Highly Complex Peptide Aggregates of the S100 Fused-Type Protein Hornerin Are Present in Human Skin
Human hornerin (HRNR) is a 245kDa S100 fused-type protein which contains 95% tandem quasi-repeating glycine- and serine-rich domains. Previously HRNR was not thought to be expressed in healthy skin; however, we purified an HRNR peptide fragment from stratum corneum. Moreover, we found that HRNR mRNA...
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| Veröffentlicht in: | Journal of investigative dermatology 2009-06, Vol.129 (6), p.1446-1458 |
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| creator | Wu, Zhihong Meyer-Hoffert, Ulf Reithmayer, Katrin Paus, Ralf Hansmann, Britta He, Yinghong Bartels, Joachim Gläser, Regine Harder, Jürgen Schröder, Jens-Michael |
| description | Human hornerin (HRNR) is a 245kDa S100 fused-type protein which contains 95% tandem quasi-repeating glycine- and serine-rich domains. Previously HRNR was not thought to be expressed in healthy skin; however, we purified an HRNR peptide fragment from stratum corneum. Moreover, we found that HRNR mRNA is expressed in skin biopsies from different sites as head, trunk, legs, hands, and feet. In cultured human epidermal keratinocytes, HRNR mRNA expression was transiently induced during Ca2+-dependent differentiation. Immunostaining using distinct antibodies generated against four putative HRNR domains revealed strong HRNR immunoreactivity in healthy epidermis as well as in the entire outer root sheath of normal human scalp hair follicles. In lesions from psoriasis and atopic dermatitis patients, HRNR immunoreactivity was reduced compared with uninvolved skin of these patients. Electrospray ionization mass spectrometry and Western blot analyses revealed that HRNR is a highly degradable protein that forms complex high molecular weight peptide aggregates. Our findings suggest that HRNR is expressed in healthy skin and give insight into the complex biology of this protein. HRNR and its degradation products might contribute to the barrier function of healthy human skin. |
| doi_str_mv | 10.1038/jid.2008.370 |
| format | Article |
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Previously HRNR was not thought to be expressed in healthy skin; however, we purified an HRNR peptide fragment from stratum corneum. Moreover, we found that HRNR mRNA is expressed in skin biopsies from different sites as head, trunk, legs, hands, and feet. In cultured human epidermal keratinocytes, HRNR mRNA expression was transiently induced during Ca2+-dependent differentiation. Immunostaining using distinct antibodies generated against four putative HRNR domains revealed strong HRNR immunoreactivity in healthy epidermis as well as in the entire outer root sheath of normal human scalp hair follicles. In lesions from psoriasis and atopic dermatitis patients, HRNR immunoreactivity was reduced compared with uninvolved skin of these patients. Electrospray ionization mass spectrometry and Western blot analyses revealed that HRNR is a highly degradable protein that forms complex high molecular weight peptide aggregates. Our findings suggest that HRNR is expressed in healthy skin and give insight into the complex biology of this protein. HRNR and its degradation products might contribute to the barrier function of healthy human skin.</description><identifier>ISSN: 0022-202X</identifier><identifier>EISSN: 1523-1747</identifier><identifier>DOI: 10.1038/jid.2008.370</identifier><identifier>PMID: 19020553</identifier><identifier>CODEN: JIDEAE</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Biological and medical sciences ; Calcium-Binding Proteins - biosynthesis ; Calcium-Binding Proteins - physiology ; Cell Differentiation ; Cells, Cultured ; Dermatitis, Atopic - metabolism ; Dermatology ; Epidermis - metabolism ; Gene Expression Regulation ; Humans ; Intermediate Filament Proteins - biosynthesis ; Intermediate Filament Proteins - physiology ; Medical sciences ; Models, Biological ; Molecular Sequence Data ; Psoriasis - metabolism ; S100 Proteins - metabolism ; Sequence Homology, Amino Acid ; Skin - metabolism ; Spectrometry, Mass, Electrospray Ionization</subject><ispartof>Journal of investigative dermatology, 2009-06, Vol.129 (6), p.1446-1458</ispartof><rights>2009 The Society for Investigative Dermatology, Inc</rights><rights>2009 INIST-CNRS</rights><rights>Copyright Nature Publishing Group Jun 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-75e7511b28f34fa14eb3d14d015255ff70d7dcb7db9e7d10a297b339490529703</citedby><cites>FETCH-LOGICAL-c522t-75e7511b28f34fa14eb3d14d015255ff70d7dcb7db9e7d10a297b339490529703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/210350962?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,64385,64387,64389,72469</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21487554$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19020553$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, Zhihong</creatorcontrib><creatorcontrib>Meyer-Hoffert, Ulf</creatorcontrib><creatorcontrib>Reithmayer, Katrin</creatorcontrib><creatorcontrib>Paus, Ralf</creatorcontrib><creatorcontrib>Hansmann, Britta</creatorcontrib><creatorcontrib>He, Yinghong</creatorcontrib><creatorcontrib>Bartels, Joachim</creatorcontrib><creatorcontrib>Gläser, Regine</creatorcontrib><creatorcontrib>Harder, Jürgen</creatorcontrib><creatorcontrib>Schröder, Jens-Michael</creatorcontrib><title>Highly Complex Peptide Aggregates of the S100 Fused-Type Protein Hornerin Are Present in Human Skin</title><title>Journal of investigative dermatology</title><addtitle>J Invest Dermatol</addtitle><description>Human hornerin (HRNR) is a 245kDa S100 fused-type protein which contains 95% tandem quasi-repeating glycine- and serine-rich domains. Previously HRNR was not thought to be expressed in healthy skin; however, we purified an HRNR peptide fragment from stratum corneum. Moreover, we found that HRNR mRNA is expressed in skin biopsies from different sites as head, trunk, legs, hands, and feet. In cultured human epidermal keratinocytes, HRNR mRNA expression was transiently induced during Ca2+-dependent differentiation. Immunostaining using distinct antibodies generated against four putative HRNR domains revealed strong HRNR immunoreactivity in healthy epidermis as well as in the entire outer root sheath of normal human scalp hair follicles. In lesions from psoriasis and atopic dermatitis patients, HRNR immunoreactivity was reduced compared with uninvolved skin of these patients. Electrospray ionization mass spectrometry and Western blot analyses revealed that HRNR is a highly degradable protein that forms complex high molecular weight peptide aggregates. Our findings suggest that HRNR is expressed in healthy skin and give insight into the complex biology of this protein. HRNR and its degradation products might contribute to the barrier function of healthy human skin.</description><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Calcium-Binding Proteins - biosynthesis</subject><subject>Calcium-Binding Proteins - physiology</subject><subject>Cell Differentiation</subject><subject>Cells, Cultured</subject><subject>Dermatitis, Atopic - metabolism</subject><subject>Dermatology</subject><subject>Epidermis - metabolism</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Intermediate Filament Proteins - biosynthesis</subject><subject>Intermediate Filament Proteins - physiology</subject><subject>Medical sciences</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Psoriasis - metabolism</subject><subject>S100 Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Skin - metabolism</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><issn>0022-202X</issn><issn>1523-1747</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNptkNGL1DAQh4Mo3nr65rMEQZ_sOkmapn1cFs8VDjy4E3wLaTPdy9qma9KK-9-bXpcTxKcZho_5zXyEvGawZiDKjwdn1xygXAsFT8iKSS4ypnL1lKwAOM848O8X5EWMBwBW5LJ8Ti5YBRykFCvS7Nz-vjvR7dAfO_xNb_A4Oot0s98H3JsRIx1aOt4jvWUA9GqKaLO70xHpTRhGdJ7uhuAxpGYT5iFG9COd51NvPL394fxL8qw1XcRX53pJvl19utvusuuvn79sN9dZIzkfMyVRScZqXrYibw3LsRaW5RbSS1K2rQKrbFMrW1eoLAPDK1ULUeUVyNSCuCTvl73HMPycMI66d7HBrjMehynqQnFeFgVP4Nt_wMMwBZ9u0zw5lVA9QB8WqAlDjAFbfQyuN-GkGejZvE7m9Wxei4fwN-edU92j_QufVSfg3RkwsTFdG4xvXHzkOMtLJWWeOLpw3oxTwEcgpc1hS1axIJhs_nIYdGwc-gatC9iM2g7u_0f-AQ4cpk4</recordid><startdate>20090601</startdate><enddate>20090601</enddate><creator>Wu, Zhihong</creator><creator>Meyer-Hoffert, Ulf</creator><creator>Reithmayer, Katrin</creator><creator>Paus, Ralf</creator><creator>Hansmann, Britta</creator><creator>He, Yinghong</creator><creator>Bartels, Joachim</creator><creator>Gläser, Regine</creator><creator>Harder, Jürgen</creator><creator>Schröder, Jens-Michael</creator><general>Elsevier Inc</general><general>Nature Publishing Group</general><general>Elsevier Limited</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><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>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20090601</creationdate><title>Highly Complex Peptide Aggregates of the S100 Fused-Type Protein Hornerin Are Present in Human Skin</title><author>Wu, Zhihong ; Meyer-Hoffert, Ulf ; Reithmayer, Katrin ; Paus, Ralf ; Hansmann, Britta ; He, Yinghong ; Bartels, Joachim ; Gläser, Regine ; Harder, Jürgen ; Schröder, Jens-Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-75e7511b28f34fa14eb3d14d015255ff70d7dcb7db9e7d10a297b339490529703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Calcium-Binding Proteins - biosynthesis</topic><topic>Calcium-Binding Proteins - physiology</topic><topic>Cell Differentiation</topic><topic>Cells, Cultured</topic><topic>Dermatitis, Atopic - metabolism</topic><topic>Dermatology</topic><topic>Epidermis - metabolism</topic><topic>Gene Expression Regulation</topic><topic>Humans</topic><topic>Intermediate Filament Proteins - biosynthesis</topic><topic>Intermediate Filament Proteins - physiology</topic><topic>Medical sciences</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>Psoriasis - metabolism</topic><topic>S100 Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Skin - metabolism</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Zhihong</creatorcontrib><creatorcontrib>Meyer-Hoffert, Ulf</creatorcontrib><creatorcontrib>Reithmayer, Katrin</creatorcontrib><creatorcontrib>Paus, Ralf</creatorcontrib><creatorcontrib>Hansmann, Britta</creatorcontrib><creatorcontrib>He, Yinghong</creatorcontrib><creatorcontrib>Bartels, Joachim</creatorcontrib><creatorcontrib>Gläser, Regine</creatorcontrib><creatorcontrib>Harder, Jürgen</creatorcontrib><creatorcontrib>Schröder, Jens-Michael</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</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>Technology Research Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of investigative dermatology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Zhihong</au><au>Meyer-Hoffert, Ulf</au><au>Reithmayer, Katrin</au><au>Paus, Ralf</au><au>Hansmann, Britta</au><au>He, Yinghong</au><au>Bartels, Joachim</au><au>Gläser, Regine</au><au>Harder, Jürgen</au><au>Schröder, Jens-Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Highly Complex Peptide Aggregates of the S100 Fused-Type Protein Hornerin Are Present in Human Skin</atitle><jtitle>Journal of investigative dermatology</jtitle><addtitle>J Invest Dermatol</addtitle><date>2009-06-01</date><risdate>2009</risdate><volume>129</volume><issue>6</issue><spage>1446</spage><epage>1458</epage><pages>1446-1458</pages><issn>0022-202X</issn><eissn>1523-1747</eissn><coden>JIDEAE</coden><abstract>Human hornerin (HRNR) is a 245kDa S100 fused-type protein which contains 95% tandem quasi-repeating glycine- and serine-rich domains. Previously HRNR was not thought to be expressed in healthy skin; however, we purified an HRNR peptide fragment from stratum corneum. Moreover, we found that HRNR mRNA is expressed in skin biopsies from different sites as head, trunk, legs, hands, and feet. In cultured human epidermal keratinocytes, HRNR mRNA expression was transiently induced during Ca2+-dependent differentiation. Immunostaining using distinct antibodies generated against four putative HRNR domains revealed strong HRNR immunoreactivity in healthy epidermis as well as in the entire outer root sheath of normal human scalp hair follicles. In lesions from psoriasis and atopic dermatitis patients, HRNR immunoreactivity was reduced compared with uninvolved skin of these patients. Electrospray ionization mass spectrometry and Western blot analyses revealed that HRNR is a highly degradable protein that forms complex high molecular weight peptide aggregates. Our findings suggest that HRNR is expressed in healthy skin and give insight into the complex biology of this protein. HRNR and its degradation products might contribute to the barrier function of healthy human skin.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>19020553</pmid><doi>10.1038/jid.2008.370</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Biological and medical sciences Calcium-Binding Proteins - biosynthesis Calcium-Binding Proteins - physiology Cell Differentiation Cells, Cultured Dermatitis, Atopic - metabolism Dermatology Epidermis - metabolism Gene Expression Regulation Humans Intermediate Filament Proteins - biosynthesis Intermediate Filament Proteins - physiology Medical sciences Models, Biological Molecular Sequence Data Psoriasis - metabolism S100 Proteins - metabolism Sequence Homology, Amino Acid Skin - metabolism Spectrometry, Mass, Electrospray Ionization |
| title | Highly Complex Peptide Aggregates of the S100 Fused-Type Protein Hornerin Are Present in Human Skin |
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