Proteins of the apical and basal plasma membranes of the human placental syncytiotrophoblast: Immunochemical and electrophoretic studies
Proteins of the basal and microvillous plasma membranes of the human placental syncytiotrophoblast were compared to elucidate the basis for structural and functional differences in the two membranes. Among the proteins common to both membranes were actin, alkaline phosphatase, albumin, transferrin,...
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| Veröffentlicht in: | Placenta (Eastbourne) 1987-11, Vol.8 (6), p.591-608 |
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| creator | Vanderpuye, Oluseyi A. Smith, Carl H. |
| description | Proteins of the basal and microvillous plasma membranes of the human placental syncytiotrophoblast were compared to elucidate the basis for structural and functional differences in the two membranes. Among the proteins common to both membranes were actin, alkaline phosphatase, albumin, transferrin, immunoglobulin G, proteins of
M
r 35 000, 55 000 and 180 000 and five immunochemically detected proteins. Each membrane also contained unique proteins. Major microvillous cytoskeleton proteins of
M
r 68 000, 80 000 and 105 000 (α-actinin) were lacking or absent from basal membrane cytoskeletons which instead contained unique proteins of
M
r 14 000, 16 000 220 000 and 240 000. In addition, immunochemical analyses revealed four glycoprotein antigens unique to microvillous membrane and five unique to basal membrane. Fibronectin was also found to be exclusive to basal membrane. The differences in membrane-associated cytoskeletal proteins correlated with the different organization of actin microfilaments at the two membranes. The protein antigens unique to each of the two membranes provided further evidence for the polarization of membrane proteins and functions in the syncytium. |
| doi_str_mv | 10.1016/0143-4004(87)90030-0 |
| format | Article |
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M
r 35 000, 55 000 and 180 000 and five immunochemically detected proteins. Each membrane also contained unique proteins. Major microvillous cytoskeleton proteins of
M
r 68 000, 80 000 and 105 000 (α-actinin) were lacking or absent from basal membrane cytoskeletons which instead contained unique proteins of
M
r 14 000, 16 000 220 000 and 240 000. In addition, immunochemical analyses revealed four glycoprotein antigens unique to microvillous membrane and five unique to basal membrane. Fibronectin was also found to be exclusive to basal membrane. The differences in membrane-associated cytoskeletal proteins correlated with the different organization of actin microfilaments at the two membranes. The protein antigens unique to each of the two membranes provided further evidence for the polarization of membrane proteins and functions in the syncytium.</description><identifier>ISSN: 0143-4004</identifier><identifier>EISSN: 1532-3102</identifier><identifier>DOI: 10.1016/0143-4004(87)90030-0</identifier><identifier>PMID: 3438256</identifier><identifier>CODEN: PLACDF</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Biological and medical sciences ; Cell Membrane - analysis ; Chorionic Villi - analysis ; Electrophoresis, Polyacrylamide Gel ; Female ; Fundamental and applied biological sciences. Psychology ; Humans ; Immunoelectrophoresis, Two-Dimensional ; Membrane Glycoproteins - analysis ; Microvilli - analysis ; Mother. Fetoplacental unit. Mammary gland. Milk ; Pregnancy ; Pregnancy Proteins - analysis ; Pregnancy. Parturition. Lactation ; Trophoblasts - analysis ; Vertebrates: reproduction</subject><ispartof>Placenta (Eastbourne), 1987-11, Vol.8 (6), p.591-608</ispartof><rights>1987</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-49f44d512255b464f174252f6581d0b5b5cfaaa3f266f978bdb974462647a1a93</citedby><cites>FETCH-LOGICAL-c386t-49f44d512255b464f174252f6581d0b5b5cfaaa3f266f978bdb974462647a1a93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0143-4004(87)90030-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7045505$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3438256$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vanderpuye, Oluseyi A.</creatorcontrib><creatorcontrib>Smith, Carl H.</creatorcontrib><title>Proteins of the apical and basal plasma membranes of the human placental syncytiotrophoblast: Immunochemical and electrophoretic studies</title><title>Placenta (Eastbourne)</title><addtitle>Placenta</addtitle><description>Proteins of the basal and microvillous plasma membranes of the human placental syncytiotrophoblast were compared to elucidate the basis for structural and functional differences in the two membranes. Among the proteins common to both membranes were actin, alkaline phosphatase, albumin, transferrin, immunoglobulin G, proteins of
M
r 35 000, 55 000 and 180 000 and five immunochemically detected proteins. Each membrane also contained unique proteins. Major microvillous cytoskeleton proteins of
M
r 68 000, 80 000 and 105 000 (α-actinin) were lacking or absent from basal membrane cytoskeletons which instead contained unique proteins of
M
r 14 000, 16 000 220 000 and 240 000. In addition, immunochemical analyses revealed four glycoprotein antigens unique to microvillous membrane and five unique to basal membrane. Fibronectin was also found to be exclusive to basal membrane. The differences in membrane-associated cytoskeletal proteins correlated with the different organization of actin microfilaments at the two membranes. The protein antigens unique to each of the two membranes provided further evidence for the polarization of membrane proteins and functions in the syncytium.</description><subject>Biological and medical sciences</subject><subject>Cell Membrane - analysis</subject><subject>Chorionic Villi - analysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Immunoelectrophoresis, Two-Dimensional</subject><subject>Membrane Glycoproteins - analysis</subject><subject>Microvilli - analysis</subject><subject>Mother. Fetoplacental unit. Mammary gland. Milk</subject><subject>Pregnancy</subject><subject>Pregnancy Proteins - analysis</subject><subject>Pregnancy. Parturition. Lactation</subject><subject>Trophoblasts - analysis</subject><subject>Vertebrates: reproduction</subject><issn>0143-4004</issn><issn>1532-3102</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcuKFDEUhoM4jO3oGyjUQkQXNeaeqlkIMngZGBgXug6p1AkdqVTKJCX0G8xjm7abWrpK4Hz_T_IdhF4RfE0wkR8w4azlGPN3nXrfY8xwi5-gHRGMtoxg-hTtNuQZep7zL4xxzwm9RJeMs44KuUOP31Ms4OfcRNeUPTRm8dZMjZnHZjC53pbJ5GCaAGFIZoYN3K_BzMephblULh9meyg-lhSXfRxqqtw0dyGsc7R7CFsrTGBPTILibZPLOnrIL9CFM1OGl-fzCv388vnH7bf2_uHr3e2n-9ayTpaW947zURBKhRi45I4oTgV1UnRkxIMYhHXGGOaolK5X3TAOveJcUsmVIaZnV-jtqXdJ8fcKuejgs4Vpqn-La9ZK9VwwxSvIT6BNMecETi_JB5MOmmB9XIA-2tVHu7pT-t8CNK6x1-f-dQgwbqGz8Tp_c56bXJW46tT6vGEKcyGwqNjHEwbVxR8PSWfrYbYw-lT96TH6_7_jL8BWo4U</recordid><startdate>19871101</startdate><enddate>19871101</enddate><creator>Vanderpuye, Oluseyi A.</creator><creator>Smith, Carl H.</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>19871101</creationdate><title>Proteins of the apical and basal plasma membranes of the human placental syncytiotrophoblast: Immunochemical and electrophoretic studies</title><author>Vanderpuye, Oluseyi A. ; Smith, Carl H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-49f44d512255b464f174252f6581d0b5b5cfaaa3f266f978bdb974462647a1a93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Biological and medical sciences</topic><topic>Cell Membrane - analysis</topic><topic>Chorionic Villi - analysis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Immunoelectrophoresis, Two-Dimensional</topic><topic>Membrane Glycoproteins - analysis</topic><topic>Microvilli - analysis</topic><topic>Mother. Fetoplacental unit. Mammary gland. Milk</topic><topic>Pregnancy</topic><topic>Pregnancy Proteins - analysis</topic><topic>Pregnancy. Parturition. Lactation</topic><topic>Trophoblasts - analysis</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vanderpuye, Oluseyi A.</creatorcontrib><creatorcontrib>Smith, Carl H.</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>Vanderpuye, Oluseyi A.</au><au>Smith, Carl H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteins of the apical and basal plasma membranes of the human placental syncytiotrophoblast: Immunochemical and electrophoretic studies</atitle><jtitle>Placenta (Eastbourne)</jtitle><addtitle>Placenta</addtitle><date>1987-11-01</date><risdate>1987</risdate><volume>8</volume><issue>6</issue><spage>591</spage><epage>608</epage><pages>591-608</pages><issn>0143-4004</issn><eissn>1532-3102</eissn><coden>PLACDF</coden><abstract>Proteins of the basal and microvillous plasma membranes of the human placental syncytiotrophoblast were compared to elucidate the basis for structural and functional differences in the two membranes. Among the proteins common to both membranes were actin, alkaline phosphatase, albumin, transferrin, immunoglobulin G, proteins of
M
r 35 000, 55 000 and 180 000 and five immunochemically detected proteins. Each membrane also contained unique proteins. Major microvillous cytoskeleton proteins of
M
r 68 000, 80 000 and 105 000 (α-actinin) were lacking or absent from basal membrane cytoskeletons which instead contained unique proteins of
M
r 14 000, 16 000 220 000 and 240 000. In addition, immunochemical analyses revealed four glycoprotein antigens unique to microvillous membrane and five unique to basal membrane. Fibronectin was also found to be exclusive to basal membrane. The differences in membrane-associated cytoskeletal proteins correlated with the different organization of actin microfilaments at the two membranes. The protein antigens unique to each of the two membranes provided further evidence for the polarization of membrane proteins and functions in the syncytium.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>3438256</pmid><doi>10.1016/0143-4004(87)90030-0</doi><tpages>18</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0143-4004 |
| ispartof | Placenta (Eastbourne), 1987-11, Vol.8 (6), p.591-608 |
| issn | 0143-4004 1532-3102 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Biological and medical sciences Cell Membrane - analysis Chorionic Villi - analysis Electrophoresis, Polyacrylamide Gel Female Fundamental and applied biological sciences. Psychology Humans Immunoelectrophoresis, Two-Dimensional Membrane Glycoproteins - analysis Microvilli - analysis Mother. Fetoplacental unit. Mammary gland. Milk Pregnancy Pregnancy Proteins - analysis Pregnancy. Parturition. Lactation Trophoblasts - analysis Vertebrates: reproduction |
| title | Proteins of the apical and basal plasma membranes of the human placental syncytiotrophoblast: Immunochemical and electrophoretic studies |
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