PLP2/A4 interacts with CCR1 and stimulates migration of CCR1-expressing HOS cells
Multiple CC chemokines bind to CCR1, which plays important roles in immune and inflammatory responses. To search for proteins involved in the CCR1 signaling pathway, we screened a yeast two-hybrid library using the cytoplasmic tail of CCR1 as the bait. One of the positive clones contained an open re...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2004-11, Vol.324 (2), p.768-772 |
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| creator | Lee, Sang Min Shin, Hwayean Jang, Sung-Wuk Shim, Jung-Jae Song, In-sung Son, Kyung-No Hwang, Jungsu Shin, Yong-Hyun Kim, Hong-Hee Lee, Chong-Kil Ko, Jesang Na, Doe Sun Kwon, Byoung S. Kim, Jiyoung |
| description | Multiple CC chemokines bind to CCR1, which plays important roles in immune and inflammatory responses. To search for proteins involved in the CCR1 signaling pathway, we screened a yeast two-hybrid library using the cytoplasmic tail of CCR1 as the bait. One of the positive clones contained an open reading frame of 456bp, of which the nucleotide sequence was identical to that of proteolipid protein 2 (PLP2), also known as protein A4. Mammalian two-hybrid and coimmunoprecipitation analyses demonstrated the association of PLP2/A4 with CCR1. Indirect immunofluorescence analysis revealed that PLP2/A4 was predominantly located in plasma membrane and colocalized with CCR1 in transfected human HEK293 cells. In addition, focal staining of CCR1 appeared on the periphery of the membrane upon short exposure to Leukotactin-1(Lkn-1)/CCL15, a CCR1 agonist, and was costained with PLP2/A4 on the focal regions. PLP2/A4 mRNAs were detected in various cells such as U-937, HL-60, HEK293, and HOS cells. Overexpression of PLP2/A4 stimulated a twofold increase in the agonist-induced migration of HOS/CCR1 cells, implicating a functional role for PLP2/A4 in the chemotactic processes via CCR1. |
| doi_str_mv | 10.1016/j.bbrc.2004.09.118 |
| format | Article |
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To search for proteins involved in the CCR1 signaling pathway, we screened a yeast two-hybrid library using the cytoplasmic tail of CCR1 as the bait. One of the positive clones contained an open reading frame of 456bp, of which the nucleotide sequence was identical to that of proteolipid protein 2 (PLP2), also known as protein A4. Mammalian two-hybrid and coimmunoprecipitation analyses demonstrated the association of PLP2/A4 with CCR1. Indirect immunofluorescence analysis revealed that PLP2/A4 was predominantly located in plasma membrane and colocalized with CCR1 in transfected human HEK293 cells. In addition, focal staining of CCR1 appeared on the periphery of the membrane upon short exposure to Leukotactin-1(Lkn-1)/CCL15, a CCR1 agonist, and was costained with PLP2/A4 on the focal regions. PLP2/A4 mRNAs were detected in various cells such as U-937, HL-60, HEK293, and HOS cells. Overexpression of PLP2/A4 stimulated a twofold increase in the agonist-induced migration of HOS/CCR1 cells, implicating a functional role for PLP2/A4 in the chemotactic processes via CCR1.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2004.09.118</identifier><identifier>PMID: 15474493</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Blotting, Western ; CCR1 ; Cell Line ; Cell Line, Tumor ; Cell Movement ; Chemokine receptor ; Chemotaxis ; Chloramphenicol O-Acetyltransferase - metabolism ; Cytoplasm - metabolism ; Fluorescent Antibody Technique, Indirect ; HL-60 Cells ; Humans ; Immunoprecipitation ; MARVEL Domain-Containing Proteins ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Microscopy, Confocal ; Microscopy, Fluorescence ; Molecular Sequence Data ; Open Reading Frames ; Plasmids - metabolism ; Protein A4 ; Protein Binding ; Protein interaction ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases - metabolism ; Proteolipid protein 2 ; Proteolipids ; Reverse Transcriptase Polymerase Chain Reaction ; RNA - metabolism ; Saccharomyces cerevisiae - metabolism ; Sarcoma - metabolism ; Signal Transduction ; Transfection ; Two-Hybrid System Techniques ; U937 Cells</subject><ispartof>Biochemical and biophysical research communications, 2004-11, Vol.324 (2), p.768-772</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c352t-458e400b08a7bc389d3db532bbb52e7a4fae93ba8cf9ffdf102cf2c0fd0face63</citedby><cites>FETCH-LOGICAL-c352t-458e400b08a7bc389d3db532bbb52e7a4fae93ba8cf9ffdf102cf2c0fd0face63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X04021072$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15474493$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Sang Min</creatorcontrib><creatorcontrib>Shin, Hwayean</creatorcontrib><creatorcontrib>Jang, Sung-Wuk</creatorcontrib><creatorcontrib>Shim, Jung-Jae</creatorcontrib><creatorcontrib>Song, In-sung</creatorcontrib><creatorcontrib>Son, Kyung-No</creatorcontrib><creatorcontrib>Hwang, Jungsu</creatorcontrib><creatorcontrib>Shin, Yong-Hyun</creatorcontrib><creatorcontrib>Kim, Hong-Hee</creatorcontrib><creatorcontrib>Lee, Chong-Kil</creatorcontrib><creatorcontrib>Ko, Jesang</creatorcontrib><creatorcontrib>Na, Doe Sun</creatorcontrib><creatorcontrib>Kwon, Byoung S.</creatorcontrib><creatorcontrib>Kim, Jiyoung</creatorcontrib><title>PLP2/A4 interacts with CCR1 and stimulates migration of CCR1-expressing HOS cells</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Multiple CC chemokines bind to CCR1, which plays important roles in immune and inflammatory responses. To search for proteins involved in the CCR1 signaling pathway, we screened a yeast two-hybrid library using the cytoplasmic tail of CCR1 as the bait. One of the positive clones contained an open reading frame of 456bp, of which the nucleotide sequence was identical to that of proteolipid protein 2 (PLP2), also known as protein A4. Mammalian two-hybrid and coimmunoprecipitation analyses demonstrated the association of PLP2/A4 with CCR1. Indirect immunofluorescence analysis revealed that PLP2/A4 was predominantly located in plasma membrane and colocalized with CCR1 in transfected human HEK293 cells. In addition, focal staining of CCR1 appeared on the periphery of the membrane upon short exposure to Leukotactin-1(Lkn-1)/CCL15, a CCR1 agonist, and was costained with PLP2/A4 on the focal regions. PLP2/A4 mRNAs were detected in various cells such as U-937, HL-60, HEK293, and HOS cells. Overexpression of PLP2/A4 stimulated a twofold increase in the agonist-induced migration of HOS/CCR1 cells, implicating a functional role for PLP2/A4 in the chemotactic processes via CCR1.</description><subject>Amino Acid Sequence</subject><subject>Blotting, Western</subject><subject>CCR1</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Cell Movement</subject><subject>Chemokine receptor</subject><subject>Chemotaxis</subject><subject>Chloramphenicol O-Acetyltransferase - metabolism</subject><subject>Cytoplasm - metabolism</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>HL-60 Cells</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>MARVEL Domain-Containing Proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Microscopy, Confocal</subject><subject>Microscopy, Fluorescence</subject><subject>Molecular Sequence Data</subject><subject>Open Reading Frames</subject><subject>Plasmids - metabolism</subject><subject>Protein A4</subject><subject>Protein Binding</subject><subject>Protein interaction</subject><subject>Protein Structure, Tertiary</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proteolipid protein 2</subject><subject>Proteolipids</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA - metabolism</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Sarcoma - metabolism</subject><subject>Signal Transduction</subject><subject>Transfection</subject><subject>Two-Hybrid System Techniques</subject><subject>U937 Cells</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kLFu2zAURYkiQew4-YEOBadsUh4pShaBLIGR1gUM2GlToBtBUo8uDUtySLpJ_z5ybSBbprece3HfIeQzg5wBq243uTHB5hxA5CBzxupPZMxAQsYZiDMyBoAq45L9HpHLGDcAjIlKXpARK8VUCFmMyeNqseK394L6LmHQNkX64tMfOpv9YFR3DY3Jt_utThhp69dBJ993tHf_gQxfdwFj9N2azpc_qcXtNl6Rc6e3Ea9Pd0J-fX14ms2zxfLb99n9IrNFyVMmyhoFgIFaT40tatkUjSkLbowpOU61cBplYXRtnXSucQy4ddyCa8Bpi1UxITfH3l3on_cYk2p9PCzQHfb7qKpKilKU5QDyI2hDH2NAp3bBtzr8UwzUQaTaqINIdRCpQKpB5BD6cmrfmxab98jJ3ADcHQEcfvzrMahoPXYWGx_QJtX0_qP-N5nNhBA</recordid><startdate>20041112</startdate><enddate>20041112</enddate><creator>Lee, Sang Min</creator><creator>Shin, Hwayean</creator><creator>Jang, Sung-Wuk</creator><creator>Shim, Jung-Jae</creator><creator>Song, In-sung</creator><creator>Son, Kyung-No</creator><creator>Hwang, Jungsu</creator><creator>Shin, Yong-Hyun</creator><creator>Kim, Hong-Hee</creator><creator>Lee, Chong-Kil</creator><creator>Ko, Jesang</creator><creator>Na, Doe Sun</creator><creator>Kwon, Byoung S.</creator><creator>Kim, Jiyoung</creator><general>Elsevier Inc</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>20041112</creationdate><title>PLP2/A4 interacts with CCR1 and stimulates migration of CCR1-expressing HOS cells</title><author>Lee, Sang Min ; Shin, Hwayean ; Jang, Sung-Wuk ; Shim, Jung-Jae ; Song, In-sung ; Son, Kyung-No ; Hwang, Jungsu ; Shin, Yong-Hyun ; Kim, Hong-Hee ; Lee, Chong-Kil ; Ko, Jesang ; Na, Doe Sun ; Kwon, Byoung S. ; Kim, Jiyoung</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c352t-458e400b08a7bc389d3db532bbb52e7a4fae93ba8cf9ffdf102cf2c0fd0face63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Blotting, Western</topic><topic>CCR1</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>Cell Movement</topic><topic>Chemokine receptor</topic><topic>Chemotaxis</topic><topic>Chloramphenicol O-Acetyltransferase - metabolism</topic><topic>Cytoplasm - metabolism</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>HL-60 Cells</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>MARVEL Domain-Containing Proteins</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Microscopy, Confocal</topic><topic>Microscopy, Fluorescence</topic><topic>Molecular Sequence Data</topic><topic>Open Reading Frames</topic><topic>Plasmids - metabolism</topic><topic>Protein A4</topic><topic>Protein Binding</topic><topic>Protein interaction</topic><topic>Protein Structure, Tertiary</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proteolipid protein 2</topic><topic>Proteolipids</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA - metabolism</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Sarcoma - metabolism</topic><topic>Signal Transduction</topic><topic>Transfection</topic><topic>Two-Hybrid System Techniques</topic><topic>U937 Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Sang Min</creatorcontrib><creatorcontrib>Shin, Hwayean</creatorcontrib><creatorcontrib>Jang, Sung-Wuk</creatorcontrib><creatorcontrib>Shim, Jung-Jae</creatorcontrib><creatorcontrib>Song, In-sung</creatorcontrib><creatorcontrib>Son, Kyung-No</creatorcontrib><creatorcontrib>Hwang, Jungsu</creatorcontrib><creatorcontrib>Shin, Yong-Hyun</creatorcontrib><creatorcontrib>Kim, Hong-Hee</creatorcontrib><creatorcontrib>Lee, Chong-Kil</creatorcontrib><creatorcontrib>Ko, Jesang</creatorcontrib><creatorcontrib>Na, Doe Sun</creatorcontrib><creatorcontrib>Kwon, Byoung S.</creatorcontrib><creatorcontrib>Kim, Jiyoung</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Sang Min</au><au>Shin, Hwayean</au><au>Jang, Sung-Wuk</au><au>Shim, Jung-Jae</au><au>Song, In-sung</au><au>Son, Kyung-No</au><au>Hwang, Jungsu</au><au>Shin, Yong-Hyun</au><au>Kim, Hong-Hee</au><au>Lee, Chong-Kil</au><au>Ko, Jesang</au><au>Na, Doe Sun</au><au>Kwon, Byoung S.</au><au>Kim, Jiyoung</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PLP2/A4 interacts with CCR1 and stimulates migration of CCR1-expressing HOS cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2004-11-12</date><risdate>2004</risdate><volume>324</volume><issue>2</issue><spage>768</spage><epage>772</epage><pages>768-772</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Multiple CC chemokines bind to CCR1, which plays important roles in immune and inflammatory responses. To search for proteins involved in the CCR1 signaling pathway, we screened a yeast two-hybrid library using the cytoplasmic tail of CCR1 as the bait. One of the positive clones contained an open reading frame of 456bp, of which the nucleotide sequence was identical to that of proteolipid protein 2 (PLP2), also known as protein A4. Mammalian two-hybrid and coimmunoprecipitation analyses demonstrated the association of PLP2/A4 with CCR1. Indirect immunofluorescence analysis revealed that PLP2/A4 was predominantly located in plasma membrane and colocalized with CCR1 in transfected human HEK293 cells. In addition, focal staining of CCR1 appeared on the periphery of the membrane upon short exposure to Leukotactin-1(Lkn-1)/CCL15, a CCR1 agonist, and was costained with PLP2/A4 on the focal regions. PLP2/A4 mRNAs were detected in various cells such as U-937, HL-60, HEK293, and HOS cells. Overexpression of PLP2/A4 stimulated a twofold increase in the agonist-induced migration of HOS/CCR1 cells, implicating a functional role for PLP2/A4 in the chemotactic processes via CCR1.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15474493</pmid><doi>10.1016/j.bbrc.2004.09.118</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2004-11, Vol.324 (2), p.768-772 |
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| subjects | Amino Acid Sequence Blotting, Western CCR1 Cell Line Cell Line, Tumor Cell Movement Chemokine receptor Chemotaxis Chloramphenicol O-Acetyltransferase - metabolism Cytoplasm - metabolism Fluorescent Antibody Technique, Indirect HL-60 Cells Humans Immunoprecipitation MARVEL Domain-Containing Proteins Membrane Proteins - chemistry Membrane Proteins - metabolism Microscopy, Confocal Microscopy, Fluorescence Molecular Sequence Data Open Reading Frames Plasmids - metabolism Protein A4 Protein Binding Protein interaction Protein Structure, Tertiary Protein-Serine-Threonine Kinases - metabolism Proteolipid protein 2 Proteolipids Reverse Transcriptase Polymerase Chain Reaction RNA - metabolism Saccharomyces cerevisiae - metabolism Sarcoma - metabolism Signal Transduction Transfection Two-Hybrid System Techniques U937 Cells |
| title | PLP2/A4 interacts with CCR1 and stimulates migration of CCR1-expressing HOS cells |
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