic aspects Genomics Human behavior Humans Hypotheses Intermediate filament proteins Lamin Type A - chemistry Lamin Type A - genetics Lamin Type A - metabolism Lamin Type A - ultrastructure Lamins Mechanical properties Mechanotransduction Medicine Membrane proteins Microscopy Modulus of elasticity Mutants Mutation Nuclear physics Nuclei Protein Folding Proteins Rheological properties Rigidity Rods Shear Strength Shear stress Stem cells Stiffening Stiffness Studies Tethers Viscoelasticity Viscosity Xenopus |
| title | Viscoelastic behavior of human lamin A proteins in the context of dilated cardiomyopathy |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T22%3A27%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Viscoelastic%20behavior%20of%20human%20lamin%20A%20proteins%20in%20the%20context%20of%20dilated%20cardiomyopathy&rft.jtitle=PloS%20one&rft.au=Banerjee,%20Avinanda&rft.date=2013-12-30&rft.volume=8&rft.issue=12&rft.spage=e83410&rft.epage=e83410&rft.pages=e83410-e83410&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0083410&rft_dat=%3Cgale_plos_%3EA477937771%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1472014539&rft_id=info:pmid/24386194&rft_galeid=A477937771&rft_doaj_id=oai_doaj_org_article_45e9ae7da20d4b72b244a2fcbf73c3b9&rfr_iscdi=true |