Association of PAT Proteins with Lipid Storage Droplets in Term Fetal Membranes
Abstract As depots for neutral lipids, lipid storage droplets (LDs) accumulate with advancing gestation within the fetal membranes. Little is currently known about the proteins associated with the LDs of these cells. The PAT family [ p erilipin, a dipose differentiation-related protein (ADRP), and t...
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Veröffentlicht in: | Placenta (Eastbourne) 2007-05, Vol.28 (5), p.465-476 |
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description | Abstract As depots for neutral lipids, lipid storage droplets (LDs) accumulate with advancing gestation within the fetal membranes. Little is currently known about the proteins associated with the LDs of these cells. The PAT family [ p erilipin, a dipose differentiation-related protein (ADRP), and t ail-interacting protein of 47 kilodaltons (TIP47)] represents a unique group of proteins thought to contribute to LD formation and function. We examined the association of each of the PAT proteins with LDs of term fetal membranes. We found that large LDs of amnion epithelial cells were reactive for neutral lipid stains and simultaneously encoated with ADRP and TIP47, but not perilipin. Within the remaining cell types, LDs were frequently co-labeled with antibodies recognizing ADRP and TIP47; however, in cells harboring only small LDs, the majority of TIP47 labeling was cytoplasmic. Structures labeled with perilipin antibodies were present only in chorion laeve trophoblasts. Gene and protein expression analyses suggested this to be a small molecular weight perilipin isoform, such as that seen in steroidogenic cells. We conclude that LDs are heterogeneous among differing cell types of the fetal membranes. Subclassification of LDs based on associated proteins suggests that these organelles may serve specialized functions within individual cells. |
doi_str_mv | 10.1016/j.placenta.2006.06.009 |
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Little is currently known about the proteins associated with the LDs of these cells. The PAT family [ p erilipin, a dipose differentiation-related protein (ADRP), and t ail-interacting protein of 47 kilodaltons (TIP47)] represents a unique group of proteins thought to contribute to LD formation and function. We examined the association of each of the PAT proteins with LDs of term fetal membranes. We found that large LDs of amnion epithelial cells were reactive for neutral lipid stains and simultaneously encoated with ADRP and TIP47, but not perilipin. Within the remaining cell types, LDs were frequently co-labeled with antibodies recognizing ADRP and TIP47; however, in cells harboring only small LDs, the majority of TIP47 labeling was cytoplasmic. Structures labeled with perilipin antibodies were present only in chorion laeve trophoblasts. Gene and protein expression analyses suggested this to be a small molecular weight perilipin isoform, such as that seen in steroidogenic cells. We conclude that LDs are heterogeneous among differing cell types of the fetal membranes. Subclassification of LDs based on associated proteins suggests that these organelles may serve specialized functions within individual cells.</description><identifier>ISSN: 0143-4004</identifier><identifier>EISSN: 1532-3102</identifier><identifier>DOI: 10.1016/j.placenta.2006.06.009</identifier><identifier>PMID: 16965813</identifier><identifier>CODEN: PLACDF</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>3T3 Cells ; Adipose differentiation-related protein ; Amino Acid Transport Systems, Neutral - genetics ; Amnion - metabolism ; Animals ; Biological and medical sciences ; DNA Primers ; Embryology: invertebrates and vertebrates. Teratology ; Extraembryonic Membranes - metabolism ; Female ; Fundamental and applied biological sciences. Psychology ; Goats ; Guinea Pigs ; Internal Medicine ; Lipid storage droplets ; Lipids - physiology ; Mice ; Obstetrics and Gynecology ; Perilipin ; Placental membranes ; Pregnancy ; Rabbits ; Reverse Transcriptase Polymerase Chain Reaction ; Symporters - genetics ; Tail-interacting protein of 47 kilodaltons</subject><ispartof>Placenta (Eastbourne), 2007-05, Vol.28 (5), p.465-476</ispartof><rights>Elsevier Ltd</rights><rights>2006 Elsevier Ltd</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-b5d06317e3be6ec825a1c3fe9a3a65c5dce098d0987c557b202c3ea19a261a333</citedby><cites>FETCH-LOGICAL-c451t-b5d06317e3be6ec825a1c3fe9a3a65c5dce098d0987c557b202c3ea19a261a333</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0143400406001639$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18742300$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16965813$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ackerman, W.E</creatorcontrib><creatorcontrib>Robinson, J.M</creatorcontrib><creatorcontrib>Kniss, D.A</creatorcontrib><title>Association of PAT Proteins with Lipid Storage Droplets in Term Fetal Membranes</title><title>Placenta (Eastbourne)</title><addtitle>Placenta</addtitle><description>Abstract As depots for neutral lipids, lipid storage droplets (LDs) accumulate with advancing gestation within the fetal membranes. Little is currently known about the proteins associated with the LDs of these cells. The PAT family [ p erilipin, a dipose differentiation-related protein (ADRP), and t ail-interacting protein of 47 kilodaltons (TIP47)] represents a unique group of proteins thought to contribute to LD formation and function. We examined the association of each of the PAT proteins with LDs of term fetal membranes. We found that large LDs of amnion epithelial cells were reactive for neutral lipid stains and simultaneously encoated with ADRP and TIP47, but not perilipin. Within the remaining cell types, LDs were frequently co-labeled with antibodies recognizing ADRP and TIP47; however, in cells harboring only small LDs, the majority of TIP47 labeling was cytoplasmic. Structures labeled with perilipin antibodies were present only in chorion laeve trophoblasts. Gene and protein expression analyses suggested this to be a small molecular weight perilipin isoform, such as that seen in steroidogenic cells. We conclude that LDs are heterogeneous among differing cell types of the fetal membranes. Subclassification of LDs based on associated proteins suggests that these organelles may serve specialized functions within individual cells.</description><subject>3T3 Cells</subject><subject>Adipose differentiation-related protein</subject><subject>Amino Acid Transport Systems, Neutral - genetics</subject><subject>Amnion - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>DNA Primers</subject><subject>Embryology: invertebrates and vertebrates. Teratology</subject><subject>Extraembryonic Membranes - metabolism</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Goats</subject><subject>Guinea Pigs</subject><subject>Internal Medicine</subject><subject>Lipid storage droplets</subject><subject>Lipids - physiology</subject><subject>Mice</subject><subject>Obstetrics and Gynecology</subject><subject>Perilipin</subject><subject>Placental membranes</subject><subject>Pregnancy</subject><subject>Rabbits</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Symporters - genetics</subject><subject>Tail-interacting protein of 47 kilodaltons</subject><issn>0143-4004</issn><issn>1532-3102</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQQC0EokvhL1S-wC3bsR07yQWxaikgLWqlLmfLcSbgJYmD7aXqv8fRLqrEBWksX958vSHkgsGaAVOX-_U8GItTMmsOoNZLQPOMrJgUvBAM-HOyAlaKogQoz8irGPeQiZLxl-SMqUbJmokVud3E6K0zyfmJ-p7ebXb0LviEbor0waUfdOtm19H75IP5jvQ6-HnAFKmb6A7DSG8wmYF-xbENZsL4mrzozRDxzek_J99uPu6uPhfb209frjbbwpaSpaKVHSjBKhQtKrQ1l4ZZ0WNjhFHSys4iNHWXX2WlrFoO3Ao0rDFcMSOEOCfvjnXn4H8dMCY9umhxGPIQ_hB1BSUra8EzqI6gDT7GgL2egxtNeNQM9KJS7_VflXpRqZeAJidenDoc2hG7p7STuwy8PQEmWjP0eX_r4hNXVyUXAJn7cOQw-_jtMOhoHU4WOxfQJt159_9Z3v9Twg5ucrnrT3zEuPeHMGXbmunINej75fDL3UFBrioa8QfJT6k4</recordid><startdate>20070501</startdate><enddate>20070501</enddate><creator>Ackerman, W.E</creator><creator>Robinson, J.M</creator><creator>Kniss, D.A</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>20070501</creationdate><title>Association of PAT Proteins with Lipid Storage Droplets in Term Fetal Membranes</title><author>Ackerman, W.E ; Robinson, J.M ; Kniss, D.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-b5d06317e3be6ec825a1c3fe9a3a65c5dce098d0987c557b202c3ea19a261a333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>3T3 Cells</topic><topic>Adipose differentiation-related protein</topic><topic>Amino Acid Transport Systems, Neutral - genetics</topic><topic>Amnion - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>DNA Primers</topic><topic>Embryology: invertebrates and vertebrates. Teratology</topic><topic>Extraembryonic Membranes - metabolism</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Goats</topic><topic>Guinea Pigs</topic><topic>Internal Medicine</topic><topic>Lipid storage droplets</topic><topic>Lipids - physiology</topic><topic>Mice</topic><topic>Obstetrics and Gynecology</topic><topic>Perilipin</topic><topic>Placental membranes</topic><topic>Pregnancy</topic><topic>Rabbits</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Symporters - genetics</topic><topic>Tail-interacting protein of 47 kilodaltons</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ackerman, W.E</creatorcontrib><creatorcontrib>Robinson, J.M</creatorcontrib><creatorcontrib>Kniss, D.A</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>MEDLINE - Academic</collection><jtitle>Placenta (Eastbourne)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ackerman, W.E</au><au>Robinson, J.M</au><au>Kniss, D.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Association of PAT Proteins with Lipid Storage Droplets in Term Fetal Membranes</atitle><jtitle>Placenta (Eastbourne)</jtitle><addtitle>Placenta</addtitle><date>2007-05-01</date><risdate>2007</risdate><volume>28</volume><issue>5</issue><spage>465</spage><epage>476</epage><pages>465-476</pages><issn>0143-4004</issn><eissn>1532-3102</eissn><coden>PLACDF</coden><abstract>Abstract As depots for neutral lipids, lipid storage droplets (LDs) accumulate with advancing gestation within the fetal membranes. Little is currently known about the proteins associated with the LDs of these cells. The PAT family [ p erilipin, a dipose differentiation-related protein (ADRP), and t ail-interacting protein of 47 kilodaltons (TIP47)] represents a unique group of proteins thought to contribute to LD formation and function. We examined the association of each of the PAT proteins with LDs of term fetal membranes. We found that large LDs of amnion epithelial cells were reactive for neutral lipid stains and simultaneously encoated with ADRP and TIP47, but not perilipin. Within the remaining cell types, LDs were frequently co-labeled with antibodies recognizing ADRP and TIP47; however, in cells harboring only small LDs, the majority of TIP47 labeling was cytoplasmic. Structures labeled with perilipin antibodies were present only in chorion laeve trophoblasts. Gene and protein expression analyses suggested this to be a small molecular weight perilipin isoform, such as that seen in steroidogenic cells. We conclude that LDs are heterogeneous among differing cell types of the fetal membranes. Subclassification of LDs based on associated proteins suggests that these organelles may serve specialized functions within individual cells.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>16965813</pmid><doi>10.1016/j.placenta.2006.06.009</doi><tpages>12</tpages></addata></record> |
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subjects | 3T3 Cells Adipose differentiation-related protein Amino Acid Transport Systems, Neutral - genetics Amnion - metabolism Animals Biological and medical sciences DNA Primers Embryology: invertebrates and vertebrates. Teratology Extraembryonic Membranes - metabolism Female Fundamental and applied biological sciences. Psychology Goats Guinea Pigs Internal Medicine Lipid storage droplets Lipids - physiology Mice Obstetrics and Gynecology Perilipin Placental membranes Pregnancy Rabbits Reverse Transcriptase Polymerase Chain Reaction Symporters - genetics Tail-interacting protein of 47 kilodaltons |
title | Association of PAT Proteins with Lipid Storage Droplets in Term Fetal Membranes |
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