Characterization of a microvillous membrane preparation from human placental syncytiotrophoblast: A morphologic, biochemical, and physiologic study
The syncytiotrophoblast microvillous membrane must play a vital role in many essential functions of the placenta. In order to better understand the functional characteristics of this membrane, we have investigated an isolated membrane preparation by a variety of techniques. Electron microscopic obse...
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| Veröffentlicht in: | American journal of obstetrics and gynecology 1977-05, Vol.128 (2), p.190-196 |
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| container_title | American journal of obstetrics and gynecology |
| container_volume | 128 |
| creator | Smith, Carl H. Nelson, D. Michael King, Barry F. Donohue, Thomas M. Ruzycki, Stephen M. Kelley, Lucky K. |
| description | The syncytiotrophoblast microvillous membrane must play a vital role in many essential functions of the placenta. In order to better understand the functional characteristics of this membrane, we have investigated an isolated membrane preparation by a variety of techniques. Electron microscopic observations showed membranous structures similar to microvilli of intact placental villi in size, shape, and microfilamentous content. Similarities in colloidal iron staining and transferrin localization were also shown. The preparation was enriched in enzymes characteristic of surface membranes and diminished in enzymes characteristic of intracellular organelles. Sialic acid content was also increased. SDS gel electrophoresis revealed the presence of a 45,000 molecular weight band, which may be actin. The preparation transported serine, glycine, and α-aminoisobutyric acid by a temperature-dependent, saturable process. |
| doi_str_mv | 10.1016/0002-9378(77)90686-X |
| format | Article |
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Michael ; King, Barry F. ; Donohue, Thomas M. ; Ruzycki, Stephen M. ; Kelley, Lucky K.</creator><creatorcontrib>Smith, Carl H. ; Nelson, D. Michael ; King, Barry F. ; Donohue, Thomas M. ; Ruzycki, Stephen M. ; Kelley, Lucky K.</creatorcontrib><description>The syncytiotrophoblast microvillous membrane must play a vital role in many essential functions of the placenta. In order to better understand the functional characteristics of this membrane, we have investigated an isolated membrane preparation by a variety of techniques. Electron microscopic observations showed membranous structures similar to microvilli of intact placental villi in size, shape, and microfilamentous content. Similarities in colloidal iron staining and transferrin localization were also shown. The preparation was enriched in enzymes characteristic of surface membranes and diminished in enzymes characteristic of intracellular organelles. Sialic acid content was also increased. SDS gel electrophoresis revealed the presence of a 45,000 molecular weight band, which may be actin. The preparation transported serine, glycine, and α-aminoisobutyric acid by a temperature-dependent, saturable process.</description><identifier>ISSN: 0002-9378</identifier><identifier>EISSN: 1097-6868</identifier><identifier>DOI: 10.1016/0002-9378(77)90686-X</identifier><identifier>PMID: 855869</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Alkaline Phosphatase - metabolism ; Amino Acids - metabolism ; Electrophoresis, Polyacrylamide Gel ; Female ; Histocytochemistry ; Humans ; Membranes - ultrastructure ; Nucleotidases - metabolism ; Pregnancy ; Sialic Acids - metabolism ; Trophoblasts - enzymology ; Trophoblasts - metabolism ; Trophoblasts - physiology ; Trophoblasts - ultrastructure</subject><ispartof>American journal of obstetrics and gynecology, 1977-05, Vol.128 (2), p.190-196</ispartof><rights>1977 C. V. 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Similarities in colloidal iron staining and transferrin localization were also shown. The preparation was enriched in enzymes characteristic of surface membranes and diminished in enzymes characteristic of intracellular organelles. Sialic acid content was also increased. SDS gel electrophoresis revealed the presence of a 45,000 molecular weight band, which may be actin. The preparation transported serine, glycine, and α-aminoisobutyric acid by a temperature-dependent, saturable process.</description><subject>Alkaline Phosphatase - metabolism</subject><subject>Amino Acids - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Histocytochemistry</subject><subject>Humans</subject><subject>Membranes - ultrastructure</subject><subject>Nucleotidases - metabolism</subject><subject>Pregnancy</subject><subject>Sialic Acids - metabolism</subject><subject>Trophoblasts - enzymology</subject><subject>Trophoblasts - metabolism</subject><subject>Trophoblasts - physiology</subject><subject>Trophoblasts - ultrastructure</subject><issn>0002-9378</issn><issn>1097-6868</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9Uctq3TAUFKWv27R_kIVWpYW4lWTZkrMohEtfEOimheyELB_XKpLlSnLA_Y3-cHXjkGVXh2HmzGHmIHROyTtKaPueEMKqrhbyjRBvO9LKtrp5hA6UdKIqQD5GhwfJc_QipV8nyDr2DD2VTSPb7oD-HicdtckQ7R-dbZhxGLHG3poYbq1zYU3Yg--jngEvEZaivpONMXg8rV7PeHHawJy1w2mbzVboHMMyhd7plC_xFfYhFujCT2sucG-DmaAc0O4C63nAy7Qlu7M45XXYXqIno3YJXt3PM_Tj08fvxy_V9bfPX49X15XhjOWqEbWAhrdDDz1toNacamNaTkZmtCG91FR23WBGYIxAzSUVLaej4bTnTJq2PkOvd98lht8rpKy8TQacK1lLbiVrKQWTXRHyXVhKSSnCqJZovY6bokSdXqFOxapTz0oIdfcKdVPWzu_9197D8LC0d1_oDzsNJeOthaiSsTAbGGwEk9UQ7P_9_wFJoJ01</recordid><startdate>19770515</startdate><enddate>19770515</enddate><creator>Smith, Carl H.</creator><creator>Nelson, D. 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Michael ; King, Barry F. ; Donohue, Thomas M. ; Ruzycki, Stephen M. ; Kelley, Lucky K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-5737e546dbeb15e3a41acc640f2cac0b8a1899dcfe220e34817641fc41b428c63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Alkaline Phosphatase - metabolism</topic><topic>Amino Acids - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Histocytochemistry</topic><topic>Humans</topic><topic>Membranes - ultrastructure</topic><topic>Nucleotidases - metabolism</topic><topic>Pregnancy</topic><topic>Sialic Acids - metabolism</topic><topic>Trophoblasts - enzymology</topic><topic>Trophoblasts - metabolism</topic><topic>Trophoblasts - physiology</topic><topic>Trophoblasts - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smith, Carl H.</creatorcontrib><creatorcontrib>Nelson, D. 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Electron microscopic observations showed membranous structures similar to microvilli of intact placental villi in size, shape, and microfilamentous content. Similarities in colloidal iron staining and transferrin localization were also shown. The preparation was enriched in enzymes characteristic of surface membranes and diminished in enzymes characteristic of intracellular organelles. Sialic acid content was also increased. SDS gel electrophoresis revealed the presence of a 45,000 molecular weight band, which may be actin. The preparation transported serine, glycine, and α-aminoisobutyric acid by a temperature-dependent, saturable process.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>855869</pmid><doi>10.1016/0002-9378(77)90686-X</doi><tpages>7</tpages></addata></record> |
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| ispartof | American journal of obstetrics and gynecology, 1977-05, Vol.128 (2), p.190-196 |
| issn | 0002-9378 1097-6868 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Alkaline Phosphatase - metabolism Amino Acids - metabolism Electrophoresis, Polyacrylamide Gel Female Histocytochemistry Humans Membranes - ultrastructure Nucleotidases - metabolism Pregnancy Sialic Acids - metabolism Trophoblasts - enzymology Trophoblasts - metabolism Trophoblasts - physiology Trophoblasts - ultrastructure |
| title | Characterization of a microvillous membrane preparation from human placental syncytiotrophoblast: A morphologic, biochemical, and physiologic study |
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