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Gene Expression and Phosphorylation of Mouse Osteopontin
Osteopontin is expressed in many different cell types and has been proposed to play several functions. Distinct forms of the protein have been detected. Various tissues and cell lines from mouse, however, exhibit two classes of transcripts with different 5'-untranslated ends but with an identic...
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| Published in: | Annals of the New York Academy of Sciences 1995-08, Vol.760 (1), p.35-43 |
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| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c352t-14bc4ab6e9582f331d3cb05ad10be4d085a68bab13447845ccff9e731b7116df3 |
| container_end_page | 43 |
| container_issue | 1 |
| container_start_page | 35 |
| container_title | Annals of the New York Academy of Sciences |
| container_volume | 760 |
| creator | SAAVEDRA, RAUL A. KIMBRO, SEAN K. STERN, DORIS N. SCHNUER, JAMIE ASHKAR, SAMY GLIMCHER, MELVIN J. LJUBETIC, CECILIA I. |
| description | Osteopontin is expressed in many different cell types and has been proposed to play several functions. Distinct forms of the protein have been detected. Various tissues and cell lines from mouse, however, exhibit two classes of transcripts with different 5'-untranslated ends but with an identical coding region (exons II through VII). These transcripts do not arise from the alternative splicing of coding exons. These results suggest that posttranslational modifications of osteopontin, such as phosphorylation, are a major mechanism to generate different forms of the protein. Mouse osteopontin was expressed in E. coli and used as a model to study its phosphorylation. |
| doi_str_mv | 10.1111/j.1749-6632.1995.tb44618.x |
| format | article |
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Distinct forms of the protein have been detected. Various tissues and cell lines from mouse, however, exhibit two classes of transcripts with different 5'-untranslated ends but with an identical coding region (exons II through VII). These transcripts do not arise from the alternative splicing of coding exons. These results suggest that posttranslational modifications of osteopontin, such as phosphorylation, are a major mechanism to generate different forms of the protein. Mouse osteopontin was expressed in E. coli and used as a model to study its phosphorylation.</description><identifier>ISSN: 0077-8923</identifier><identifier>EISSN: 1749-6632</identifier><identifier>DOI: 10.1111/j.1749-6632.1995.tb44618.x</identifier><identifier>PMID: 7540379</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Base Sequence ; Cell Adhesion ; DNA Primers - chemistry ; Gene Expression Regulation, Developmental ; Mice ; Molecular Sequence Data ; Osteopontin ; Phosphoproteins - metabolism ; Phosphorylation ; Phosphotyrosine ; RNA, Messenger - genetics ; Sialoglycoproteins - metabolism ; Tyrosine - analogs & derivatives ; Tyrosine - metabolism</subject><ispartof>Annals of the New York Academy of Sciences, 1995-08, Vol.760 (1), p.35-43</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c352t-14bc4ab6e9582f331d3cb05ad10be4d085a68bab13447845ccff9e731b7116df3</citedby><cites>FETCH-LOGICAL-c352t-14bc4ab6e9582f331d3cb05ad10be4d085a68bab13447845ccff9e731b7116df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7540379$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SAAVEDRA, RAUL A.</creatorcontrib><creatorcontrib>KIMBRO, SEAN K.</creatorcontrib><creatorcontrib>STERN, DORIS N.</creatorcontrib><creatorcontrib>SCHNUER, JAMIE</creatorcontrib><creatorcontrib>ASHKAR, SAMY</creatorcontrib><creatorcontrib>GLIMCHER, MELVIN J.</creatorcontrib><creatorcontrib>LJUBETIC, CECILIA I.</creatorcontrib><title>Gene Expression and Phosphorylation of Mouse Osteopontin</title><title>Annals of the New York Academy of Sciences</title><addtitle>Ann N Y Acad Sci</addtitle><description>Osteopontin is expressed in many different cell types and has been proposed to play several functions. Distinct forms of the protein have been detected. Various tissues and cell lines from mouse, however, exhibit two classes of transcripts with different 5'-untranslated ends but with an identical coding region (exons II through VII). These transcripts do not arise from the alternative splicing of coding exons. These results suggest that posttranslational modifications of osteopontin, such as phosphorylation, are a major mechanism to generate different forms of the protein. Mouse osteopontin was expressed in E. coli and used as a model to study its phosphorylation.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Cell Adhesion</subject><subject>DNA Primers - chemistry</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Osteopontin</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine</subject><subject>RNA, Messenger - genetics</subject><subject>Sialoglycoproteins - metabolism</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - metabolism</subject><issn>0077-8923</issn><issn>1749-6632</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNo9kFFLwzAUhYMoc05_glB88K01aZIm8U3mnMJ0e1C2t5C0Kevsmpp00P17W1Z2Xy7cc869lw-ABwQj1NXTLkKMiDBJcBwhIWjUaEISxKP2AozP0iUYQ8hYyEWMr8GN9zsIUcwJG4ERowRiJsaAz01lgllbO-N9YatAVVmw2lpfb607lqrpZzYPPu3Bm2DpG2NrWzVFdQuuclV6czf0Cfh5m31P38PFcv4xfVmEKaZxEyKiU6J0YgTlcY4xynCqIVUZgtqQDHKqEq6VRpgQxglN0zwXhmGkGUJJluMJeDztrZ39OxjfyH3hU1OWqjLdT5IxTBjmojM-n4yps947k8vaFXvljhJB2WOTO9mzkT0b2WOTAzbZduH74cpB7012jg6cOj086UVHoD3Lyv3KhGFG5fprLheb6eZ1xddyjf8BZI16EA</recordid><startdate>199508</startdate><enddate>199508</enddate><creator>SAAVEDRA, RAUL A.</creator><creator>KIMBRO, SEAN K.</creator><creator>STERN, DORIS N.</creator><creator>SCHNUER, JAMIE</creator><creator>ASHKAR, SAMY</creator><creator>GLIMCHER, MELVIN J.</creator><creator>LJUBETIC, CECILIA I.</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</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>199508</creationdate><title>Gene Expression and Phosphorylation of Mouse Osteopontin</title><author>SAAVEDRA, RAUL A. ; KIMBRO, SEAN K. ; STERN, DORIS N. ; SCHNUER, JAMIE ; ASHKAR, SAMY ; GLIMCHER, MELVIN J. ; LJUBETIC, CECILIA I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c352t-14bc4ab6e9582f331d3cb05ad10be4d085a68bab13447845ccff9e731b7116df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Cell Adhesion</topic><topic>DNA Primers - chemistry</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Osteopontin</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Phosphotyrosine</topic><topic>RNA, Messenger - genetics</topic><topic>Sialoglycoproteins - metabolism</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SAAVEDRA, RAUL A.</creatorcontrib><creatorcontrib>KIMBRO, SEAN K.</creatorcontrib><creatorcontrib>STERN, DORIS N.</creatorcontrib><creatorcontrib>SCHNUER, JAMIE</creatorcontrib><creatorcontrib>ASHKAR, SAMY</creatorcontrib><creatorcontrib>GLIMCHER, MELVIN J.</creatorcontrib><creatorcontrib>LJUBETIC, CECILIA I.</creatorcontrib><collection>Istex</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>Annals of the New York Academy of Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SAAVEDRA, RAUL A.</au><au>KIMBRO, SEAN K.</au><au>STERN, DORIS N.</au><au>SCHNUER, JAMIE</au><au>ASHKAR, SAMY</au><au>GLIMCHER, MELVIN J.</au><au>LJUBETIC, CECILIA I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene Expression and Phosphorylation of Mouse Osteopontin</atitle><jtitle>Annals of the New York Academy of Sciences</jtitle><addtitle>Ann N Y Acad Sci</addtitle><date>1995-08</date><risdate>1995</risdate><volume>760</volume><issue>1</issue><spage>35</spage><epage>43</epage><pages>35-43</pages><issn>0077-8923</issn><eissn>1749-6632</eissn><abstract>Osteopontin is expressed in many different cell types and has been proposed to play several functions. Distinct forms of the protein have been detected. Various tissues and cell lines from mouse, however, exhibit two classes of transcripts with different 5'-untranslated ends but with an identical coding region (exons II through VII). These transcripts do not arise from the alternative splicing of coding exons. These results suggest that posttranslational modifications of osteopontin, such as phosphorylation, are a major mechanism to generate different forms of the protein. Mouse osteopontin was expressed in E. coli and used as a model to study its phosphorylation.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>7540379</pmid><doi>10.1111/j.1749-6632.1995.tb44618.x</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0077-8923 |
| ispartof | Annals of the New York Academy of Sciences, 1995-08, Vol.760 (1), p.35-43 |
| issn | 0077-8923 1749-6632 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77347389 |
| source | Wiley-Blackwell Journals |
| subjects | Animals Base Sequence Cell Adhesion DNA Primers - chemistry Gene Expression Regulation, Developmental Mice Molecular Sequence Data Osteopontin Phosphoproteins - metabolism Phosphorylation Phosphotyrosine RNA, Messenger - genetics Sialoglycoproteins - metabolism Tyrosine - analogs & derivatives Tyrosine - metabolism |
| title | Gene Expression and Phosphorylation of Mouse Osteopontin |
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