Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1
Profilaggrin is a large epidermal polyprotein that is proteolytically processed during keratinocyte differentiation to release multiple filaggrin monomer, units as well as a calcium-binding regulatory NH2-terminal filaggrin S-100 protein. We show that epidermal deficiency of the transmembrane serine...
Gespeichert in:
| Veröffentlicht in: | The Journal of cell biology 2003-11, Vol.163 (4), p.901-910 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 910 |
|---|---|
| container_issue | 4 |
| container_start_page | 901 |
| container_title | The Journal of cell biology |
| container_volume | 163 |
| creator | List, Karin Szabo, Roman Wertz, Philip W. Segre, Julie Haudenschild, Christian C. Kim, Soo-Youl Bugge, Thomas H. |
| description | Profilaggrin is a large epidermal polyprotein that is proteolytically processed during keratinocyte differentiation to release multiple filaggrin monomer, units as well as a calcium-binding regulatory NH2-terminal filaggrin S-100 protein. We show that epidermal deficiency of the transmembrane serine protease Matriptase/MT-SP1 perturbs lipid matrix formation, cornified envelope morphogenesis, and stratum corneum desquamation. Surprisingly, proteomic analysis of Matriptase/MT-SP1-deficient epidermis revealed the selective loss of both proteolytically processed filaggrin monomer units and the NH2-terminal filaggrin S-100 regulatory protein. This was associated with a profound accumulation of profilaggrin and aberrant profilaggrin-processing products in the stratum corneum. The data identify keratinocyte Matriptase/MT-SP1 as an essential component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation. |
| doi_str_mv | 10.1083/jcb.200304161 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2173680</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1621880</jstor_id><sourcerecordid>1621880</sourcerecordid><originalsourceid>FETCH-LOGICAL-c528t-a6ddc8c264d0eb40eac28f5bdf0d2c149054f822a5f7eff5043eeccb83e59c703</originalsourceid><addsrcrecordid>eNqFkc2LFDEQxYMo7rh69CbSePDWu5Wv7sxFkHFXhVlccD1KSKcrY4ZMZ0y6hfnvTTPDrnrxFJL68VLvPUJeUrigoPjl1nYXDICDoA19RBZUCqgVFfCYLAAYrZeSyTPyLOctAIhW8KfkjIqGK9WIBfm-jjlX0VW3KY4Yw2H01oRwmO8Wc8a-uvbBbDbJD9XKTPNDd6iu9r7HtDOh-oABRx-HWePGjMnvR5Px8uau_npLn5MnzoSML07nOfl2fXW3-lSvv3z8vHq_rq1kaqxN0_dWWdaIHrATgMYy5WTXO-iZpWIJUjjFmJGuReckCI5obac4yqVtgZ-Td0fd_dTtsLc4jMkEvU9-Z9JBR-P135PB_9Cb-Esz2vJGzQJvTwIp_pwwj3rns8UQzIBxyrotgUKJ9r8gXTIuqWwL-OYfcBunNJQU5k-hWOKqQPURsqnUkNDdr0xBz_XqUq--r7fwr__0-UCf-izAqyOwzWNMD_OGUVVs_gYg2aru</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217090538</pqid></control><display><type>article</type><title>Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><source>EZB Electronic Journals Library</source><creator>List, Karin ; Szabo, Roman ; Wertz, Philip W. ; Segre, Julie ; Haudenschild, Christian C. ; Kim, Soo-Youl ; Bugge, Thomas H.</creator><creatorcontrib>List, Karin ; Szabo, Roman ; Wertz, Philip W. ; Segre, Julie ; Haudenschild, Christian C. ; Kim, Soo-Youl ; Bugge, Thomas H.</creatorcontrib><description>Profilaggrin is a large epidermal polyprotein that is proteolytically processed during keratinocyte differentiation to release multiple filaggrin monomer, units as well as a calcium-binding regulatory NH2-terminal filaggrin S-100 protein. We show that epidermal deficiency of the transmembrane serine protease Matriptase/MT-SP1 perturbs lipid matrix formation, cornified envelope morphogenesis, and stratum corneum desquamation. Surprisingly, proteomic analysis of Matriptase/MT-SP1-deficient epidermis revealed the selective loss of both proteolytically processed filaggrin monomer units and the NH2-terminal filaggrin S-100 regulatory protein. This was associated with a profound accumulation of profilaggrin and aberrant profilaggrin-processing products in the stratum corneum. The data identify keratinocyte Matriptase/MT-SP1 as an essential component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200304161</identifier><identifier>PMID: 14638864</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Animals ; Antibodies ; Cell Differentiation - genetics ; Cellular biology ; Dehydration - enzymology ; Epidermis ; Epidermis - enzymology ; Epidermis - growth & development ; Epidermis - pathology ; Extracellular Matrix - genetics ; Extracellular Matrix - metabolism ; Extracellular Matrix - pathology ; filaggrin ; Ichthyosis ; Ichthyosis - enzymology ; Ichthyosis - genetics ; Ichthyosis - pathology ; Intermediate Filament Proteins - biosynthesis ; Intermediate Filament Proteins - deficiency ; Intermediate Filament Proteins - metabolism ; Keratinocytes ; Keratinocytes - enzymology ; Keratinocytes - pathology ; Keratinocytes - ultrastructure ; Lipid Metabolism ; Lipids ; Matriptase ; Membrane Proteins ; Mice ; Mice, Knockout ; Microscopy, Electron ; Monomers ; MT-SP1 protein ; Newborns ; Peptide Hydrolases - deficiency ; Peptide Hydrolases - genetics ; Permeability ; Protein Precursors - metabolism ; Proteins ; S100 Proteins - metabolism ; Serine Endopeptidases - deficiency ; Serine Endopeptidases - genetics ; Skin ; Skin Abnormalities - enzymology ; Skin Abnormalities - genetics ; Skin Abnormalities - pathology ; Skin diseases ; Trypsin - deficiency ; Trypsin - genetics</subject><ispartof>The Journal of cell biology, 2003-11, Vol.163 (4), p.901-910</ispartof><rights>Copyright 2003 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Nov 24, 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-a6ddc8c264d0eb40eac28f5bdf0d2c149054f822a5f7eff5043eeccb83e59c703</citedby><cites>FETCH-LOGICAL-c528t-a6ddc8c264d0eb40eac28f5bdf0d2c149054f822a5f7eff5043eeccb83e59c703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14638864$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>List, Karin</creatorcontrib><creatorcontrib>Szabo, Roman</creatorcontrib><creatorcontrib>Wertz, Philip W.</creatorcontrib><creatorcontrib>Segre, Julie</creatorcontrib><creatorcontrib>Haudenschild, Christian C.</creatorcontrib><creatorcontrib>Kim, Soo-Youl</creatorcontrib><creatorcontrib>Bugge, Thomas H.</creatorcontrib><title>Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Profilaggrin is a large epidermal polyprotein that is proteolytically processed during keratinocyte differentiation to release multiple filaggrin monomer, units as well as a calcium-binding regulatory NH2-terminal filaggrin S-100 protein. We show that epidermal deficiency of the transmembrane serine protease Matriptase/MT-SP1 perturbs lipid matrix formation, cornified envelope morphogenesis, and stratum corneum desquamation. Surprisingly, proteomic analysis of Matriptase/MT-SP1-deficient epidermis revealed the selective loss of both proteolytically processed filaggrin monomer units and the NH2-terminal filaggrin S-100 regulatory protein. This was associated with a profound accumulation of profilaggrin and aberrant profilaggrin-processing products in the stratum corneum. The data identify keratinocyte Matriptase/MT-SP1 as an essential component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Cell Differentiation - genetics</subject><subject>Cellular biology</subject><subject>Dehydration - enzymology</subject><subject>Epidermis</subject><subject>Epidermis - enzymology</subject><subject>Epidermis - growth & development</subject><subject>Epidermis - pathology</subject><subject>Extracellular Matrix - genetics</subject><subject>Extracellular Matrix - metabolism</subject><subject>Extracellular Matrix - pathology</subject><subject>filaggrin</subject><subject>Ichthyosis</subject><subject>Ichthyosis - enzymology</subject><subject>Ichthyosis - genetics</subject><subject>Ichthyosis - pathology</subject><subject>Intermediate Filament Proteins - biosynthesis</subject><subject>Intermediate Filament Proteins - deficiency</subject><subject>Intermediate Filament Proteins - metabolism</subject><subject>Keratinocytes</subject><subject>Keratinocytes - enzymology</subject><subject>Keratinocytes - pathology</subject><subject>Keratinocytes - ultrastructure</subject><subject>Lipid Metabolism</subject><subject>Lipids</subject><subject>Matriptase</subject><subject>Membrane Proteins</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Microscopy, Electron</subject><subject>Monomers</subject><subject>MT-SP1 protein</subject><subject>Newborns</subject><subject>Peptide Hydrolases - deficiency</subject><subject>Peptide Hydrolases - genetics</subject><subject>Permeability</subject><subject>Protein Precursors - metabolism</subject><subject>Proteins</subject><subject>S100 Proteins - metabolism</subject><subject>Serine Endopeptidases - deficiency</subject><subject>Serine Endopeptidases - genetics</subject><subject>Skin</subject><subject>Skin Abnormalities - enzymology</subject><subject>Skin Abnormalities - genetics</subject><subject>Skin Abnormalities - pathology</subject><subject>Skin diseases</subject><subject>Trypsin - deficiency</subject><subject>Trypsin - genetics</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2LFDEQxYMo7rh69CbSePDWu5Wv7sxFkHFXhVlccD1KSKcrY4ZMZ0y6hfnvTTPDrnrxFJL68VLvPUJeUrigoPjl1nYXDICDoA19RBZUCqgVFfCYLAAYrZeSyTPyLOctAIhW8KfkjIqGK9WIBfm-jjlX0VW3KY4Yw2H01oRwmO8Wc8a-uvbBbDbJD9XKTPNDd6iu9r7HtDOh-oABRx-HWePGjMnvR5Px8uau_npLn5MnzoSML07nOfl2fXW3-lSvv3z8vHq_rq1kaqxN0_dWWdaIHrATgMYy5WTXO-iZpWIJUjjFmJGuReckCI5obac4yqVtgZ-Td0fd_dTtsLc4jMkEvU9-Z9JBR-P135PB_9Cb-Esz2vJGzQJvTwIp_pwwj3rns8UQzIBxyrotgUKJ9r8gXTIuqWwL-OYfcBunNJQU5k-hWOKqQPURsqnUkNDdr0xBz_XqUq--r7fwr__0-UCf-izAqyOwzWNMD_OGUVVs_gYg2aru</recordid><startdate>20031124</startdate><enddate>20031124</enddate><creator>List, Karin</creator><creator>Szabo, Roman</creator><creator>Wertz, Philip W.</creator><creator>Segre, Julie</creator><creator>Haudenschild, Christian C.</creator><creator>Kim, Soo-Youl</creator><creator>Bugge, Thomas H.</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20031124</creationdate><title>Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1</title><author>List, Karin ; Szabo, Roman ; Wertz, Philip W. ; Segre, Julie ; Haudenschild, Christian C. ; Kim, Soo-Youl ; Bugge, Thomas H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-a6ddc8c264d0eb40eac28f5bdf0d2c149054f822a5f7eff5043eeccb83e59c703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Cell Differentiation - genetics</topic><topic>Cellular biology</topic><topic>Dehydration - enzymology</topic><topic>Epidermis</topic><topic>Epidermis - enzymology</topic><topic>Epidermis - growth & development</topic><topic>Epidermis - pathology</topic><topic>Extracellular Matrix - genetics</topic><topic>Extracellular Matrix - metabolism</topic><topic>Extracellular Matrix - pathology</topic><topic>filaggrin</topic><topic>Ichthyosis</topic><topic>Ichthyosis - enzymology</topic><topic>Ichthyosis - genetics</topic><topic>Ichthyosis - pathology</topic><topic>Intermediate Filament Proteins - biosynthesis</topic><topic>Intermediate Filament Proteins - deficiency</topic><topic>Intermediate Filament Proteins - metabolism</topic><topic>Keratinocytes</topic><topic>Keratinocytes - enzymology</topic><topic>Keratinocytes - pathology</topic><topic>Keratinocytes - ultrastructure</topic><topic>Lipid Metabolism</topic><topic>Lipids</topic><topic>Matriptase</topic><topic>Membrane Proteins</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Microscopy, Electron</topic><topic>Monomers</topic><topic>MT-SP1 protein</topic><topic>Newborns</topic><topic>Peptide Hydrolases - deficiency</topic><topic>Peptide Hydrolases - genetics</topic><topic>Permeability</topic><topic>Protein Precursors - metabolism</topic><topic>Proteins</topic><topic>S100 Proteins - metabolism</topic><topic>Serine Endopeptidases - deficiency</topic><topic>Serine Endopeptidases - genetics</topic><topic>Skin</topic><topic>Skin Abnormalities - enzymology</topic><topic>Skin Abnormalities - genetics</topic><topic>Skin Abnormalities - pathology</topic><topic>Skin diseases</topic><topic>Trypsin - deficiency</topic><topic>Trypsin - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>List, Karin</creatorcontrib><creatorcontrib>Szabo, Roman</creatorcontrib><creatorcontrib>Wertz, Philip W.</creatorcontrib><creatorcontrib>Segre, Julie</creatorcontrib><creatorcontrib>Haudenschild, Christian C.</creatorcontrib><creatorcontrib>Kim, Soo-Youl</creatorcontrib><creatorcontrib>Bugge, Thomas H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>List, Karin</au><au>Szabo, Roman</au><au>Wertz, Philip W.</au><au>Segre, Julie</au><au>Haudenschild, Christian C.</au><au>Kim, Soo-Youl</au><au>Bugge, Thomas H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2003-11-24</date><risdate>2003</risdate><volume>163</volume><issue>4</issue><spage>901</spage><epage>910</epage><pages>901-910</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Profilaggrin is a large epidermal polyprotein that is proteolytically processed during keratinocyte differentiation to release multiple filaggrin monomer, units as well as a calcium-binding regulatory NH2-terminal filaggrin S-100 protein. We show that epidermal deficiency of the transmembrane serine protease Matriptase/MT-SP1 perturbs lipid matrix formation, cornified envelope morphogenesis, and stratum corneum desquamation. Surprisingly, proteomic analysis of Matriptase/MT-SP1-deficient epidermis revealed the selective loss of both proteolytically processed filaggrin monomer units and the NH2-terminal filaggrin S-100 regulatory protein. This was associated with a profound accumulation of profilaggrin and aberrant profilaggrin-processing products in the stratum corneum. The data identify keratinocyte Matriptase/MT-SP1 as an essential component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>14638864</pmid><doi>10.1083/jcb.200304161</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9525 |
| ispartof | The Journal of cell biology, 2003-11, Vol.163 (4), p.901-910 |
| issn | 0021-9525 1540-8140 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2173680 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Animals Antibodies Cell Differentiation - genetics Cellular biology Dehydration - enzymology Epidermis Epidermis - enzymology Epidermis - growth & development Epidermis - pathology Extracellular Matrix - genetics Extracellular Matrix - metabolism Extracellular Matrix - pathology filaggrin Ichthyosis Ichthyosis - enzymology Ichthyosis - genetics Ichthyosis - pathology Intermediate Filament Proteins - biosynthesis Intermediate Filament Proteins - deficiency Intermediate Filament Proteins - metabolism Keratinocytes Keratinocytes - enzymology Keratinocytes - pathology Keratinocytes - ultrastructure Lipid Metabolism Lipids Matriptase Membrane Proteins Mice Mice, Knockout Microscopy, Electron Monomers MT-SP1 protein Newborns Peptide Hydrolases - deficiency Peptide Hydrolases - genetics Permeability Protein Precursors - metabolism Proteins S100 Proteins - metabolism Serine Endopeptidases - deficiency Serine Endopeptidases - genetics Skin Skin Abnormalities - enzymology Skin Abnormalities - genetics Skin Abnormalities - pathology Skin diseases Trypsin - deficiency Trypsin - genetics |
| title | Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T15%3A02%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Loss%20of%20Proteolytically%20Processed%20Filaggrin%20Caused%20by%20Epidermal%20Deletion%20of%20Matriptase/MT-SP1&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=List,%20Karin&rft.date=2003-11-24&rft.volume=163&rft.issue=4&rft.spage=901&rft.epage=910&rft.pages=901-910&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.200304161&rft_dat=%3Cjstor_pubme%3E1621880%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217090538&rft_id=info:pmid/14638864&rft_jstor_id=1621880&rfr_iscdi=true |