Cell Adhesion Mediated by a Purified Fucosyltransferase
Human embryonic skin fibroblasts attach and spread on surfaces on which a fucosyltransferase purified from human milk has been immobilized. The adhesion-enhancing effect of the transferase involves specific interactions of the enzyme surface with the cell surface carbohydrate acceptors, as suggested...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1983-07, Vol.80 (13), p.3991-3995 |
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creator | Rauvala, Heikki Prieels, Jean-Paul Finne, Jukka |
description | Human embryonic skin fibroblasts attach and spread on surfaces on which a fucosyltransferase purified from human milk has been immobilized. The adhesion-enhancing effect of the transferase involves specific interactions of the enzyme surface with the cell surface carbohydrate acceptors, as suggested by the following findings. About 80% of human embryonic skin fibroblasts attach and spread in 1 hr on fucosyltransferase surfaces; in contrast, bovine serum albumin, fetuin, asialofetuin, and asialotransferrin surfaces fail to enhance adhesion. The adhesion-mediating activity of the transferase is destroyed by alkylation of the sulfhydryl groups or by heating. The adhesion on fucosyltransferase surfaces is inhibited by glycoprotein, glycolipid, and oligosaccharide acceptors containing the sugar sequence galactosyl-(β 1→ 4)-N-acetylglucosamine, in agreement with the substrate specificity of the enzyme. The results suggest that glycosyltransferases are able to stimulate cell adhesion in a manner similar to that proposed for lectins. |
doi_str_mv | 10.1073/pnas.80.13.3991 |
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The adhesion-enhancing effect of the transferase involves specific interactions of the enzyme surface with the cell surface carbohydrate acceptors, as suggested by the following findings. About 80% of human embryonic skin fibroblasts attach and spread in 1 hr on fucosyltransferase surfaces; in contrast, bovine serum albumin, fetuin, asialofetuin, and asialotransferrin surfaces fail to enhance adhesion. The adhesion-mediating activity of the transferase is destroyed by alkylation of the sulfhydryl groups or by heating. The adhesion on fucosyltransferase surfaces is inhibited by glycoprotein, glycolipid, and oligosaccharide acceptors containing the sugar sequence galactosyl-(β 1→ 4)-N-acetylglucosamine, in agreement with the substrate specificity of the enzyme. The results suggest that glycosyltransferases are able to stimulate cell adhesion in a manner similar to that proposed for lectins.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.80.13.3991</identifier><identifier>PMID: 6575391</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>3T3 cells ; Cell Adhesion ; Cell lines ; Cells ; Embryo, Mammalian ; embryos ; Enzymes ; Ethylmaleimide - pharmacology ; Female ; Fibroblasts ; Fibroblasts - physiology ; Fibronectins - pharmacology ; Fibrosis ; Fucosyltransferases - physiology ; Glycoproteins ; Hexosyltransferases - physiology ; Humans ; Kinetics ; man ; Milk, Human - enzymology ; N-acetylglucosaminide- alpha 1,3, alpha 1,4-fucosyltransferase ; Neurons ; Pregnancy ; Skin Physiological Phenomena ; Ungulates</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1983-07, Vol.80 (13), p.3991-3995</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4071-868ee07609e6e4193308b6b1ee095072cf63ca791a3d9a49d4a1346b5ecd22403</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/80/13.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/14312$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/14312$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6575391$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rauvala, Heikki</creatorcontrib><creatorcontrib>Prieels, Jean-Paul</creatorcontrib><creatorcontrib>Finne, Jukka</creatorcontrib><title>Cell Adhesion Mediated by a Purified Fucosyltransferase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Human embryonic skin fibroblasts attach and spread on surfaces on which a fucosyltransferase purified from human milk has been immobilized. The adhesion-enhancing effect of the transferase involves specific interactions of the enzyme surface with the cell surface carbohydrate acceptors, as suggested by the following findings. About 80% of human embryonic skin fibroblasts attach and spread in 1 hr on fucosyltransferase surfaces; in contrast, bovine serum albumin, fetuin, asialofetuin, and asialotransferrin surfaces fail to enhance adhesion. The adhesion-mediating activity of the transferase is destroyed by alkylation of the sulfhydryl groups or by heating. The adhesion on fucosyltransferase surfaces is inhibited by glycoprotein, glycolipid, and oligosaccharide acceptors containing the sugar sequence galactosyl-(β 1→ 4)-N-acetylglucosamine, in agreement with the substrate specificity of the enzyme. The results suggest that glycosyltransferases are able to stimulate cell adhesion in a manner similar to that proposed for lectins.</description><subject>3T3 cells</subject><subject>Cell Adhesion</subject><subject>Cell lines</subject><subject>Cells</subject><subject>Embryo, Mammalian</subject><subject>embryos</subject><subject>Enzymes</subject><subject>Ethylmaleimide - pharmacology</subject><subject>Female</subject><subject>Fibroblasts</subject><subject>Fibroblasts - physiology</subject><subject>Fibronectins - pharmacology</subject><subject>Fibrosis</subject><subject>Fucosyltransferases - physiology</subject><subject>Glycoproteins</subject><subject>Hexosyltransferases - physiology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>man</subject><subject>Milk, Human - enzymology</subject><subject>N-acetylglucosaminide- alpha 1,3, alpha 1,4-fucosyltransferase</subject><subject>Neurons</subject><subject>Pregnancy</subject><subject>Skin Physiological Phenomena</subject><subject>Ungulates</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkb1PwzAQxS0EKqUwIyGBMsGU9hw7djwwVBVfEggGmC0nuUCqNCl2guh_j6OWrwUm6_x-73znR8ghhTEFySbL2rhx4gs2ZkrRLTKkoGgouIJtMgSIZJjwiO-SPefmAKDiBAZkIGIZM0WHRM6wqoJp_oKubOrgDvPStJgH6SowwUNny6L01WWXNW5VtdbUrkBrHO6TncJUDg8254g8XV48zq7D2_urm9n0Nsw4SBomIkEEKUChQE4VY5CkIqX-UsUgo6wQLDNSUcNyZbjKuaGMizTGLI8iDmxEztd9l126wDzD2g9R6aUtF8audGNK_Vupyxf93LxppjhNYu8_3fht89qha_WidJnf2dTYdE4nEHP_vPgXpMz_GePSg5M1mNnGOYvF1zAUdJ-J7jPxjb1F95l4x_HPHb74TQheP9vovfFT_W6gi66qWnxvPXnyJ-mBozUwd21jvyfjjEbsA4HqqFM</recordid><startdate>19830701</startdate><enddate>19830701</enddate><creator>Rauvala, Heikki</creator><creator>Prieels, Jean-Paul</creator><creator>Finne, Jukka</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19830701</creationdate><title>Cell Adhesion Mediated by a Purified Fucosyltransferase</title><author>Rauvala, Heikki ; Prieels, Jean-Paul ; Finne, Jukka</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4071-868ee07609e6e4193308b6b1ee095072cf63ca791a3d9a49d4a1346b5ecd22403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>3T3 cells</topic><topic>Cell Adhesion</topic><topic>Cell lines</topic><topic>Cells</topic><topic>Embryo, Mammalian</topic><topic>embryos</topic><topic>Enzymes</topic><topic>Ethylmaleimide - pharmacology</topic><topic>Female</topic><topic>Fibroblasts</topic><topic>Fibroblasts - physiology</topic><topic>Fibronectins - pharmacology</topic><topic>Fibrosis</topic><topic>Fucosyltransferases - physiology</topic><topic>Glycoproteins</topic><topic>Hexosyltransferases - physiology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>man</topic><topic>Milk, Human - enzymology</topic><topic>N-acetylglucosaminide- alpha 1,3, alpha 1,4-fucosyltransferase</topic><topic>Neurons</topic><topic>Pregnancy</topic><topic>Skin Physiological Phenomena</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rauvala, Heikki</creatorcontrib><creatorcontrib>Prieels, Jean-Paul</creatorcontrib><creatorcontrib>Finne, Jukka</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rauvala, Heikki</au><au>Prieels, Jean-Paul</au><au>Finne, Jukka</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cell Adhesion Mediated by a Purified Fucosyltransferase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1983-07-01</date><risdate>1983</risdate><volume>80</volume><issue>13</issue><spage>3991</spage><epage>3995</epage><pages>3991-3995</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Human embryonic skin fibroblasts attach and spread on surfaces on which a fucosyltransferase purified from human milk has been immobilized. The adhesion-enhancing effect of the transferase involves specific interactions of the enzyme surface with the cell surface carbohydrate acceptors, as suggested by the following findings. About 80% of human embryonic skin fibroblasts attach and spread in 1 hr on fucosyltransferase surfaces; in contrast, bovine serum albumin, fetuin, asialofetuin, and asialotransferrin surfaces fail to enhance adhesion. The adhesion-mediating activity of the transferase is destroyed by alkylation of the sulfhydryl groups or by heating. The adhesion on fucosyltransferase surfaces is inhibited by glycoprotein, glycolipid, and oligosaccharide acceptors containing the sugar sequence galactosyl-(β 1→ 4)-N-acetylglucosamine, in agreement with the substrate specificity of the enzyme. The results suggest that glycosyltransferases are able to stimulate cell adhesion in a manner similar to that proposed for lectins.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6575391</pmid><doi>10.1073/pnas.80.13.3991</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 3T3 cells Cell Adhesion Cell lines Cells Embryo, Mammalian embryos Enzymes Ethylmaleimide - pharmacology Female Fibroblasts Fibroblasts - physiology Fibronectins - pharmacology Fibrosis Fucosyltransferases - physiology Glycoproteins Hexosyltransferases - physiology Humans Kinetics man Milk, Human - enzymology N-acetylglucosaminide- alpha 1,3, alpha 1,4-fucosyltransferase Neurons Pregnancy Skin Physiological Phenomena Ungulates |
title | Cell Adhesion Mediated by a Purified Fucosyltransferase |
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