Surface distribution and internalization of erbB-2 Proteins
We report the localization over the cell surface and the early steps of antibody-induced internalization of the product of the erbB-2 proto-oncogene, structurally related to the epidermal growth factor receptor (EGFR). We show that erbB-2/p185 is mostly excluded from endocytic pits on the cell surfa...
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Veröffentlicht in: | Experimental cell research 1992-10, Vol.202 (2), p.274-280 |
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creator | Lotti, Lavinia Vittoria Di Lazzaro, Claudia Zompetta, Claudia Frati, Luigi Torrisi, Maria Rosaria |
description | We report the localization over the cell surface and the early steps of antibody-induced internalization of the product of the erbB-2 proto-oncogene, structurally related to the epidermal growth factor receptor (EGFR). We show that erbB-2/p185 is mostly excluded from endocytic pits on the cell surface. Incubation at 37 °C with an anti-erbB-2/p185 monoclonal antibody induces the rapid entry of the protein into the cell. Similar internalization is shown by a chimeric molecule EGFB/erbB-2 in response to EGF. Both the timing and the pathway of internalization followed by the erbB-2/ p185 appear totally similar to those described for the EGFR. At variance with the normal erbB-2/p185, two mutant activated erbB-2 proteins are frequently localized within endocytic pits of the cell surface, indicating that mutations in the transmembrane regions may determine constitutive internalization of the protein. |
doi_str_mv | 10.1016/0014-4827(92)90075-J |
format | Article |
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We show that erbB-2/p185 is mostly excluded from endocytic pits on the cell surface. Incubation at 37 °C with an anti-erbB-2/p185 monoclonal antibody induces the rapid entry of the protein into the cell. Similar internalization is shown by a chimeric molecule EGFB/erbB-2 in response to EGF. Both the timing and the pathway of internalization followed by the erbB-2/ p185 appear totally similar to those described for the EGFR. At variance with the normal erbB-2/p185, two mutant activated erbB-2 proteins are frequently localized within endocytic pits of the cell surface, indicating that mutations in the transmembrane regions may determine constitutive internalization of the protein.</description><identifier>ISSN: 0014-4827</identifier><identifier>EISSN: 1090-2422</identifier><identifier>DOI: 10.1016/0014-4827(92)90075-J</identifier><identifier>PMID: 1356817</identifier><identifier>CODEN: ECREAL</identifier><language>eng</language><publisher>Orlando, FL: Elsevier Inc</publisher><subject>3T3 Cells ; Animals ; Antibodies, Monoclonal - immunology ; Biological and medical sciences ; Cell Membrane - metabolism ; Cell physiology ; Endocytosis ; Epidermal Growth Factor - physiology ; ErbB Receptors - genetics ; ErbB Receptors - metabolism ; Fluorescent Antibody Technique ; Fundamental and applied biological sciences. Psychology ; Mice ; Molecular and cellular biology ; Mutagenesis ; Phagocytosis ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins - immunology ; Proto-Oncogene Proteins - metabolism ; Receptor, ErbB-2 ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism</subject><ispartof>Experimental cell research, 1992-10, Vol.202 (2), p.274-280</ispartof><rights>1992</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-ff00d92d0d7b73cfc231f6faea756b4b1ad408e69366a3a2b84c9a07fd462fc73</citedby><cites>FETCH-LOGICAL-c417t-ff00d92d0d7b73cfc231f6faea756b4b1ad408e69366a3a2b84c9a07fd462fc73</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(92)90075-J$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4402338$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1356817$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lotti, Lavinia Vittoria</creatorcontrib><creatorcontrib>Di Lazzaro, Claudia</creatorcontrib><creatorcontrib>Zompetta, Claudia</creatorcontrib><creatorcontrib>Frati, Luigi</creatorcontrib><creatorcontrib>Torrisi, Maria Rosaria</creatorcontrib><title>Surface distribution and internalization of erbB-2 Proteins</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>We report the localization over the cell surface and the early steps of antibody-induced internalization of the product of the erbB-2 proto-oncogene, structurally related to the epidermal growth factor receptor (EGFR). We show that erbB-2/p185 is mostly excluded from endocytic pits on the cell surface. Incubation at 37 °C with an anti-erbB-2/p185 monoclonal antibody induces the rapid entry of the protein into the cell. Similar internalization is shown by a chimeric molecule EGFB/erbB-2 in response to EGF. Both the timing and the pathway of internalization followed by the erbB-2/ p185 appear totally similar to those described for the EGFR. At variance with the normal erbB-2/p185, two mutant activated erbB-2 proteins are frequently localized within endocytic pits of the cell surface, indicating that mutations in the transmembrane regions may determine constitutive internalization of the protein.</description><subject>3T3 Cells</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Cell physiology</subject><subject>Endocytosis</subject><subject>Epidermal Growth Factor - physiology</subject><subject>ErbB Receptors - genetics</subject><subject>ErbB Receptors - metabolism</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Mutagenesis</subject><subject>Phagocytosis</subject><subject>Proto-Oncogene Proteins - genetics</subject><subject>Proto-Oncogene Proteins - immunology</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Receptor, ErbB-2</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kNtKxDAQhoMouh7eQKEXInpRnRw2aREEXTwtCwrqdUiTCUS6rSatoE9v1130zquBme__GT5C9imcUqDyDICKXBRMHZfspARQ43y6RkYUSsiZYGydjH6RLbKd0isAFAWVm2ST8rEsqBqR86c-emMxcyF1MVR9F9omM43LQtNhbEwdvszPrvUZxuoqZ9ljbDsMTdolG97UCfdWc4e83Fw_T-7y2cPt_eRylltBVZd7D-BK5sCpSnHrLePUS2_QqLGsREWNE1CgLLmUhhtWFcKWBpR3QjJvFd8hR8vet9i-95g6PQ_JYl2bBts-aSpFyYVagGIJ2timFNHrtxjmJn5qCnrhTC-E6IUQXTL940xPh9jBqr-v5uj-QktJw_1wdTfJmtpH09iQfjEhgHFeDNjFEsPBxUfAqJMN2Fh0IaLttGvD_398A3NJh6Y</recordid><startdate>19921001</startdate><enddate>19921001</enddate><creator>Lotti, Lavinia Vittoria</creator><creator>Di Lazzaro, Claudia</creator><creator>Zompetta, Claudia</creator><creator>Frati, Luigi</creator><creator>Torrisi, Maria Rosaria</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>7TO</scope><scope>H94</scope></search><sort><creationdate>19921001</creationdate><title>Surface distribution and internalization of erbB-2 Proteins</title><author>Lotti, Lavinia Vittoria ; Di Lazzaro, Claudia ; Zompetta, Claudia ; Frati, Luigi ; Torrisi, Maria Rosaria</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-ff00d92d0d7b73cfc231f6faea756b4b1ad408e69366a3a2b84c9a07fd462fc73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>3T3 Cells</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - metabolism</topic><topic>Cell physiology</topic><topic>Endocytosis</topic><topic>Epidermal Growth Factor - physiology</topic><topic>ErbB Receptors - genetics</topic><topic>ErbB Receptors - metabolism</topic><topic>Fluorescent Antibody Technique</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Mutagenesis</topic><topic>Phagocytosis</topic><topic>Proto-Oncogene Proteins - genetics</topic><topic>Proto-Oncogene Proteins - immunology</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Receptor, ErbB-2</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lotti, Lavinia Vittoria</creatorcontrib><creatorcontrib>Di Lazzaro, Claudia</creatorcontrib><creatorcontrib>Zompetta, Claudia</creatorcontrib><creatorcontrib>Frati, Luigi</creatorcontrib><creatorcontrib>Torrisi, Maria Rosaria</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>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lotti, Lavinia Vittoria</au><au>Di Lazzaro, Claudia</au><au>Zompetta, Claudia</au><au>Frati, Luigi</au><au>Torrisi, Maria Rosaria</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Surface distribution and internalization of erbB-2 Proteins</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>1992-10-01</date><risdate>1992</risdate><volume>202</volume><issue>2</issue><spage>274</spage><epage>280</epage><pages>274-280</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><coden>ECREAL</coden><abstract>We report the localization over the cell surface and the early steps of antibody-induced internalization of the product of the erbB-2 proto-oncogene, structurally related to the epidermal growth factor receptor (EGFR). We show that erbB-2/p185 is mostly excluded from endocytic pits on the cell surface. Incubation at 37 °C with an anti-erbB-2/p185 monoclonal antibody induces the rapid entry of the protein into the cell. Similar internalization is shown by a chimeric molecule EGFB/erbB-2 in response to EGF. Both the timing and the pathway of internalization followed by the erbB-2/ p185 appear totally similar to those described for the EGFR. At variance with the normal erbB-2/p185, two mutant activated erbB-2 proteins are frequently localized within endocytic pits of the cell surface, indicating that mutations in the transmembrane regions may determine constitutive internalization of the protein.</abstract><cop>Orlando, FL</cop><pub>Elsevier Inc</pub><pmid>1356817</pmid><doi>10.1016/0014-4827(92)90075-J</doi><tpages>7</tpages></addata></record> |
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subjects | 3T3 Cells Animals Antibodies, Monoclonal - immunology Biological and medical sciences Cell Membrane - metabolism Cell physiology Endocytosis Epidermal Growth Factor - physiology ErbB Receptors - genetics ErbB Receptors - metabolism Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Mice Molecular and cellular biology Mutagenesis Phagocytosis Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - immunology Proto-Oncogene Proteins - metabolism Receptor, ErbB-2 Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism |
title | Surface distribution and internalization of erbB-2 Proteins |
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