A mathematical model for the dependence of keratin aggregate formation on the quantity of mutant keratin expressed in EGFP-K14 R125P keratinocytes
We examined keratin aggregate formation and the possible mechanisms involved. With this aim, we observed the effect that different ratios between mutant and wild-type keratins expressed in cultured keratinocytes may have on aggregate formation in vitro, as well as how keratin aggregate formation aff...
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| Veröffentlicht in: | PloS one 2021-12, Vol.16 (12), p.e0261227-e0261227 |
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| creator | Gouveia, Marcos Sorčan, Tjaša Zemljič-Jokhadar, Špela Travasso, Rui D M Liović, Mirjana |
| description | We examined keratin aggregate formation and the possible mechanisms involved. With this aim, we observed the effect that different ratios between mutant and wild-type keratins expressed in cultured keratinocytes may have on aggregate formation in vitro, as well as how keratin aggregate formation affects the mechanical properties of cells at the cell cortex. To this end we prepared clones with expression rates as close as possible to 25%, 50% and 100% of the EGFP-K14 proteins (either WT or R125P and V270M mutants). Our results showed that only in the case of the 25% EGFP-K14 R125P mutant significant differences could be seen. Namely, we observed in this case the largest accumulation of keratin aggregates and a significant reduction in cell stiffness. To gain insight into the possible mechanisms behind this observation, we extended our previous mathematical model of keratin dynamics by implementing a more complex reaction network that considers the coexistence of wild-type and mutant keratins in the cell. The new model, consisting of a set of coupled, non-linear, ordinary differential equations, allowed us to draw conclusions regarding the relative amounts of intermediate filaments and aggregates in cells, and suggested that aggregate formation by asymmetric binding between wild-type and mutant keratins could explain the data obtained on cells grown in culture. |
| doi_str_mv | 10.1371/journal.pone.0261227 |
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With this aim, we observed the effect that different ratios between mutant and wild-type keratins expressed in cultured keratinocytes may have on aggregate formation in vitro, as well as how keratin aggregate formation affects the mechanical properties of cells at the cell cortex. To this end we prepared clones with expression rates as close as possible to 25%, 50% and 100% of the EGFP-K14 proteins (either WT or R125P and V270M mutants). Our results showed that only in the case of the 25% EGFP-K14 R125P mutant significant differences could be seen. Namely, we observed in this case the largest accumulation of keratin aggregates and a significant reduction in cell stiffness. To gain insight into the possible mechanisms behind this observation, we extended our previous mathematical model of keratin dynamics by implementing a more complex reaction network that considers the coexistence of wild-type and mutant keratins in the cell. The new model, consisting of a set of coupled, non-linear, ordinary differential equations, allowed us to draw conclusions regarding the relative amounts of intermediate filaments and aggregates in cells, and suggested that aggregate formation by asymmetric binding between wild-type and mutant keratins could explain the data obtained on cells grown in culture.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0261227</identifier><identifier>PMID: 34962936</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Aggregates ; Analysis ; Biology and Life Sciences ; Cell culture ; Cell Line ; Cloning ; Computer Simulation ; Differential equations ; Filaments ; Fluorescent Dyes - chemistry ; Green Fluorescent Proteins - metabolism ; Humans ; Intermediate filaments ; Keratin ; Keratinocytes ; Keratinocytes - drug effects ; Keratinocytes - metabolism ; Keratins - chemistry ; Mathematical analysis ; Mathematical models ; Mechanical properties ; Medicine and Health Sciences ; Models, Biological ; Mutant Proteins - chemistry ; Mutants ; Mutation ; Ordinary differential equations ; Physical Sciences ; Physics ; Properties ; Proteasome Inhibitors - pharmacology ; Protein Aggregates - drug effects ; Proteins ; Research and Analysis Methods ; Stiffness</subject><ispartof>PloS one, 2021-12, Vol.16 (12), p.e0261227-e0261227</ispartof><rights>COPYRIGHT 2021 Public Library of Science</rights><rights>2021 Gouveia 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>2021 Gouveia et al 2021 Gouveia et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c641t-1006862b0cee665068a9779bb46005feb425f922595bc499becdefb1c3722c2a3</cites><orcidid>0000-0001-6078-0721 ; 0000-0002-2552-9993</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8714116/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8714116/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2101,2927,23865,27923,27924,53790,53792,79471,79472</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34962936$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Xu, Jian</contributor><creatorcontrib>Gouveia, Marcos</creatorcontrib><creatorcontrib>Sorčan, Tjaša</creatorcontrib><creatorcontrib>Zemljič-Jokhadar, Špela</creatorcontrib><creatorcontrib>Travasso, Rui D M</creatorcontrib><creatorcontrib>Liović, Mirjana</creatorcontrib><title>A mathematical model for the dependence of keratin aggregate formation on the quantity of mutant keratin expressed in EGFP-K14 R125P keratinocytes</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>We examined keratin aggregate formation and the possible mechanisms involved. With this aim, we observed the effect that different ratios between mutant and wild-type keratins expressed in cultured keratinocytes may have on aggregate formation in vitro, as well as how keratin aggregate formation affects the mechanical properties of cells at the cell cortex. To this end we prepared clones with expression rates as close as possible to 25%, 50% and 100% of the EGFP-K14 proteins (either WT or R125P and V270M mutants). Our results showed that only in the case of the 25% EGFP-K14 R125P mutant significant differences could be seen. Namely, we observed in this case the largest accumulation of keratin aggregates and a significant reduction in cell stiffness. To gain insight into the possible mechanisms behind this observation, we extended our previous mathematical model of keratin dynamics by implementing a more complex reaction network that considers the coexistence of wild-type and mutant keratins in the cell. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gouveia, Marcos</au><au>Sorčan, Tjaša</au><au>Zemljič-Jokhadar, Špela</au><au>Travasso, Rui D M</au><au>Liović, Mirjana</au><au>Xu, Jian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A mathematical model for the dependence of keratin aggregate formation on the quantity of mutant keratin expressed in EGFP-K14 R125P keratinocytes</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2021-12-28</date><risdate>2021</risdate><volume>16</volume><issue>12</issue><spage>e0261227</spage><epage>e0261227</epage><pages>e0261227-e0261227</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>We examined keratin aggregate formation and the possible mechanisms involved. With this aim, we observed the effect that different ratios between mutant and wild-type keratins expressed in cultured keratinocytes may have on aggregate formation in vitro, as well as how keratin aggregate formation affects the mechanical properties of cells at the cell cortex. To this end we prepared clones with expression rates as close as possible to 25%, 50% and 100% of the EGFP-K14 proteins (either WT or R125P and V270M mutants). Our results showed that only in the case of the 25% EGFP-K14 R125P mutant significant differences could be seen. Namely, we observed in this case the largest accumulation of keratin aggregates and a significant reduction in cell stiffness. To gain insight into the possible mechanisms behind this observation, we extended our previous mathematical model of keratin dynamics by implementing a more complex reaction network that considers the coexistence of wild-type and mutant keratins in the cell. The new model, consisting of a set of coupled, non-linear, ordinary differential equations, allowed us to draw conclusions regarding the relative amounts of intermediate filaments and aggregates in cells, and suggested that aggregate formation by asymmetric binding between wild-type and mutant keratins could explain the data obtained on cells grown in culture.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>34962936</pmid><doi>10.1371/journal.pone.0261227</doi><tpages>e0261227</tpages><orcidid>https://orcid.org/0000-0001-6078-0721</orcidid><orcidid>https://orcid.org/0000-0002-2552-9993</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Aggregates Analysis Biology and Life Sciences Cell culture Cell Line Cloning Computer Simulation Differential equations Filaments Fluorescent Dyes - chemistry Green Fluorescent Proteins - metabolism Humans Intermediate filaments Keratin Keratinocytes Keratinocytes - drug effects Keratinocytes - metabolism Keratins - chemistry Mathematical analysis Mathematical models Mechanical properties Medicine and Health Sciences Models, Biological Mutant Proteins - chemistry Mutants Mutation Ordinary differential equations Physical Sciences Physics Properties Proteasome Inhibitors - pharmacology Protein Aggregates - drug effects Proteins Research and Analysis Methods Stiffness |
| title | A mathematical model for the dependence of keratin aggregate formation on the quantity of mutant keratin expressed in EGFP-K14 R125P keratinocytes |
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