cis-Golgi resident proteins and O-glycans are abnormally compartmentalized in the RER of colon cancer cells
Neoplastic transformation is commonly associated with altered glycosylation of proteins and lipids. To understand the basis for altered mucin glycosylation, we have examined the distribution of RER markers, a cis-Golgi resident protein, and the GalNAc alpha-O-Ser/Thr epitope (Tn) in human colon canc...
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| Veröffentlicht in: | Journal of cell science 1993-07, Vol.105 (3), p.819-830 |
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| creator | EGEA, G FRANCI, C GAMBUS, G LESUFFLEUR, T ZWEIBAUM, A REAL, F. X |
| description | Neoplastic transformation is commonly associated with altered glycosylation of proteins and lipids. To understand the basis for altered mucin glycosylation, we have examined the distribution of RER markers, a cis-Golgi resident protein, and the GalNAc alpha-O-Ser/Thr epitope (Tn) in human colon cancer cells and in normal colon. In cultured mucin-producing colon cancer cells, Gal-NAc alpha-O-Ser/Thr was found in mucin droplets and in RER cisternae. In addition, the Golgi apparatus was disorganized in a proportion of cells and a 130 kDa cis-Golgi resident protein was also abnormally redistributed to the RER. The distribution of the MUC2 intestinal apomucin, protein disulphide isomerase, Gal-NAc alpha-O-Ser/Thr, and the 130 kDa cis-Golgi resident protein was analysed in normal colon and in colon cancer tissues. In normal colon, MUC2 apomucin and protein disulphide isomerase were located in the RER, whereas the cis-Golgi resident protein and GalNAc alpha-O-Ser/Thr were detected only in the cis-Golgi compartment. In contrast, the two Golgi markers colocalized with the MUC2 apomucin and protein disulphide isomerase in the RER of colon cancer cells. On the basis of these results, we propose that in colon cancer cells a redistribution of molecules normally present in the Golgi apparatus takes place; this alteration may contribute to the abnormal glycosylation of proteins and lipids associated with neoplastic transformation. |
| doi_str_mv | 10.1242/jcs.105.3.819 |
| format | Article |
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X</creator><creatorcontrib>EGEA, G ; FRANCI, C ; GAMBUS, G ; LESUFFLEUR, T ; ZWEIBAUM, A ; REAL, F. X</creatorcontrib><description>Neoplastic transformation is commonly associated with altered glycosylation of proteins and lipids. To understand the basis for altered mucin glycosylation, we have examined the distribution of RER markers, a cis-Golgi resident protein, and the GalNAc alpha-O-Ser/Thr epitope (Tn) in human colon cancer cells and in normal colon. In cultured mucin-producing colon cancer cells, Gal-NAc alpha-O-Ser/Thr was found in mucin droplets and in RER cisternae. In addition, the Golgi apparatus was disorganized in a proportion of cells and a 130 kDa cis-Golgi resident protein was also abnormally redistributed to the RER. The distribution of the MUC2 intestinal apomucin, protein disulphide isomerase, Gal-NAc alpha-O-Ser/Thr, and the 130 kDa cis-Golgi resident protein was analysed in normal colon and in colon cancer tissues. In normal colon, MUC2 apomucin and protein disulphide isomerase were located in the RER, whereas the cis-Golgi resident protein and GalNAc alpha-O-Ser/Thr were detected only in the cis-Golgi compartment. In contrast, the two Golgi markers colocalized with the MUC2 apomucin and protein disulphide isomerase in the RER of colon cancer cells. On the basis of these results, we propose that in colon cancer cells a redistribution of molecules normally present in the Golgi apparatus takes place; this alteration may contribute to the abnormal glycosylation of proteins and lipids associated with neoplastic transformation.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.105.3.819</identifier><identifier>PMID: 7691849</identifier><identifier>CODEN: JNCSAI</identifier><language>eng</language><publisher>Cambridge: Company of Biologists</publisher><subject>Biological and medical sciences ; Cell Compartmentation ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Colonic Neoplasms - immunology ; Colonic Neoplasms - metabolism ; Colonic Neoplasms - ultrastructure ; Endoplasmic Reticulum - metabolism ; Epitopes - metabolism ; Fundamental and applied biological sciences. Psychology ; Golgi Apparatus - metabolism ; Humans ; Microscopy, Immunoelectron ; Molecular and cellular biology ; Neoplasm Proteins - immunology ; Neoplasm Proteins - metabolism ; Polysaccharides - immunology ; Polysaccharides - metabolism ; Tumor Cells, Cultured - metabolism ; Tumor Cells, Cultured - ultrastructure</subject><ispartof>Journal of cell science, 1993-07, Vol.105 (3), p.819-830</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-ead673189ee43ca6666d856243e4fba1cff5c66d07f6771ee44fe9227b6ae0c33</citedby><cites>FETCH-LOGICAL-c391t-ead673189ee43ca6666d856243e4fba1cff5c66d07f6771ee44fe9227b6ae0c33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3665,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3781950$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7691849$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>EGEA, G</creatorcontrib><creatorcontrib>FRANCI, C</creatorcontrib><creatorcontrib>GAMBUS, G</creatorcontrib><creatorcontrib>LESUFFLEUR, T</creatorcontrib><creatorcontrib>ZWEIBAUM, A</creatorcontrib><creatorcontrib>REAL, F. X</creatorcontrib><title>cis-Golgi resident proteins and O-glycans are abnormally compartmentalized in the RER of colon cancer cells</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>Neoplastic transformation is commonly associated with altered glycosylation of proteins and lipids. To understand the basis for altered mucin glycosylation, we have examined the distribution of RER markers, a cis-Golgi resident protein, and the GalNAc alpha-O-Ser/Thr epitope (Tn) in human colon cancer cells and in normal colon. In cultured mucin-producing colon cancer cells, Gal-NAc alpha-O-Ser/Thr was found in mucin droplets and in RER cisternae. In addition, the Golgi apparatus was disorganized in a proportion of cells and a 130 kDa cis-Golgi resident protein was also abnormally redistributed to the RER. The distribution of the MUC2 intestinal apomucin, protein disulphide isomerase, Gal-NAc alpha-O-Ser/Thr, and the 130 kDa cis-Golgi resident protein was analysed in normal colon and in colon cancer tissues. In normal colon, MUC2 apomucin and protein disulphide isomerase were located in the RER, whereas the cis-Golgi resident protein and GalNAc alpha-O-Ser/Thr were detected only in the cis-Golgi compartment. In contrast, the two Golgi markers colocalized with the MUC2 apomucin and protein disulphide isomerase in the RER of colon cancer cells. On the basis of these results, we propose that in colon cancer cells a redistribution of molecules normally present in the Golgi apparatus takes place; this alteration may contribute to the abnormal glycosylation of proteins and lipids associated with neoplastic transformation.</description><subject>Biological and medical sciences</subject><subject>Cell Compartmentation</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Colonic Neoplasms - immunology</subject><subject>Colonic Neoplasms - metabolism</subject><subject>Colonic Neoplasms - ultrastructure</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Epitopes - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Golgi Apparatus - metabolism</subject><subject>Humans</subject><subject>Microscopy, Immunoelectron</subject><subject>Molecular and cellular biology</subject><subject>Neoplasm Proteins - immunology</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Polysaccharides - immunology</subject><subject>Polysaccharides - metabolism</subject><subject>Tumor Cells, Cultured - metabolism</subject><subject>Tumor Cells, Cultured - ultrastructure</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMFPwyAUxonRzDk9ejThYLy1QmlLORozp8mSJYueG0ofk0nLhO4w_3pZ1ozLg_f93hfeh9A9JSnN8ux5q0JKSZGytKLiAk1pznkiKOOXaEpIRhNRMHaNbkLYEkJ4JvgETXgpaJWLKfpRJiQLZzcGewimhX7AO-8GMH3Asm_xKtnYg5LHlwcsm975Tlp7wMp1O-mHLk5Ia_6gxabHwzfg9XyNnY66dT2Okwo8VmBtuEVXWtoAd2Odoa-3-efre7JcLT5eX5aJYoIOCci25IxWAiBnSpbxtFVRZjmDXDeSKq0LFXuE65JzGqlcg8gy3pQSiGJshp5OvnGR3z2Eoe5MOP5A9uD2oeaFEIxUNILJCVTeheBB1ztvOukPNSX1Mdw6hhvvRc3qGG7kH0bjfdNBe6bHNKP-OOoyKGm1j8ubcMYYjyYFYf-HS4Nl</recordid><startdate>19930701</startdate><enddate>19930701</enddate><creator>EGEA, G</creator><creator>FRANCI, C</creator><creator>GAMBUS, G</creator><creator>LESUFFLEUR, T</creator><creator>ZWEIBAUM, A</creator><creator>REAL, F. 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Action of oncogenes and antioncogenes</topic><topic>Colonic Neoplasms - immunology</topic><topic>Colonic Neoplasms - metabolism</topic><topic>Colonic Neoplasms - ultrastructure</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Epitopes - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Golgi Apparatus - metabolism</topic><topic>Humans</topic><topic>Microscopy, Immunoelectron</topic><topic>Molecular and cellular biology</topic><topic>Neoplasm Proteins - immunology</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Polysaccharides - immunology</topic><topic>Polysaccharides - metabolism</topic><topic>Tumor Cells, Cultured - metabolism</topic><topic>Tumor Cells, Cultured - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>EGEA, G</creatorcontrib><creatorcontrib>FRANCI, C</creatorcontrib><creatorcontrib>GAMBUS, G</creatorcontrib><creatorcontrib>LESUFFLEUR, T</creatorcontrib><creatorcontrib>ZWEIBAUM, A</creatorcontrib><creatorcontrib>REAL, F. 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X</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cis-Golgi resident proteins and O-glycans are abnormally compartmentalized in the RER of colon cancer cells</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>1993-07-01</date><risdate>1993</risdate><volume>105</volume><issue>3</issue><spage>819</spage><epage>830</epage><pages>819-830</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><coden>JNCSAI</coden><abstract>Neoplastic transformation is commonly associated with altered glycosylation of proteins and lipids. To understand the basis for altered mucin glycosylation, we have examined the distribution of RER markers, a cis-Golgi resident protein, and the GalNAc alpha-O-Ser/Thr epitope (Tn) in human colon cancer cells and in normal colon. In cultured mucin-producing colon cancer cells, Gal-NAc alpha-O-Ser/Thr was found in mucin droplets and in RER cisternae. In addition, the Golgi apparatus was disorganized in a proportion of cells and a 130 kDa cis-Golgi resident protein was also abnormally redistributed to the RER. The distribution of the MUC2 intestinal apomucin, protein disulphide isomerase, Gal-NAc alpha-O-Ser/Thr, and the 130 kDa cis-Golgi resident protein was analysed in normal colon and in colon cancer tissues. In normal colon, MUC2 apomucin and protein disulphide isomerase were located in the RER, whereas the cis-Golgi resident protein and GalNAc alpha-O-Ser/Thr were detected only in the cis-Golgi compartment. In contrast, the two Golgi markers colocalized with the MUC2 apomucin and protein disulphide isomerase in the RER of colon cancer cells. 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Company of Biologists |
| subjects | Biological and medical sciences Cell Compartmentation Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Colonic Neoplasms - immunology Colonic Neoplasms - metabolism Colonic Neoplasms - ultrastructure Endoplasmic Reticulum - metabolism Epitopes - metabolism Fundamental and applied biological sciences. Psychology Golgi Apparatus - metabolism Humans Microscopy, Immunoelectron Molecular and cellular biology Neoplasm Proteins - immunology Neoplasm Proteins - metabolism Polysaccharides - immunology Polysaccharides - metabolism Tumor Cells, Cultured - metabolism Tumor Cells, Cultured - ultrastructure |
| title | cis-Golgi resident proteins and O-glycans are abnormally compartmentalized in the RER of colon cancer cells |
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