Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene encoding a putative actin-associated protein (p27)
A cDNA clone for a basic putative actin microfilament-associated protein, p27, highly induced in serum-stimulated NIH 3T3 cells, has been isolated by polyclonal antibodies and sequenced. p27 mRNA is a 1.2-kb molecule which is very low in resting NIH 3T3 cells but can be induced at least 100 times af...
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| Veröffentlicht in: | Experimental cell research 1989-04, Vol.181 (2), p.518-530 |
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| creator | Almendral, J.M. Santarén, J.F. Perera, J. Zerial, M. Bravo, R. |
| description | A cDNA clone for a basic putative actin microfilament-associated protein, p27, highly induced in serum-stimulated NIH 3T3 cells, has been isolated by polyclonal antibodies and sequenced. p27 mRNA is a 1.2-kb molecule which is very low in resting NIH 3T3 cells but can be induced at least 100 times after 8 h of fetal calf serum stimulation. In contrast to other inducible mRNAs, p27 mRNA is stable, and its levels can be superinduced by cycloheximide mainly by prolonging transcription. The lack of expression of this messenger in mouse tissues, as well as in all cell lines so far tested, suggests that p27 may be an fibroblast-specific protein. One major open reading frame found in p27 cDNA codes for a 201 amino acid polypeptide not related to any previously described actin-binding protein. Interestingly, it shows alternative hydrophilic and hydrophobic domains of amino acids symmetrically arranged from the middle of the protein. The coordinate induction of p27 and actin mRNAs suggest that p27 may be involved in the cytoskeletal rearrangements induced early in cell growth and proliferation. |
| doi_str_mv | 10.1016/0014-4827(89)90108-0 |
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In contrast to other inducible mRNAs, p27 mRNA is stable, and its levels can be superinduced by cycloheximide mainly by prolonging transcription. The lack of expression of this messenger in mouse tissues, as well as in all cell lines so far tested, suggests that p27 may be an fibroblast-specific protein. One major open reading frame found in p27 cDNA codes for a 201 amino acid polypeptide not related to any previously described actin-binding protein. Interestingly, it shows alternative hydrophilic and hydrophobic domains of amino acids symmetrically arranged from the middle of the protein. The coordinate induction of p27 and actin mRNAs suggest that p27 may be involved in the cytoskeletal rearrangements induced early in cell growth and proliferation.</description><identifier>ISSN: 0014-4827</identifier><identifier>EISSN: 1090-2422</identifier><identifier>DOI: 10.1016/0014-4827(89)90108-0</identifier><identifier>PMID: 2924801</identifier><identifier>CODEN: ECREAL</identifier><language>eng</language><publisher>Orlando, FL: Elsevier Inc</publisher><subject>actin ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Base Sequence ; Binding and carrier proteins ; Biological and medical sciences ; Blood ; Cell Line ; Cloning, Molecular ; Culture Media ; Cycloheximide - pharmacology ; DNA - genetics ; Fundamental and applied biological sciences. Psychology ; Interphase ; mice ; Microfilament Proteins - biosynthesis ; Microfilament Proteins - genetics ; microfilament-associated protein p27 ; Molecular Sequence Data ; Molecular Weight ; Muscle Proteins ; Protein Biosynthesis ; Proteins ; RNA, Messenger - genetics ; Transcription, Genetic</subject><ispartof>Experimental cell research, 1989-04, Vol.181 (2), p.518-530</ispartof><rights>1989</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-f6f9aad75436c884c04d7076391e137d5b2f91c8f46dd7c7967749a29b52080c3</citedby><cites>FETCH-LOGICAL-c484t-f6f9aad75436c884c04d7076391e137d5b2f91c8f46dd7c7967749a29b52080c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-4827(89)90108-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19311520$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2924801$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Almendral, J.M.</creatorcontrib><creatorcontrib>Santarén, J.F.</creatorcontrib><creatorcontrib>Perera, J.</creatorcontrib><creatorcontrib>Zerial, M.</creatorcontrib><creatorcontrib>Bravo, R.</creatorcontrib><title>Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene encoding a putative actin-associated protein (p27)</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>A cDNA clone for a basic putative actin microfilament-associated protein, p27, highly induced in serum-stimulated NIH 3T3 cells, has been isolated by polyclonal antibodies and sequenced. p27 mRNA is a 1.2-kb molecule which is very low in resting NIH 3T3 cells but can be induced at least 100 times after 8 h of fetal calf serum stimulation. In contrast to other inducible mRNAs, p27 mRNA is stable, and its levels can be superinduced by cycloheximide mainly by prolonging transcription. The lack of expression of this messenger in mouse tissues, as well as in all cell lines so far tested, suggests that p27 may be an fibroblast-specific protein. One major open reading frame found in p27 cDNA codes for a 201 amino acid polypeptide not related to any previously described actin-binding protein. Interestingly, it shows alternative hydrophilic and hydrophobic domains of amino acids symmetrically arranged from the middle of the protein. The coordinate induction of p27 and actin mRNAs suggest that p27 may be involved in the cytoskeletal rearrangements induced early in cell growth and proliferation.</description><subject>actin</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Blood</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>Culture Media</subject><subject>Cycloheximide - pharmacology</subject><subject>DNA - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Interphase</subject><subject>mice</subject><subject>Microfilament Proteins - biosynthesis</subject><subject>Microfilament Proteins - genetics</subject><subject>microfilament-associated protein p27</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Muscle Proteins</subject><subject>Protein Biosynthesis</subject><subject>Proteins</subject><subject>RNA, Messenger - genetics</subject><subject>Transcription, Genetic</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9vFSEUxYnR1NfqN9CEjaZNHL0wzACbJk1b_ySNbnRNGGBeMPNgBKbRhd9d5r2XutMVi_s7h3vPQegFgbcESP8OgLCGCcrPhbyQQEA08AhtCEhoKKP0Mdo8IE_Rac7fAUAI0p-gEyopE0A26Pftzzm5nH0Mb7CZYvBhi3Ww2Nx8vsLZ_VhcMA7HEWs8-iHFYdK51EFadk1y22XSxVm8dcHhSka71-N5Kbr4e4e1KT40Oudo_J6cUyzOB3w-U37xDD0Z9ZTd8-N7hr69v_16_bG5-_Lh0_XVXWOYYKUZ-1FqbXnH2t4IwQwwy4H3rSSOtNx2Ax0lMWJkvbXccNlzzqSmcugoCDDtGXp98K2_14tyUTufjZsmHVxcsuJCcNK3_L8g6WpunHUVZAfQpJhzcqOak9_p9EsRUGs9as1erdkrIdW-HgVV9vLovww7Zx9Exz7q_NVxrrPR05h0MD7_9ZYtqSusPpcHztXU7r1LKhu_NmV9cqYoG_2_F_kD5burMQ</recordid><startdate>19890401</startdate><enddate>19890401</enddate><creator>Almendral, J.M.</creator><creator>Santarén, J.F.</creator><creator>Perera, J.</creator><creator>Zerial, M.</creator><creator>Bravo, R.</creator><general>Elsevier Inc</general><general>Elsevier</general><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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19890401</creationdate><title>Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene encoding a putative actin-associated protein (p27)</title><author>Almendral, J.M. ; Santarén, J.F. ; Perera, J. ; Zerial, M. ; Bravo, R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c484t-f6f9aad75436c884c04d7076391e137d5b2f91c8f46dd7c7967749a29b52080c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>actin</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Blood</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>Culture Media</topic><topic>Cycloheximide - pharmacology</topic><topic>DNA - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Interphase</topic><topic>mice</topic><topic>Microfilament Proteins - biosynthesis</topic><topic>Microfilament Proteins - genetics</topic><topic>microfilament-associated protein p27</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Muscle Proteins</topic><topic>Protein Biosynthesis</topic><topic>Proteins</topic><topic>RNA, Messenger - genetics</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Almendral, J.M.</creatorcontrib><creatorcontrib>Santarén, J.F.</creatorcontrib><creatorcontrib>Perera, J.</creatorcontrib><creatorcontrib>Zerial, M.</creatorcontrib><creatorcontrib>Bravo, R.</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Almendral, J.M.</au><au>Santarén, J.F.</au><au>Perera, J.</au><au>Zerial, M.</au><au>Bravo, R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene encoding a putative actin-associated protein (p27)</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>1989-04-01</date><risdate>1989</risdate><volume>181</volume><issue>2</issue><spage>518</spage><epage>530</epage><pages>518-530</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><coden>ECREAL</coden><abstract>A cDNA clone for a basic putative actin microfilament-associated protein, p27, highly induced in serum-stimulated NIH 3T3 cells, has been isolated by polyclonal antibodies and sequenced. p27 mRNA is a 1.2-kb molecule which is very low in resting NIH 3T3 cells but can be induced at least 100 times after 8 h of fetal calf serum stimulation. In contrast to other inducible mRNAs, p27 mRNA is stable, and its levels can be superinduced by cycloheximide mainly by prolonging transcription. The lack of expression of this messenger in mouse tissues, as well as in all cell lines so far tested, suggests that p27 may be an fibroblast-specific protein. One major open reading frame found in p27 cDNA codes for a 201 amino acid polypeptide not related to any previously described actin-binding protein. Interestingly, it shows alternative hydrophilic and hydrophobic domains of amino acids symmetrically arranged from the middle of the protein. The coordinate induction of p27 and actin mRNAs suggest that p27 may be involved in the cytoskeletal rearrangements induced early in cell growth and proliferation.</abstract><cop>Orlando, FL</cop><pub>Elsevier Inc</pub><pmid>2924801</pmid><doi>10.1016/0014-4827(89)90108-0</doi><tpages>13</tpages></addata></record> |
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| subjects | actin Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Binding and carrier proteins Biological and medical sciences Blood Cell Line Cloning, Molecular Culture Media Cycloheximide - pharmacology DNA - genetics Fundamental and applied biological sciences. Psychology Interphase mice Microfilament Proteins - biosynthesis Microfilament Proteins - genetics microfilament-associated protein p27 Molecular Sequence Data Molecular Weight Muscle Proteins Protein Biosynthesis Proteins RNA, Messenger - genetics Transcription, Genetic |
| title | Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene encoding a putative actin-associated protein (p27) |
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