Mouse PeP: A novel peroxisomal protein linked to myoblast differentiation and development
The identification of several peroxisomal proteins in the past decade has deepened our understanding of the biology of peroxisomes and their involvement in human disorders. We report the cloning and expression pattern during the mouse development of a cDNA encoding a novel protein, named PeP, and sh...
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Veröffentlicht in: | Developmental dynamics 2002-06, Vol.224 (2), p.154-167 |
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description | The identification of several peroxisomal proteins in the past decade has deepened our understanding of the biology of peroxisomes and their involvement in human disorders. We report the cloning and expression pattern during the mouse development of a cDNA encoding a novel protein, named PeP, and show that its product is imported specifically to the peroxisome matrix in a variety of cell types. We also demonstrate that PeP is imported to the organelle through the PEX5 receptor pathway, which indicates that the C‐terminal tripeptide SKI behaves as a type 1 peroxisomal targeting signal (PTS1). PeP expression is tightly regulated, as shown by Northern and in situ hybridization experiments. Thus during embryonic development in the mouse, PeP mRNA is detected almost exclusively in the skeletal muscle, whereas in adult mice, strong expression is also found in the heart and brain. In addition, PeP mRNA accumulation is induced after myoblast differentiation in vitro, when myotube formation is promoted. Sequence analysis reveals that PeP has no significant homology to any known protein, except for a short stretch of amino acids containing the fingerprint of the fibronectin type III superfamily, a domain present in proteins often related to molecular and cellular recognition and binding processes. Thus our data suggest a connection between the function of PeP and murine cell differentiation and development. © 2002 Wiley‐Liss, Inc. |
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We report the cloning and expression pattern during the mouse development of a cDNA encoding a novel protein, named PeP, and show that its product is imported specifically to the peroxisome matrix in a variety of cell types. We also demonstrate that PeP is imported to the organelle through the PEX5 receptor pathway, which indicates that the C‐terminal tripeptide SKI behaves as a type 1 peroxisomal targeting signal (PTS1). PeP expression is tightly regulated, as shown by Northern and in situ hybridization experiments. Thus during embryonic development in the mouse, PeP mRNA is detected almost exclusively in the skeletal muscle, whereas in adult mice, strong expression is also found in the heart and brain. In addition, PeP mRNA accumulation is induced after myoblast differentiation in vitro, when myotube formation is promoted. Sequence analysis reveals that PeP has no significant homology to any known protein, except for a short stretch of amino acids containing the fingerprint of the fibronectin type III superfamily, a domain present in proteins often related to molecular and cellular recognition and binding processes. Thus our data suggest a connection between the function of PeP and murine cell differentiation and development. © 2002 Wiley‐Liss, Inc.</description><identifier>ISSN: 1058-8388</identifier><identifier>EISSN: 1097-0177</identifier><identifier>DOI: 10.1002/dvdy.10099</identifier><identifier>PMID: 12112469</identifier><language>eng</language><publisher>New York: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Bezafibrate - pharmacology ; Blotting, Northern ; Cell Differentiation ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; DNA - metabolism ; DNA, Complementary - metabolism ; embryo development ; fibronectin type III domain ; Fibronectins - metabolism ; Gene Expression Regulation, Developmental ; Gene Library ; Green Fluorescent Proteins ; Humans ; Hypolipidemic Agents - pharmacology ; In Situ Hybridization ; Luminescent Proteins - metabolism ; Male ; Mice ; Microscopy, Fluorescence ; Models, Genetic ; Molecular Sequence Data ; Muscles - cytology ; Muscles - embryology ; Myoblasts - cytology ; myotube ; Peptides - chemistry ; peroxisomal targeting signal ; Peroxisomes - metabolism ; Plasmids - metabolism ; Polymerase Chain Reaction ; Protein Biosynthesis ; Protein Structure, Tertiary ; Proteins - chemistry ; Proteins - genetics ; PTS1 ; Rats ; Rats, Wistar ; RNA, Messenger - metabolism ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Time Factors ; Tissue Distribution ; Transfection ; Up-Regulation</subject><ispartof>Developmental dynamics, 2002-06, Vol.224 (2), p.154-167</ispartof><rights>Copyright © 2002 Wiley‐Liss, Inc.</rights><rights>Copyright 2002 Wiley-Liss, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4279-c39dadd1500f478b290d85adcf4d0fbfeda5959b3391c58e34985eb3c1cb32a23</citedby><cites>FETCH-LOGICAL-c4279-c39dadd1500f478b290d85adcf4d0fbfeda5959b3391c58e34985eb3c1cb32a23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fdvdy.10099$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fdvdy.10099$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,1428,27905,27906,45555,45556,46390,46814</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12112469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ferrer‐Martínez, Andreu</creatorcontrib><creatorcontrib>Ruiz‐Lozano, Pilar</creatorcontrib><creatorcontrib>Chien, Kenneth R.</creatorcontrib><title>Mouse PeP: A novel peroxisomal protein linked to myoblast differentiation and development</title><title>Developmental dynamics</title><addtitle>Dev Dyn</addtitle><description>The identification of several peroxisomal proteins in the past decade has deepened our understanding of the biology of peroxisomes and their involvement in human disorders. We report the cloning and expression pattern during the mouse development of a cDNA encoding a novel protein, named PeP, and show that its product is imported specifically to the peroxisome matrix in a variety of cell types. We also demonstrate that PeP is imported to the organelle through the PEX5 receptor pathway, which indicates that the C‐terminal tripeptide SKI behaves as a type 1 peroxisomal targeting signal (PTS1). PeP expression is tightly regulated, as shown by Northern and in situ hybridization experiments. Thus during embryonic development in the mouse, PeP mRNA is detected almost exclusively in the skeletal muscle, whereas in adult mice, strong expression is also found in the heart and brain. In addition, PeP mRNA accumulation is induced after myoblast differentiation in vitro, when myotube formation is promoted. Sequence analysis reveals that PeP has no significant homology to any known protein, except for a short stretch of amino acids containing the fingerprint of the fibronectin type III superfamily, a domain present in proteins often related to molecular and cellular recognition and binding processes. Thus our data suggest a connection between the function of PeP and murine cell differentiation and development. © 2002 Wiley‐Liss, Inc.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Bezafibrate - pharmacology</subject><subject>Blotting, Northern</subject><subject>Cell Differentiation</subject><subject>Cell Line</subject><subject>Cells, Cultured</subject><subject>Cloning, Molecular</subject><subject>DNA - metabolism</subject><subject>DNA, Complementary - metabolism</subject><subject>embryo development</subject><subject>fibronectin type III domain</subject><subject>Fibronectins - metabolism</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Gene Library</subject><subject>Green Fluorescent Proteins</subject><subject>Humans</subject><subject>Hypolipidemic Agents - pharmacology</subject><subject>In Situ Hybridization</subject><subject>Luminescent Proteins - metabolism</subject><subject>Male</subject><subject>Mice</subject><subject>Microscopy, Fluorescence</subject><subject>Models, Genetic</subject><subject>Molecular Sequence Data</subject><subject>Muscles - cytology</subject><subject>Muscles - embryology</subject><subject>Myoblasts - cytology</subject><subject>myotube</subject><subject>Peptides - chemistry</subject><subject>peroxisomal targeting signal</subject><subject>Peroxisomes - metabolism</subject><subject>Plasmids - metabolism</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Biosynthesis</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>PTS1</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Time Factors</subject><subject>Tissue Distribution</subject><subject>Transfection</subject><subject>Up-Regulation</subject><issn>1058-8388</issn><issn>1097-0177</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMotlYv_gDJyYOwmuxHN_FWWr9AsQcVegrZZALR3U3dbKv77826BW-e5mV4eJh5ETql5JISEl_pre76xPkeGlPC84jQPN_vc8YiljA2QkfevxNC2DSlh2hEY0rjdMrHaPXkNh7wEpbXeIZrt4USr6Fx39a7SobcuBZsjUtbf4DGrcNV54pS-hZraww0ULdWttbVWNYaawgCt67C9hgdGFl6ONnNCXq9vXmZ30ePz3cP89ljpNI455FKuJZa04wQk-asiDnRLJNamVQTUxjQMuMZL5KEU5UxSFLOMigSRVWRxDJOJuh88IZTPzfgW1FZr6AsZQ3hN5FTTlKWswBeDKBqnPcNGLFubCWbTlAi-iJFX6T4LTLAZzvrpqhA_6G75gJAB-DLltD9oxKLt8VqkP4A2lR_og</recordid><startdate>200206</startdate><enddate>200206</enddate><creator>Ferrer‐Martínez, Andreu</creator><creator>Ruiz‐Lozano, Pilar</creator><creator>Chien, Kenneth R.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</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>7X8</scope></search><sort><creationdate>200206</creationdate><title>Mouse PeP: A novel peroxisomal protein linked to myoblast differentiation and development</title><author>Ferrer‐Martínez, Andreu ; Ruiz‐Lozano, Pilar ; Chien, Kenneth R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4279-c39dadd1500f478b290d85adcf4d0fbfeda5959b3391c58e34985eb3c1cb32a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Bezafibrate - pharmacology</topic><topic>Blotting, Northern</topic><topic>Cell Differentiation</topic><topic>Cell Line</topic><topic>Cells, Cultured</topic><topic>Cloning, Molecular</topic><topic>DNA - metabolism</topic><topic>DNA, Complementary - metabolism</topic><topic>embryo development</topic><topic>fibronectin type III domain</topic><topic>Fibronectins - metabolism</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Gene Library</topic><topic>Green Fluorescent Proteins</topic><topic>Humans</topic><topic>Hypolipidemic Agents - pharmacology</topic><topic>In Situ Hybridization</topic><topic>Luminescent Proteins - metabolism</topic><topic>Male</topic><topic>Mice</topic><topic>Microscopy, Fluorescence</topic><topic>Models, Genetic</topic><topic>Molecular Sequence Data</topic><topic>Muscles - cytology</topic><topic>Muscles - embryology</topic><topic>Myoblasts - cytology</topic><topic>myotube</topic><topic>Peptides - chemistry</topic><topic>peroxisomal targeting signal</topic><topic>Peroxisomes - metabolism</topic><topic>Plasmids - metabolism</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Biosynthesis</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>PTS1</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Time Factors</topic><topic>Tissue Distribution</topic><topic>Transfection</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ferrer‐Martínez, Andreu</creatorcontrib><creatorcontrib>Ruiz‐Lozano, Pilar</creatorcontrib><creatorcontrib>Chien, Kenneth R.</creatorcontrib><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>Developmental dynamics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ferrer‐Martínez, Andreu</au><au>Ruiz‐Lozano, Pilar</au><au>Chien, Kenneth R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mouse PeP: A novel peroxisomal protein linked to myoblast differentiation and development</atitle><jtitle>Developmental dynamics</jtitle><addtitle>Dev Dyn</addtitle><date>2002-06</date><risdate>2002</risdate><volume>224</volume><issue>2</issue><spage>154</spage><epage>167</epage><pages>154-167</pages><issn>1058-8388</issn><eissn>1097-0177</eissn><abstract>The identification of several peroxisomal proteins in the past decade has deepened our understanding of the biology of peroxisomes and their involvement in human disorders. We report the cloning and expression pattern during the mouse development of a cDNA encoding a novel protein, named PeP, and show that its product is imported specifically to the peroxisome matrix in a variety of cell types. We also demonstrate that PeP is imported to the organelle through the PEX5 receptor pathway, which indicates that the C‐terminal tripeptide SKI behaves as a type 1 peroxisomal targeting signal (PTS1). PeP expression is tightly regulated, as shown by Northern and in situ hybridization experiments. Thus during embryonic development in the mouse, PeP mRNA is detected almost exclusively in the skeletal muscle, whereas in adult mice, strong expression is also found in the heart and brain. In addition, PeP mRNA accumulation is induced after myoblast differentiation in vitro, when myotube formation is promoted. Sequence analysis reveals that PeP has no significant homology to any known protein, except for a short stretch of amino acids containing the fingerprint of the fibronectin type III superfamily, a domain present in proteins often related to molecular and cellular recognition and binding processes. Thus our data suggest a connection between the function of PeP and murine cell differentiation and development. © 2002 Wiley‐Liss, Inc.</abstract><cop>New York</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>12112469</pmid><doi>10.1002/dvdy.10099</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Base Sequence Bezafibrate - pharmacology Blotting, Northern Cell Differentiation Cell Line Cells, Cultured Cloning, Molecular DNA - metabolism DNA, Complementary - metabolism embryo development fibronectin type III domain Fibronectins - metabolism Gene Expression Regulation, Developmental Gene Library Green Fluorescent Proteins Humans Hypolipidemic Agents - pharmacology In Situ Hybridization Luminescent Proteins - metabolism Male Mice Microscopy, Fluorescence Models, Genetic Molecular Sequence Data Muscles - cytology Muscles - embryology Myoblasts - cytology myotube Peptides - chemistry peroxisomal targeting signal Peroxisomes - metabolism Plasmids - metabolism Polymerase Chain Reaction Protein Biosynthesis Protein Structure, Tertiary Proteins - chemistry Proteins - genetics PTS1 Rats Rats, Wistar RNA, Messenger - metabolism Sequence Analysis, DNA Sequence Homology, Amino Acid Time Factors Tissue Distribution Transfection Up-Regulation |
title | Mouse PeP: A novel peroxisomal protein linked to myoblast differentiation and development |
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