HSP25 Is Involved in Two Steps of the Differentiation of PAM212 Keratinocytes
HSP25 is a member of the small heat shock protein family. This 25-kDa protein exhibits a highly specific distribution during mouse embryonic development. Although multiple functions have been proposed for HSP25, the role it plays during differentiation is still unknown. High levels of HSP25 can be d...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-03, Vol.279 (11), p.10252-10260 |
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| container_title | The Journal of biological chemistry |
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| creator | Duverger, Olivier Paslaru, Liliana Morange, Michel |
| description | HSP25 is a member of the small heat shock protein family. This 25-kDa protein exhibits a highly specific distribution during mouse embryonic development. Although multiple functions have been proposed for HSP25, the role it plays during differentiation is still unknown. High levels of HSP25 can be detected in embryonic and adult skin. During epidermis differentiation, the concentration of HSP25 increases with the distance of keratinocytes from the basal layer, in parallel with the extent of keratinization. We used an ex vivo cellular system, PAM212 cells, to analyze quantitatively and qualitatively the dynamics of HSP25 production and phosphorylation during the differentiation of keratinocytes. Our observations suggest that HSP25 is involved in two steps of PAM212 keratinocyte differentiation. Shortly after the induction of differentiation, a transient hyperphosphorylation of HSP25 seems to be essential for the expression of differentiation markers. Later, the chaperone-active form of HSP25 is organized progressively into characteristic aggregates involved in the dynamics of keratin filament networks. |
| doi_str_mv | 10.1074/jbc.M309906200 |
| format | Article |
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This 25-kDa protein exhibits a highly specific distribution during mouse embryonic development. Although multiple functions have been proposed for HSP25, the role it plays during differentiation is still unknown. High levels of HSP25 can be detected in embryonic and adult skin. During epidermis differentiation, the concentration of HSP25 increases with the distance of keratinocytes from the basal layer, in parallel with the extent of keratinization. We used an ex vivo cellular system, PAM212 cells, to analyze quantitatively and qualitatively the dynamics of HSP25 production and phosphorylation during the differentiation of keratinocytes. Our observations suggest that HSP25 is involved in two steps of PAM212 keratinocyte differentiation. Shortly after the induction of differentiation, a transient hyperphosphorylation of HSP25 seems to be essential for the expression of differentiation markers. Later, the chaperone-active form of HSP25 is organized progressively into characteristic aggregates involved in the dynamics of keratin filament networks.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M309906200</identifier><identifier>PMID: 14662766</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Blotting, Western ; Cell Differentiation ; Cell Line ; Cell Line, Transformed ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Enzyme Inhibitors - pharmacology ; Epidermis - embryology ; Heat-Shock Proteins - metabolism ; Heat-Shock Proteins - physiology ; Immunoblotting ; Immunohistochemistry ; Keratinocytes - cytology ; Keratinocytes - metabolism ; Keratins - chemistry ; Keratins - metabolism ; Mice ; Microscopy, Electron ; Microscopy, Fluorescence ; Mitogen-Activated Protein Kinases - metabolism ; Molecular Chaperones ; Neoplasm Proteins - metabolism ; Neoplasm Proteins - physiology ; p38 Mitogen-Activated Protein Kinases ; Phosphorylation ; Time Factors</subject><ispartof>The Journal of biological chemistry, 2004-03, Vol.279 (11), p.10252-10260</ispartof><rights>2004 © 2004 ASBMB. 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This 25-kDa protein exhibits a highly specific distribution during mouse embryonic development. Although multiple functions have been proposed for HSP25, the role it plays during differentiation is still unknown. High levels of HSP25 can be detected in embryonic and adult skin. During epidermis differentiation, the concentration of HSP25 increases with the distance of keratinocytes from the basal layer, in parallel with the extent of keratinization. We used an ex vivo cellular system, PAM212 cells, to analyze quantitatively and qualitatively the dynamics of HSP25 production and phosphorylation during the differentiation of keratinocytes. Our observations suggest that HSP25 is involved in two steps of PAM212 keratinocyte differentiation. Shortly after the induction of differentiation, a transient hyperphosphorylation of HSP25 seems to be essential for the expression of differentiation markers. Later, the chaperone-active form of HSP25 is organized progressively into characteristic aggregates involved in the dynamics of keratin filament networks.</description><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cell Differentiation</subject><subject>Cell Line</subject><subject>Cell Line, Transformed</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Epidermis - embryology</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Heat-Shock Proteins - physiology</subject><subject>Immunoblotting</subject><subject>Immunohistochemistry</subject><subject>Keratinocytes - cytology</subject><subject>Keratinocytes - metabolism</subject><subject>Keratins - chemistry</subject><subject>Keratins - metabolism</subject><subject>Mice</subject><subject>Microscopy, Electron</subject><subject>Microscopy, Fluorescence</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Molecular Chaperones</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Neoplasm Proteins - physiology</subject><subject>p38 Mitogen-Activated Protein Kinases</subject><subject>Phosphorylation</subject><subject>Time Factors</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1rGzEQhkVpaNyk1x6LDqW3dWe0u9LqGNKPmMYkkAR6EytptlawV660dsi_r4INOXUuA8MzLzMPYx8R5giq-fpo3XxZg9YgBcAbNkPo6qpu8fdbNgMQWGnRdqfsfc6PUKrR-I6dYiOlUFLO2PLq7la0fJH5YtzH9Z48DyO_f4r8bqJt5nHg04r4tzAMlGicQj-FOL6Mby-WAgX_RamMxuieJ8rn7GTo15k-HPsZe_jx_f7yqrq--bm4vLiuXKPaqRqs184RdN4J31CHHhrVy_KP6J31skFdW-xlbSVK10vVykFYtFJ3UtYa6jP25ZC7TfHvjvJkNiE7Wq_7keIuG4UKFEBdwPkBdCnmnGgw2xQ2fXo2COZFoCkCzavAsvDpmLyzG_Kv-NFYAT4fgFX4s3oKiYwN0a1oY4TSBrGkilYUrDtgVDTsAyWTXaDRkS8rbjI-hv-d8A_GP4g8</recordid><startdate>20040312</startdate><enddate>20040312</enddate><creator>Duverger, Olivier</creator><creator>Paslaru, Liliana</creator><creator>Morange, Michel</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>20040312</creationdate><title>HSP25 Is Involved in Two Steps of the Differentiation of PAM212 Keratinocytes</title><author>Duverger, Olivier ; Paslaru, Liliana ; Morange, Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-fbd9cce08dc2d4e81d047a60742acbd64193b1a63b616ca6756f2b1b698663903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cell Differentiation</topic><topic>Cell Line</topic><topic>Cell Line, Transformed</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Epidermis - embryology</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Heat-Shock Proteins - physiology</topic><topic>Immunoblotting</topic><topic>Immunohistochemistry</topic><topic>Keratinocytes - cytology</topic><topic>Keratinocytes - metabolism</topic><topic>Keratins - chemistry</topic><topic>Keratins - metabolism</topic><topic>Mice</topic><topic>Microscopy, Electron</topic><topic>Microscopy, Fluorescence</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Molecular Chaperones</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Neoplasm Proteins - physiology</topic><topic>p38 Mitogen-Activated Protein Kinases</topic><topic>Phosphorylation</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Duverger, Olivier</creatorcontrib><creatorcontrib>Paslaru, Liliana</creatorcontrib><creatorcontrib>Morange, Michel</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Duverger, Olivier</au><au>Paslaru, Liliana</au><au>Morange, Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HSP25 Is Involved in Two Steps of the Differentiation of PAM212 Keratinocytes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-03-12</date><risdate>2004</risdate><volume>279</volume><issue>11</issue><spage>10252</spage><epage>10260</epage><pages>10252-10260</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>HSP25 is a member of the small heat shock protein family. This 25-kDa protein exhibits a highly specific distribution during mouse embryonic development. Although multiple functions have been proposed for HSP25, the role it plays during differentiation is still unknown. High levels of HSP25 can be detected in embryonic and adult skin. During epidermis differentiation, the concentration of HSP25 increases with the distance of keratinocytes from the basal layer, in parallel with the extent of keratinization. We used an ex vivo cellular system, PAM212 cells, to analyze quantitatively and qualitatively the dynamics of HSP25 production and phosphorylation during the differentiation of keratinocytes. Our observations suggest that HSP25 is involved in two steps of PAM212 keratinocyte differentiation. Shortly after the induction of differentiation, a transient hyperphosphorylation of HSP25 seems to be essential for the expression of differentiation markers. 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Blotting, Western Cell Differentiation Cell Line Cell Line, Transformed Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Enzyme Inhibitors - pharmacology Epidermis - embryology Heat-Shock Proteins - metabolism Heat-Shock Proteins - physiology Immunoblotting Immunohistochemistry Keratinocytes - cytology Keratinocytes - metabolism Keratins - chemistry Keratins - metabolism Mice Microscopy, Electron Microscopy, Fluorescence Mitogen-Activated Protein Kinases - metabolism Molecular Chaperones Neoplasm Proteins - metabolism Neoplasm Proteins - physiology p38 Mitogen-Activated Protein Kinases Phosphorylation Time Factors |
| title | HSP25 Is Involved in Two Steps of the Differentiation of PAM212 Keratinocytes |
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