Glycoprotein contributions to mammary gland and mammary tumor structure and function: Roles of adherens junctions, ErbBs and membrane MUCs
Mammary function is dependent on its three‐dimensional organization, which is established and maintained by cell adhesive junctions linked through the membrane to the cell cytoskeleton. These junctions serve not only as structural elements, but also function as initiators and integrators of cell sig...
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| Veröffentlicht in: | Journal of cellular biochemistry 2005-12, Vol.96 (5), p.914-926 |
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| container_title | Journal of cellular biochemistry |
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| creator | Carraway, Kermit L. Ramsauer, Victoria P. Carothers Carraway, Coralie A. |
| description | Mammary function is dependent on its three‐dimensional organization, which is established and maintained by cell adhesive junctions linked through the membrane to the cell cytoskeleton. These junctions serve not only as structural elements, but also function as initiators and integrators of cell signals. In this review we discuss three types of glycoproteins whose interactions impinge on the function of mammary cell–cell junctions, cadherins, ErbB receptor tyrosine kinases and membrane mucins, as a microcosm of events regulating mammary cell behaviors. Actions of these components are integrated by the critical signaling element β‐catenin. When functioning properly, these glycoproteins, β‐catenin and associated signaling pathways mesh into a highly structured program for development and function of the gland. However, disruption or dysfunction of these glycoproteins or the signaling elements can lead to disorganization of the epithelia and ultimately to neoplasia. J. Cell. Biochem. © 2005 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/jcb.20612 |
| format | Article |
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These junctions serve not only as structural elements, but also function as initiators and integrators of cell signals. In this review we discuss three types of glycoproteins whose interactions impinge on the function of mammary cell–cell junctions, cadherins, ErbB receptor tyrosine kinases and membrane mucins, as a microcosm of events regulating mammary cell behaviors. Actions of these components are integrated by the critical signaling element β‐catenin. When functioning properly, these glycoproteins, β‐catenin and associated signaling pathways mesh into a highly structured program for development and function of the gland. However, disruption or dysfunction of these glycoproteins or the signaling elements can lead to disorganization of the epithelia and ultimately to neoplasia. J. Cell. Biochem. © 2005 Wiley‐Liss, Inc.</description><identifier>ISSN: 0730-2312</identifier><identifier>EISSN: 1097-4644</identifier><identifier>DOI: 10.1002/jcb.20612</identifier><identifier>PMID: 16167329</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>adherens junctions ; Adherens Junctions - metabolism ; Animals ; Apoptosis ; beta Catenin - metabolism ; Breast Neoplasms - metabolism ; cadherin ; Cell Adhesion ; Cell Communication ; Cell Membrane - metabolism ; Epithelial Cells - metabolism ; ErbB ; Gap Junctions ; Glycoproteins - metabolism ; Homeostasis ; Humans ; Ligands ; mammary ; Mammary Glands, Human - metabolism ; Models, Biological ; MUC1 ; Muc4 ; Mucin-1 - metabolism ; Mucin-4 ; Mucins - metabolism ; Receptor, ErbB-2 - metabolism ; Signal Transduction ; β-catenin</subject><ispartof>Journal of cellular biochemistry, 2005-12, Vol.96 (5), p.914-926</ispartof><rights>Copyright © 2005 Wiley‐Liss, Inc.</rights><rights>2005 Wiley-Liss, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3962-3a8a70aac4d3ffd6b5529c6d026eee706069cafbc58418f3bb1d0a62bb287b7d3</citedby><cites>FETCH-LOGICAL-c3962-3a8a70aac4d3ffd6b5529c6d026eee706069cafbc58418f3bb1d0a62bb287b7d3</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%2Fjcb.20612$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjcb.20612$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16167329$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carraway, Kermit L.</creatorcontrib><creatorcontrib>Ramsauer, Victoria P.</creatorcontrib><creatorcontrib>Carothers Carraway, Coralie A.</creatorcontrib><title>Glycoprotein contributions to mammary gland and mammary tumor structure and function: Roles of adherens junctions, ErbBs and membrane MUCs</title><title>Journal of cellular biochemistry</title><addtitle>J. Cell. Biochem</addtitle><description>Mammary function is dependent on its three‐dimensional organization, which is established and maintained by cell adhesive junctions linked through the membrane to the cell cytoskeleton. These junctions serve not only as structural elements, but also function as initiators and integrators of cell signals. In this review we discuss three types of glycoproteins whose interactions impinge on the function of mammary cell–cell junctions, cadherins, ErbB receptor tyrosine kinases and membrane mucins, as a microcosm of events regulating mammary cell behaviors. Actions of these components are integrated by the critical signaling element β‐catenin. When functioning properly, these glycoproteins, β‐catenin and associated signaling pathways mesh into a highly structured program for development and function of the gland. However, disruption or dysfunction of these glycoproteins or the signaling elements can lead to disorganization of the epithelia and ultimately to neoplasia. J. Cell. Biochem. © 2005 Wiley‐Liss, Inc.</description><subject>adherens junctions</subject><subject>Adherens Junctions - metabolism</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>beta Catenin - metabolism</subject><subject>Breast Neoplasms - metabolism</subject><subject>cadherin</subject><subject>Cell Adhesion</subject><subject>Cell Communication</subject><subject>Cell Membrane - metabolism</subject><subject>Epithelial Cells - metabolism</subject><subject>ErbB</subject><subject>Gap Junctions</subject><subject>Glycoproteins - metabolism</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Ligands</subject><subject>mammary</subject><subject>Mammary Glands, Human - metabolism</subject><subject>Models, Biological</subject><subject>MUC1</subject><subject>Muc4</subject><subject>Mucin-1 - metabolism</subject><subject>Mucin-4</subject><subject>Mucins - metabolism</subject><subject>Receptor, ErbB-2 - metabolism</subject><subject>Signal Transduction</subject><subject>β-catenin</subject><issn>0730-2312</issn><issn>1097-4644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM1O3DAURq0KVKaURV8AeYWERGb8k9gJOxjBtJSChKAsLdu5oRmSGGxHZV6hT02GDO2qC-tKvuce6fsQ-kLJlBLCZktrpowIyj6gCSWFTFKRpltoQiQnCeOU7aBPISwJIUXB2Ue0QwUVkrNigv4smpV1T95FqDtsXRd9bfpYuy7g6HCr21b7FX5odFfi9Xv_iX3rPA7R9zb2Ht52Vd_Z9ekxvnENBOwqrMtf4GGQLTe7cITPvDkNowxa43UH-MfdPHxG25VuAuxt5i66Oz-7nX9NLq8X3-Ynl4nlhWAJ17mWRGublryqSmGyjBVWlIQJAJBEEFFYXRmb5SnNK24MLYkWzBiWSyNLvosORu-Q-rmHEFVbBwvNEBFcH5TIpRBZIQfwcAStdyF4qNSTr9fhFSVqXbwaildvxQ_s_kbamxbKf-Sm6QGYjcDvuoHV_03qYn76rkzGizpEePl7of2jGpQyU_dXC_XzPmXp9-xKnfNXQsie4w</recordid><startdate>20051201</startdate><enddate>20051201</enddate><creator>Carraway, Kermit L.</creator><creator>Ramsauer, Victoria P.</creator><creator>Carothers Carraway, Coralie A.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</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>20051201</creationdate><title>Glycoprotein contributions to mammary gland and mammary tumor structure and function: Roles of adherens junctions, ErbBs and membrane MUCs</title><author>Carraway, Kermit L. ; Ramsauer, Victoria P. ; Carothers Carraway, Coralie A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3962-3a8a70aac4d3ffd6b5529c6d026eee706069cafbc58418f3bb1d0a62bb287b7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>adherens junctions</topic><topic>Adherens Junctions - metabolism</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>beta Catenin - metabolism</topic><topic>Breast Neoplasms - metabolism</topic><topic>cadherin</topic><topic>Cell Adhesion</topic><topic>Cell Communication</topic><topic>Cell Membrane - metabolism</topic><topic>Epithelial Cells - metabolism</topic><topic>ErbB</topic><topic>Gap Junctions</topic><topic>Glycoproteins - metabolism</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Ligands</topic><topic>mammary</topic><topic>Mammary Glands, Human - metabolism</topic><topic>Models, Biological</topic><topic>MUC1</topic><topic>Muc4</topic><topic>Mucin-1 - metabolism</topic><topic>Mucin-4</topic><topic>Mucins - metabolism</topic><topic>Receptor, ErbB-2 - metabolism</topic><topic>Signal Transduction</topic><topic>β-catenin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carraway, Kermit L.</creatorcontrib><creatorcontrib>Ramsauer, Victoria P.</creatorcontrib><creatorcontrib>Carothers Carraway, Coralie A.</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>Journal of cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carraway, Kermit L.</au><au>Ramsauer, Victoria P.</au><au>Carothers Carraway, Coralie A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycoprotein contributions to mammary gland and mammary tumor structure and function: Roles of adherens junctions, ErbBs and membrane MUCs</atitle><jtitle>Journal of cellular biochemistry</jtitle><addtitle>J. Cell. Biochem</addtitle><date>2005-12-01</date><risdate>2005</risdate><volume>96</volume><issue>5</issue><spage>914</spage><epage>926</epage><pages>914-926</pages><issn>0730-2312</issn><eissn>1097-4644</eissn><abstract>Mammary function is dependent on its three‐dimensional organization, which is established and maintained by cell adhesive junctions linked through the membrane to the cell cytoskeleton. These junctions serve not only as structural elements, but also function as initiators and integrators of cell signals. In this review we discuss three types of glycoproteins whose interactions impinge on the function of mammary cell–cell junctions, cadherins, ErbB receptor tyrosine kinases and membrane mucins, as a microcosm of events regulating mammary cell behaviors. Actions of these components are integrated by the critical signaling element β‐catenin. When functioning properly, these glycoproteins, β‐catenin and associated signaling pathways mesh into a highly structured program for development and function of the gland. However, disruption or dysfunction of these glycoproteins or the signaling elements can lead to disorganization of the epithelia and ultimately to neoplasia. J. Cell. Biochem. © 2005 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>16167329</pmid><doi>10.1002/jcb.20612</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | adherens junctions Adherens Junctions - metabolism Animals Apoptosis beta Catenin - metabolism Breast Neoplasms - metabolism cadherin Cell Adhesion Cell Communication Cell Membrane - metabolism Epithelial Cells - metabolism ErbB Gap Junctions Glycoproteins - metabolism Homeostasis Humans Ligands mammary Mammary Glands, Human - metabolism Models, Biological MUC1 Muc4 Mucin-1 - metabolism Mucin-4 Mucins - metabolism Receptor, ErbB-2 - metabolism Signal Transduction β-catenin |
| title | Glycoprotein contributions to mammary gland and mammary tumor structure and function: Roles of adherens junctions, ErbBs and membrane MUCs |
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