Membrane glycoprotein differences between normal lactating mammary tissue and the R3230 AC mammary tumor
Membrane glycoproteins have been studied in the normal lactating mammary gland and R3230 AC mammary tumor of the rat. Plasma membrane-enriched fractions were obtained from these tissues by discontinuous sucrose gradient centrifugation of a microsomal preparation from the tissue homogenates. The ligh...
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Veröffentlicht in: | Cancer research (Chicago, Ill.) Ill.), 1975-05, Vol.35 (5), p.1135-1140 |
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description | Membrane glycoproteins have been studied in the normal lactating mammary gland and R3230 AC mammary tumor of the rat. Plasma membrane-enriched fractions were obtained from these tissues by discontinuous sucrose gradient centrifugation of a microsomal preparation from the tissue homogenates. The lightest membrane fractions (F-1 and F-2) have the greatest enrichment of plasma membrane markers, with a 14- to 20-fold purification of 5'-nucleotidase and Na+-K+ -adenosine triphosphatase over the homogenate values in both tumor and normal tissues for F-1. Electron microscopy shows smooth membrane vesicles for these fractions. Polypeptide analysis by acrylamide gel electrophoresis shows essentially the same patterns for F-1 and F-2 and only relatively minor differences between membrane components of tumor and normal tissues. Glycoprotein analysis of the polyacrylamide gels by periodate-Schiff staining indicates more dramatic differences. Membrane Fraction F-1 from normal tissue contains two major glycoproteins, GP-II and GP-III, while Fractions F-2 and F-3 contain an additional glycoprotein, GP-I, with a higher apparent molecular weight. In the tumor, the component corresponding to GP-III is decreased or absent and a new component GP-IV is seen at a lower apparent molecular weight. |
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Plasma membrane-enriched fractions were obtained from these tissues by discontinuous sucrose gradient centrifugation of a microsomal preparation from the tissue homogenates. The lightest membrane fractions (F-1 and F-2) have the greatest enrichment of plasma membrane markers, with a 14- to 20-fold purification of 5'-nucleotidase and Na+-K+ -adenosine triphosphatase over the homogenate values in both tumor and normal tissues for F-1. Electron microscopy shows smooth membrane vesicles for these fractions. Polypeptide analysis by acrylamide gel electrophoresis shows essentially the same patterns for F-1 and F-2 and only relatively minor differences between membrane components of tumor and normal tissues. Glycoprotein analysis of the polyacrylamide gels by periodate-Schiff staining indicates more dramatic differences. Membrane Fraction F-1 from normal tissue contains two major glycoproteins, GP-II and GP-III, while Fractions F-2 and F-3 contain an additional glycoprotein, GP-I, with a higher apparent molecular weight. In the tumor, the component corresponding to GP-III is decreased or absent and a new component GP-IV is seen at a lower apparent molecular weight.</description><identifier>ISSN: 0008-5472</identifier><identifier>PMID: 123479</identifier><language>eng</language><publisher>United States</publisher><subject>Adenosine Triphosphatases - metabolism ; Animals ; Cell Fractionation - methods ; Cell Membrane - enzymology ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Electrophoresis, Polyacrylamide Gel ; Female ; Glycoproteins - metabolism ; Lactation ; Mammary Glands, Animal - metabolism ; Mammary Neoplasms, Experimental - metabolism ; Neoplasm Transplantation ; Nucleotidases - metabolism ; Pregnancy ; Rats</subject><ispartof>Cancer research (Chicago, Ill.), 1975-05, Vol.35 (5), p.1135-1140</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/123479$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shin, B C</creatorcontrib><creatorcontrib>Ebner, K E</creatorcontrib><creatorcontrib>Hudson, B G</creatorcontrib><creatorcontrib>Carraway, K L</creatorcontrib><title>Membrane glycoprotein differences between normal lactating mammary tissue and the R3230 AC mammary tumor</title><title>Cancer research (Chicago, Ill.)</title><addtitle>Cancer Res</addtitle><description>Membrane glycoproteins have been studied in the normal lactating mammary gland and R3230 AC mammary tumor of the rat. Plasma membrane-enriched fractions were obtained from these tissues by discontinuous sucrose gradient centrifugation of a microsomal preparation from the tissue homogenates. The lightest membrane fractions (F-1 and F-2) have the greatest enrichment of plasma membrane markers, with a 14- to 20-fold purification of 5'-nucleotidase and Na+-K+ -adenosine triphosphatase over the homogenate values in both tumor and normal tissues for F-1. Electron microscopy shows smooth membrane vesicles for these fractions. Polypeptide analysis by acrylamide gel electrophoresis shows essentially the same patterns for F-1 and F-2 and only relatively minor differences between membrane components of tumor and normal tissues. Glycoprotein analysis of the polyacrylamide gels by periodate-Schiff staining indicates more dramatic differences. Membrane Fraction F-1 from normal tissue contains two major glycoproteins, GP-II and GP-III, while Fractions F-2 and F-3 contain an additional glycoprotein, GP-I, with a higher apparent molecular weight. In the tumor, the component corresponding to GP-III is decreased or absent and a new component GP-IV is seen at a lower apparent molecular weight.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Animals</subject><subject>Cell Fractionation - methods</subject><subject>Cell Membrane - enzymology</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - ultrastructure</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Glycoproteins - metabolism</subject><subject>Lactation</subject><subject>Mammary Glands, Animal - metabolism</subject><subject>Mammary Neoplasms, Experimental - metabolism</subject><subject>Neoplasm Transplantation</subject><subject>Nucleotidases - metabolism</subject><subject>Pregnancy</subject><subject>Rats</subject><issn>0008-5472</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFUEtLxDAYzMHXuvoPPOTkrZDm0abHpfiCFUH0XL4mX7eVJl2TFNl_b2UXPA3DDMPMnJEVY0xnSpb8ilzH-LVQlTN1SS5yLmRZrUj_iq4N4JHuxoOZ9mFKOHhqh67DgN5gpC2mH0RP_RQcjHQEkyANfkcdOAfhQNMQ44wUvKWpR_ouuGB0U__rs5vCDTnvYIx4e8I1-Xx8-Kifs-3b00u92WY9FzplJbcKVK60qXIri4Ipi12pTIGIvBWVBTC2k4UEK3JpQAlg0Bo0nVZGQivW5P6Yu0z5njGmxg3R4DguG6c5NpqXpdC6WIx3J-PcOrTNPgx_bZvjM-IX9BBglw</recordid><startdate>197505</startdate><enddate>197505</enddate><creator>Shin, B C</creator><creator>Ebner, K E</creator><creator>Hudson, B G</creator><creator>Carraway, K L</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>197505</creationdate><title>Membrane glycoprotein differences between normal lactating mammary tissue and the R3230 AC mammary tumor</title><author>Shin, B C ; Ebner, K E ; Hudson, B G ; Carraway, K L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h238t-72d5a5158c91d46605def75c6eee2b39daacdf464ad314ca53a0abcecf85c4ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>Animals</topic><topic>Cell Fractionation - methods</topic><topic>Cell Membrane - enzymology</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - ultrastructure</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Glycoproteins - metabolism</topic><topic>Lactation</topic><topic>Mammary Glands, Animal - metabolism</topic><topic>Mammary Neoplasms, Experimental - metabolism</topic><topic>Neoplasm Transplantation</topic><topic>Nucleotidases - metabolism</topic><topic>Pregnancy</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shin, B C</creatorcontrib><creatorcontrib>Ebner, K E</creatorcontrib><creatorcontrib>Hudson, B G</creatorcontrib><creatorcontrib>Carraway, K L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Cancer research (Chicago, Ill.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shin, B C</au><au>Ebner, K E</au><au>Hudson, B G</au><au>Carraway, K L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane glycoprotein differences between normal lactating mammary tissue and the R3230 AC mammary tumor</atitle><jtitle>Cancer research (Chicago, Ill.)</jtitle><addtitle>Cancer Res</addtitle><date>1975-05</date><risdate>1975</risdate><volume>35</volume><issue>5</issue><spage>1135</spage><epage>1140</epage><pages>1135-1140</pages><issn>0008-5472</issn><abstract>Membrane glycoproteins have been studied in the normal lactating mammary gland and R3230 AC mammary tumor of the rat. Plasma membrane-enriched fractions were obtained from these tissues by discontinuous sucrose gradient centrifugation of a microsomal preparation from the tissue homogenates. The lightest membrane fractions (F-1 and F-2) have the greatest enrichment of plasma membrane markers, with a 14- to 20-fold purification of 5'-nucleotidase and Na+-K+ -adenosine triphosphatase over the homogenate values in both tumor and normal tissues for F-1. Electron microscopy shows smooth membrane vesicles for these fractions. Polypeptide analysis by acrylamide gel electrophoresis shows essentially the same patterns for F-1 and F-2 and only relatively minor differences between membrane components of tumor and normal tissues. Glycoprotein analysis of the polyacrylamide gels by periodate-Schiff staining indicates more dramatic differences. Membrane Fraction F-1 from normal tissue contains two major glycoproteins, GP-II and GP-III, while Fractions F-2 and F-3 contain an additional glycoprotein, GP-I, with a higher apparent molecular weight. In the tumor, the component corresponding to GP-III is decreased or absent and a new component GP-IV is seen at a lower apparent molecular weight.</abstract><cop>United States</cop><pmid>123479</pmid><tpages>6</tpages></addata></record> |
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subjects | Adenosine Triphosphatases - metabolism Animals Cell Fractionation - methods Cell Membrane - enzymology Cell Membrane - metabolism Cell Membrane - ultrastructure Electrophoresis, Polyacrylamide Gel Female Glycoproteins - metabolism Lactation Mammary Glands, Animal - metabolism Mammary Neoplasms, Experimental - metabolism Neoplasm Transplantation Nucleotidases - metabolism Pregnancy Rats |
title | Membrane glycoprotein differences between normal lactating mammary tissue and the R3230 AC mammary tumor |
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