Fibroin and sericin from Bombyx mori silk stimulate cell migration through upregulation and phosphorylation of c-Jun
Wound healing is a biological process directed to the restoration of tissue that has suffered an injury. An important phase of wound healing is the generation of a basal epithelium able to wholly replace the epidermis of the wound. A broad range of products derived from fibroin and sericin from Bomb...
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| description | Wound healing is a biological process directed to the restoration of tissue that has suffered an injury. An important phase of wound healing is the generation of a basal epithelium able to wholly replace the epidermis of the wound. A broad range of products derived from fibroin and sericin from Bombyx mori silk are used to stimulate wound healing. However, so far the molecular mechanism underlying this phenomenon has not been elucidated. The aim of this work was to determine the molecular basis underlying wound healing properties of silk proteins using a cell model. For this purpose, we assayed fibroin and sericin in a wound healing scratch assay using MDA-MB-231 and Mv1Lu cells. Both proteins stimulated cell migration. Furthermore, treatment with sericin and fibroin involved key factors of the wound healing process such as upregulation of c-Jun and c-Jun protein phosphorylation. Moreover, fibroin and sericin stimulated the phosphorylation of ERK 1/2 and JNK 1/2 kinases. All these experiments were done in the presence of specific inhibitors for some of the cell signalling pathways referred above. The obtained results revealed that MEK, JNK and PI3K pathways are involved in fibroin and sericin stimulated cells migration. Inhibition of these three kinases prevented c-Jun upregulation and phosphorylation by fibroin or sericin. Fibroin and sericin were tested in the human keratinocyte cell line, HaCaT, with similar results. Altogether, our results showed that fibroin and sericin initiate cell migration by activating the MEK, JNK and PI3K signalling pathways ending in c-Jun activation. |
| doi_str_mv | 10.1371/journal.pone.0042271 |
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An important phase of wound healing is the generation of a basal epithelium able to wholly replace the epidermis of the wound. A broad range of products derived from fibroin and sericin from Bombyx mori silk are used to stimulate wound healing. However, so far the molecular mechanism underlying this phenomenon has not been elucidated. The aim of this work was to determine the molecular basis underlying wound healing properties of silk proteins using a cell model. For this purpose, we assayed fibroin and sericin in a wound healing scratch assay using MDA-MB-231 and Mv1Lu cells. Both proteins stimulated cell migration. Furthermore, treatment with sericin and fibroin involved key factors of the wound healing process such as upregulation of c-Jun and c-Jun protein phosphorylation. Moreover, fibroin and sericin stimulated the phosphorylation of ERK 1/2 and JNK 1/2 kinases. All these experiments were done in the presence of specific inhibitors for some of the cell signalling pathways referred above. The obtained results revealed that MEK, JNK and PI3K pathways are involved in fibroin and sericin stimulated cells migration. Inhibition of these three kinases prevented c-Jun upregulation and phosphorylation by fibroin or sericin. Fibroin and sericin were tested in the human keratinocyte cell line, HaCaT, with similar results. 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This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://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. 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An important phase of wound healing is the generation of a basal epithelium able to wholly replace the epidermis of the wound. A broad range of products derived from fibroin and sericin from Bombyx mori silk are used to stimulate wound healing. However, so far the molecular mechanism underlying this phenomenon has not been elucidated. The aim of this work was to determine the molecular basis underlying wound healing properties of silk proteins using a cell model. For this purpose, we assayed fibroin and sericin in a wound healing scratch assay using MDA-MB-231 and Mv1Lu cells. Both proteins stimulated cell migration. Furthermore, treatment with sericin and fibroin involved key factors of the wound healing process such as upregulation of c-Jun and c-Jun protein phosphorylation. Moreover, fibroin and sericin stimulated the phosphorylation of ERK 1/2 and JNK 1/2 kinases. All these experiments were done in the presence of specific inhibitors for some of the cell signalling pathways referred above. The obtained results revealed that MEK, JNK and PI3K pathways are involved in fibroin and sericin stimulated cells migration. Inhibition of these three kinases prevented c-Jun upregulation and phosphorylation by fibroin or sericin. Fibroin and sericin were tested in the human keratinocyte cell line, HaCaT, with similar results. Altogether, our results showed that fibroin and sericin initiate cell migration by activating the MEK, JNK and PI3K signalling pathways ending in c-Jun activation.</description><subject>1-Phosphatidylinositol 3-kinase</subject><subject>Animals</subject><subject>Biological activity</subject><subject>Biology</subject><subject>Biomedical materials</subject><subject>Bombyx</subject><subject>Bombyx mori</subject><subject>c-Jun protein</subject><subject>Cell adhesion & migration</subject><subject>Cell Line</subject><subject>Cell migration</subject><subject>Cell Movement - physiology</subject><subject>Cellular signal transduction</subject><subject>Epidermis</subject><subject>Epithelium</subject><subject>Extracellular signal-regulated kinase</subject><subject>Fibroblasts</subject><subject>Fibroins - physiology</subject><subject>Gene expression</subject><subject>Growth factors</subject><subject>Humans</subject><subject>Jun protein</subject><subject>Kinases</subject><subject>Phosphorylation</subject><subject>Protein Kinase Inhibitors - pharmacology</subject><subject>Protein Kinases - metabolism</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-jun - metabolism</subject><subject>Restoration</subject><subject>Sericins - physiology</subject><subject>Signal transduction</subject><subject>Signaling</subject><subject>Silk</subject><subject>Silk - chemistry</subject><subject>Textile fibers</subject><subject>Transcription factors</subject><subject>Up-regulation</subject><subject>Up-Regulation - physiology</subject><subject>Wound care</subject><subject>Wound healing</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk12L1DAUhoso7rr6D0QDgujFjPlo2uRGWBdXRxYW_LoNaZq0WdtmNkll59-bOt1lKnshJTScPOdN8uacLHuO4BqREr27cqMfZLfeukGvIcwxLtGD7BhxglcFhuThwfwoexLCFYSUsKJ4nB1hzAqIIDnO4rmtvLMDkEMNgvZWpbnxrgcfXF_tbkDvvAXBdr9AiLYfOxk1ULrrQG8bL6N1A4itd2PTgnHrdTMRU3DS27YupOF3c8wZoFZfxuFp9sjILuhn8_8k-3H-8fvZ59XF5afN2enFSpWUxVUla5NOiU1pVEGJUoRIrmnOCWTKEG4IKaCiiFUI5ZSTSrGallhCRShTSJKT7OVed9u5IGbDgkAEU4oZZCgRmz1RO3kltt720u-Ek1b8DTjfCOmjVZ0WFSWwqllZkKLOK6wrnrzkulIQSZPzOmm9n3cbq17XSg_Ry24hulwZbCsa91uQHHJU0iTwZhbw7nrUIYrehslrOWg3pnNDghBlvGAJffUPev_tZqqR6QJ2MC7tqyZRcZpzhvNURzhR63uo9NW6typVl7Epvkh4u0hITNQ3sZFjCGLz7ev_s5c_l-zrA7bVsottcN041U5YgvkeVN6F4LW5MxlBMTXHrRtiag4xN0dKe3H4QHdJt91A_gAlmgrc</recordid><startdate>20120731</startdate><enddate>20120731</enddate><creator>Martínez-Mora, Celia</creator><creator>Mrowiec, Anna</creator><creator>García-Vizcaíno, Eva María</creator><creator>Alcaraz, Antonia</creator><creator>Cenis, José Luis</creator><creator>Nicolás, Francisco José</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>AEUYN</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>20120731</creationdate><title>Fibroin and sericin from Bombyx mori silk stimulate cell migration through upregulation and phosphorylation of c-Jun</title><author>Martínez-Mora, Celia ; Mrowiec, Anna ; García-Vizcaíno, Eva María ; Alcaraz, Antonia ; Cenis, José Luis ; Nicolás, Francisco José</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-badf0102f7fc653cc33a9e549308cf39f3360c518b114593bc8d572a0c358c1a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>1-Phosphatidylinositol 3-kinase</topic><topic>Animals</topic><topic>Biological activity</topic><topic>Biology</topic><topic>Biomedical materials</topic><topic>Bombyx</topic><topic>Bombyx mori</topic><topic>c-Jun protein</topic><topic>Cell adhesion & migration</topic><topic>Cell Line</topic><topic>Cell migration</topic><topic>Cell Movement - 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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>Martínez-Mora, Celia</au><au>Mrowiec, Anna</au><au>García-Vizcaíno, Eva María</au><au>Alcaraz, Antonia</au><au>Cenis, José Luis</au><au>Nicolás, Francisco José</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fibroin and sericin from Bombyx mori silk stimulate cell migration through upregulation and phosphorylation of c-Jun</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2012-07-31</date><risdate>2012</risdate><volume>7</volume><issue>7</issue><spage>e42271</spage><epage>e42271</epage><pages>e42271-e42271</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Wound healing is a biological process directed to the restoration of tissue that has suffered an injury. An important phase of wound healing is the generation of a basal epithelium able to wholly replace the epidermis of the wound. A broad range of products derived from fibroin and sericin from Bombyx mori silk are used to stimulate wound healing. However, so far the molecular mechanism underlying this phenomenon has not been elucidated. The aim of this work was to determine the molecular basis underlying wound healing properties of silk proteins using a cell model. For this purpose, we assayed fibroin and sericin in a wound healing scratch assay using MDA-MB-231 and Mv1Lu cells. Both proteins stimulated cell migration. Furthermore, treatment with sericin and fibroin involved key factors of the wound healing process such as upregulation of c-Jun and c-Jun protein phosphorylation. Moreover, fibroin and sericin stimulated the phosphorylation of ERK 1/2 and JNK 1/2 kinases. All these experiments were done in the presence of specific inhibitors for some of the cell signalling pathways referred above. The obtained results revealed that MEK, JNK and PI3K pathways are involved in fibroin and sericin stimulated cells migration. Inhibition of these three kinases prevented c-Jun upregulation and phosphorylation by fibroin or sericin. Fibroin and sericin were tested in the human keratinocyte cell line, HaCaT, with similar results. Altogether, our results showed that fibroin and sericin initiate cell migration by activating the MEK, JNK and PI3K signalling pathways ending in c-Jun activation.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22860103</pmid><doi>10.1371/journal.pone.0042271</doi><tpages>e42271</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 1-Phosphatidylinositol 3-kinase Animals Biological activity Biology Biomedical materials Bombyx Bombyx mori c-Jun protein Cell adhesion & migration Cell Line Cell migration Cell Movement - physiology Cellular signal transduction Epidermis Epithelium Extracellular signal-regulated kinase Fibroblasts Fibroins - physiology Gene expression Growth factors Humans Jun protein Kinases Phosphorylation Protein Kinase Inhibitors - pharmacology Protein Kinases - metabolism Proteins Proto-Oncogene Proteins c-jun - metabolism Restoration Sericins - physiology Signal transduction Signaling Silk Silk - chemistry Textile fibers Transcription factors Up-regulation Up-Regulation - physiology Wound care Wound healing |
| title | Fibroin and sericin from Bombyx mori silk stimulate cell migration through upregulation and phosphorylation of c-Jun |
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