Growth-associated glycosylation of transferrin secreted by HepG2 cells
Growth-associated alterations in the oligosaccharide structures of transferrin secreted by HepG2 cells were examined by concanavalin A-crossed affinoimmuno-electrophoresis. Slowly dividing, confluent cultures produced transferrin with a approximately 4.5-fold greater proportion of biantennary comple...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-11, Vol.267 (33), p.23982-23987 |
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| container_end_page | 23987 |
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| container_issue | 33 |
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| container_title | The Journal of biological chemistry |
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| creator | HAHN, T. J GOOCHEE, C. F |
| description | Growth-associated alterations in the oligosaccharide structures of transferrin secreted by HepG2 cells were examined by concanavalin
A-crossed affinoimmuno-electrophoresis. Slowly dividing, confluent cultures produced transferrin with a approximately 4.5-fold
greater proportion of biantennary complex-type oligosaccharides than rapidly dividing, subconfluent cultures. The activity
of N-acetylglucosaminyltransferase V (GlcNAc-T V) and galactosyltransferase were measured in cell extracts from subconfluent
and confluent cultures. While the activity of galactosyltransferase remained relatively constant, the activity of GlcNAc-T
V was approximately 3.2-fold lower in confluent cultures than in subconfluent cultures. These results suggest that the growth-associated
alteration in the oligosaccharides of transferrin is due, at least in part, to the regulation of GlcNAc-T V activity. |
| doi_str_mv | 10.1016/s0021-9258(18)35933-7 |
| format | Article |
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A-crossed affinoimmuno-electrophoresis. Slowly dividing, confluent cultures produced transferrin with a approximately 4.5-fold
greater proportion of biantennary complex-type oligosaccharides than rapidly dividing, subconfluent cultures. The activity
of N-acetylglucosaminyltransferase V (GlcNAc-T V) and galactosyltransferase were measured in cell extracts from subconfluent
and confluent cultures. While the activity of galactosyltransferase remained relatively constant, the activity of GlcNAc-T
V was approximately 3.2-fold lower in confluent cultures than in subconfluent cultures. These results suggest that the growth-associated
alteration in the oligosaccharides of transferrin is due, at least in part, to the regulation of GlcNAc-T V activity.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)35933-7</identifier><identifier>PMID: 1331106</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Carbohydrate Sequence ; Carcinoma, Hepatocellular ; Cell Division ; Clone Cells ; Fundamental and applied biological sciences. Psychology ; Galactosyltransferases - metabolism ; Glycoproteins ; Glycosylation ; HepG2 cells ; Humans ; isoforms ; Kinetics ; Liver Neoplasms ; man ; Molecular Sequence Data ; N-acetylglucosaminyltransferase V ; N-Acetylglucosaminyltransferases - metabolism ; Proteins ; requirements ; secretion ; Time Factors ; transferrin ; Transferrin - biosynthesis ; Transferrin - isolation & purification ; Transferrin - metabolism ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1992-11, Vol.267 (33), p.23982-23987</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-67dbe41e3d30048c06c0a146335829b6fa3bcd1d61db4f7bc4e07e383647d55c3</citedby><cites>FETCH-LOGICAL-c506t-67dbe41e3d30048c06c0a146335829b6fa3bcd1d61db4f7bc4e07e383647d55c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4468145$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1331106$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HAHN, T. J</creatorcontrib><creatorcontrib>GOOCHEE, C. F</creatorcontrib><title>Growth-associated glycosylation of transferrin secreted by HepG2 cells</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Growth-associated alterations in the oligosaccharide structures of transferrin secreted by HepG2 cells were examined by concanavalin
A-crossed affinoimmuno-electrophoresis. Slowly dividing, confluent cultures produced transferrin with a approximately 4.5-fold
greater proportion of biantennary complex-type oligosaccharides than rapidly dividing, subconfluent cultures. The activity
of N-acetylglucosaminyltransferase V (GlcNAc-T V) and galactosyltransferase were measured in cell extracts from subconfluent
and confluent cultures. While the activity of galactosyltransferase remained relatively constant, the activity of GlcNAc-T
V was approximately 3.2-fold lower in confluent cultures than in subconfluent cultures. These results suggest that the growth-associated
alteration in the oligosaccharides of transferrin is due, at least in part, to the regulation of GlcNAc-T V activity.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Sequence</subject><subject>Carcinoma, Hepatocellular</subject><subject>Cell Division</subject><subject>Clone Cells</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactosyltransferases - metabolism</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>HepG2 cells</subject><subject>Humans</subject><subject>isoforms</subject><subject>Kinetics</subject><subject>Liver Neoplasms</subject><subject>man</subject><subject>Molecular Sequence Data</subject><subject>N-acetylglucosaminyltransferase V</subject><subject>N-Acetylglucosaminyltransferases - metabolism</subject><subject>Proteins</subject><subject>requirements</subject><subject>secretion</subject><subject>Time Factors</subject><subject>transferrin</subject><subject>Transferrin - biosynthesis</subject><subject>Transferrin - isolation & purification</subject><subject>Transferrin - metabolism</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFO3DAQhq2qiC7bPgJSDlUFhxSPx3acI0KwICFxgEq9WY7jsK6y68WTFdq3b8Ku4Igvc5hv_M98jJ0C_w0c9AVxLqCshTJnYM5R1Yhl9YXNgBssUcHfr2z2jnxjJ0T_-PhkDcfsGBABuJ6xm0VOr8OydETJRzeEtnjudz7RrndDTOsidcWQ3Zq6kHNcFxR8DhPV7IrbsFmIwoe-p-_sqHM9hR-HOmd_bq6frm7L-4fF3dXlfekV10Opq7YJEgK2OG5iPNeeO5AaURlRN7pz2PgWWg1tI7uq8TLwKqBBLatWKY9z9mv_7yanl22gwa4iTRu4dUhbstV4lzDCfAqClhqEhBFUe9DnRJRDZzc5rlzeWeB2Em0fJ4t2smjB2DfRY86cnR4Cts0qtB9Te7Nj_-eh78i7vhsd-kjvmJTagFQf2DI-L19jDraJyS_Dygpd2TFJYG0E_gc6BZEE</recordid><startdate>19921125</startdate><enddate>19921125</enddate><creator>HAHN, T. 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F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-67dbe41e3d30048c06c0a146335829b6fa3bcd1d61db4f7bc4e07e383647d55c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Sequence</topic><topic>Carcinoma, Hepatocellular</topic><topic>Cell Division</topic><topic>Clone Cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactosyltransferases - metabolism</topic><topic>Glycoproteins</topic><topic>Glycosylation</topic><topic>HepG2 cells</topic><topic>Humans</topic><topic>isoforms</topic><topic>Kinetics</topic><topic>Liver Neoplasms</topic><topic>man</topic><topic>Molecular Sequence Data</topic><topic>N-acetylglucosaminyltransferase V</topic><topic>N-Acetylglucosaminyltransferases - metabolism</topic><topic>Proteins</topic><topic>requirements</topic><topic>secretion</topic><topic>Time Factors</topic><topic>transferrin</topic><topic>Transferrin - biosynthesis</topic><topic>Transferrin - isolation & purification</topic><topic>Transferrin - metabolism</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HAHN, T. J</creatorcontrib><creatorcontrib>GOOCHEE, C. 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F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Growth-associated glycosylation of transferrin secreted by HepG2 cells</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-11-25</date><risdate>1992</risdate><volume>267</volume><issue>33</issue><spage>23982</spage><epage>23987</epage><pages>23982-23987</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Growth-associated alterations in the oligosaccharide structures of transferrin secreted by HepG2 cells were examined by concanavalin
A-crossed affinoimmuno-electrophoresis. Slowly dividing, confluent cultures produced transferrin with a approximately 4.5-fold
greater proportion of biantennary complex-type oligosaccharides than rapidly dividing, subconfluent cultures. The activity
of N-acetylglucosaminyltransferase V (GlcNAc-T V) and galactosyltransferase were measured in cell extracts from subconfluent
and confluent cultures. While the activity of galactosyltransferase remained relatively constant, the activity of GlcNAc-T
V was approximately 3.2-fold lower in confluent cultures than in subconfluent cultures. These results suggest that the growth-associated
alteration in the oligosaccharides of transferrin is due, at least in part, to the regulation of GlcNAc-T V activity.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1331106</pmid><doi>10.1016/s0021-9258(18)35933-7</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-11, Vol.267 (33), p.23982-23987 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73312828 |
| source | MEDLINE; Free E-Journal (出版社公開部分のみ）; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Carbohydrate Sequence Carcinoma, Hepatocellular Cell Division Clone Cells Fundamental and applied biological sciences. Psychology Galactosyltransferases - metabolism Glycoproteins Glycosylation HepG2 cells Humans isoforms Kinetics Liver Neoplasms man Molecular Sequence Data N-acetylglucosaminyltransferase V N-Acetylglucosaminyltransferases - metabolism Proteins requirements secretion Time Factors transferrin Transferrin - biosynthesis Transferrin - isolation & purification Transferrin - metabolism Tumor Cells, Cultured |
| title | Growth-associated glycosylation of transferrin secreted by HepG2 cells |
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