Detection of oligosaccharide ligands for hepatocyte growth factor/scatter factor (HGF/SF), keratinocyte growth factor (KGF/FGF-7), RANTES and heparin cofactor II by neoglycolipid microarrays of glycosaminoglycan-derived oligosaccharide fragments.
Identifieur interne : 000472 ( Ncbi/Merge ); précédent : 000471; suivant : 000473Detection of oligosaccharide ligands for hepatocyte growth factor/scatter factor (HGF/SF), keratinocyte growth factor (KGF/FGF-7), RANTES and heparin cofactor II by neoglycolipid microarrays of glycosaminoglycan-derived oligosaccharide fragments.
Auteurs : Keiko Yamaguchi [Japon] ; Hirotoshi Tamaki ; Shigeyuki FukuiSource :
- Glycoconjugate journal [ 0282-0080 ] ; 2006.
Descripteurs français
- KwdFr :
- Analyse sur microréseau (), Animaux, Bovins, Chimiokine CCL5 (métabolisme), Chondroitinases et chondroitin lyases, Cofacteur II de l'héparine (métabolisme), Colorants fluorescents, Facteur de croissance des hépatocytes (métabolisme), Facteur de croissance fibroblastique de type 7 (métabolisme), Glycosaminoglycanes (), Glycosaminoglycanes (métabolisme), Heparin lyase, Humains, Héparine (), Héparine (métabolisme), Lapins, Liaison aux protéines, Ligands, Oligosaccharides (), Oligosaccharides (métabolisme), Protéines recombinantes (métabolisme), Souris, Techniques in vitro.
- MESH :
- métabolisme : Chimiokine CCL5, Cofacteur II de l'héparine, Facteur de croissance des hépatocytes, Facteur de croissance fibroblastique de type 7, Glycosaminoglycanes, Héparine, Oligosaccharides, Protéines recombinantes.
- Analyse sur microréseau, Animaux, Bovins, Chondroitinases et chondroitin lyases, Colorants fluorescents, Glycosaminoglycanes, Heparin lyase, Humains, Héparine, Lapins, Liaison aux protéines, Ligands, Oligosaccharides, Souris, Techniques in vitro.
English descriptors
- KwdEn :
- Animals, Cattle, Chemokine CCL5 (metabolism), Chondroitinases and Chondroitin Lyases, Fibroblast Growth Factor 7 (metabolism), Fluorescent Dyes, Glycosaminoglycans (chemistry), Glycosaminoglycans (metabolism), Heparin (chemistry), Heparin (metabolism), Heparin Cofactor II (metabolism), Heparin Lyase, Hepatocyte Growth Factor (metabolism), Humans, In Vitro Techniques, Ligands, Mice, Microarray Analysis (methods), Oligosaccharides (chemistry), Oligosaccharides (metabolism), Protein Binding, Rabbits, Recombinant Proteins (metabolism).
- MESH :
- chemical , chemistry : Glycosaminoglycans, Heparin, Oligosaccharides.
- chemical , metabolism : Chemokine CCL5, Fibroblast Growth Factor 7, Glycosaminoglycans, Heparin, Heparin Cofactor II, Hepatocyte Growth Factor, Oligosaccharides, Recombinant Proteins.
- methods : Microarray Analysis.
- Animals, Cattle, Chondroitinases and Chondroitin Lyases, Fluorescent Dyes, Heparin Lyase, Humans, In Vitro Techniques, Ligands, Mice, Protein Binding, Rabbits.
Abstract
Neoglycolipid technology is eminently adaptable for microarray design for high-throughput detection and specificity assignments of carbohydrate-protein interactions. Dermatan sulfate (DS) is known to play an important role because of its ability to bind growth factors as well as chemokines and to modulate their biological activities during inflammation and response to injury. We prepared various iduronic acid-rich fragments from DS by complete digestion with chondroitinase ACI, and investigated whether the DS-binding proteins, such as HGF/SF, RANTES, KGF/FGF-7 and HCII, can detect their oligosaccharide ligands in a neoglycolipid microarray. First, a comparison of the intensity of binding signals obtained from chondroitin oligosaccharides with those of heparin oligosaccharides showed that our microarray system is feasible not only to single-out the oligosaccharide ligands, but also to detect the difference between an intrinsic interaction unrelated only to electrostatic interaction and non-specific electrostatic interaction. Second, HGF/SF, KGF/FGF-7 and HCII showed preferential binding to iduronic acid-rich fragments of DS oligosaccharides that are greater than 8-mers in lengths. In contrast, RANTES binding seemed to depend only on the negative charges; their binding intensity towards the DS oligosaccharides was somewhat stronger than the binding of HGF/SF, KGF/FGF-7 and HCII. Third, the use of polyvinylpyrrolidone-40 (PVP-40), ovalbumin (OV) and Tween 20 in place of BSA as a blotting agent was useful in these glycosaminoglycan dependent reactions to minimize background due to non-specific interactions.
DOI: 10.1007/s10719-006-7151-z
PubMed: 17006643
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pubmed:17006643Le document en format XML
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xml:lang="en">Neoglycolipid technology is eminently adaptable for microarray design for high-throughput detection and specificity assignments of carbohydrate-protein interactions. Dermatan sulfate (DS) is known to play an important role because of its ability to bind growth factors as well as chemokines and to modulate their biological activities during inflammation and response to injury. We prepared various iduronic acid-rich fragments from DS by complete digestion with chondroitinase ACI, and investigated whether the DS-binding proteins, such as HGF/SF, RANTES, KGF/FGF-7 and HCII, can detect their oligosaccharide ligands in a neoglycolipid microarray. First, a comparison of the intensity of binding signals obtained from chondroitin oligosaccharides with those of heparin oligosaccharides showed that our microarray system is feasible not only to single-out the oligosaccharide ligands, but also to detect the difference between an intrinsic interaction unrelated only to electrostatic interaction and non-specific electrostatic interaction. Second, HGF/SF, KGF/FGF-7 and HCII showed preferential binding to iduronic acid-rich fragments of DS oligosaccharides that are greater than 8-mers in lengths. In contrast, RANTES binding seemed to depend only on the negative charges; their binding intensity towards the DS oligosaccharides was somewhat stronger than the binding of HGF/SF, KGF/FGF-7 and HCII. Third, the use of polyvinylpyrrolidone-40 (PVP-40), ovalbumin (OV) and Tween 20 in place of BSA as a blotting agent was useful in these glycosaminoglycan dependent reactions to minimize background due to non-specific interactions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17006643</PMID><DateCompleted><Year>2007</Year><Month>04</Month><Day>11</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0282-0080</ISSN><JournalIssue CitedMedium="Print"><Volume>23</Volume><Issue>7-8</Issue><PubDate><Year>2006</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Glycoconjugate journal</Title><ISOAbbreviation>Glycoconj. J.</ISOAbbreviation></Journal><ArticleTitle>Detection of oligosaccharide ligands for hepatocyte growth factor/scatter factor (HGF/SF), keratinocyte growth factor (KGF/FGF-7), RANTES and heparin cofactor II by neoglycolipid microarrays of glycosaminoglycan-derived oligosaccharide fragments.</ArticleTitle><Pagination><MedlinePgn>513-23</MedlinePgn></Pagination><Abstract><AbstractText>Neoglycolipid technology is eminently adaptable for microarray design for high-throughput detection and specificity assignments of carbohydrate-protein interactions. Dermatan sulfate (DS) is known to play an important role because of its ability to bind growth factors as well as chemokines and to modulate their biological activities during inflammation and response to injury. We prepared various iduronic acid-rich fragments from DS by complete digestion with chondroitinase ACI, and investigated whether the DS-binding proteins, such as HGF/SF, RANTES, KGF/FGF-7 and HCII, can detect their oligosaccharide ligands in a neoglycolipid microarray. First, a comparison of the intensity of binding signals obtained from chondroitin oligosaccharides with those of heparin oligosaccharides showed that our microarray system is feasible not only to single-out the oligosaccharide ligands, but also to detect the difference between an intrinsic interaction unrelated only to electrostatic interaction and non-specific electrostatic interaction. Second, HGF/SF, KGF/FGF-7 and HCII showed preferential binding to iduronic acid-rich fragments of DS oligosaccharides that are greater than 8-mers in lengths. In contrast, RANTES binding seemed to depend only on the negative charges; their binding intensity towards the DS oligosaccharides was somewhat stronger than the binding of HGF/SF, KGF/FGF-7 and HCII. Third, the use of polyvinylpyrrolidone-40 (PVP-40), ovalbumin (OV) and Tween 20 in place of BSA as a blotting agent was useful in these glycosaminoglycan dependent reactions to minimize background due to non-specific interactions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yamaguchi</LastName><ForeName>Keiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University, Motoyama, Kita-ku, Kyoto, 603-8555, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tamaki</LastName><ForeName>Hirotoshi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Fukui</LastName><ForeName>Shigeyuki</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Glycoconj J</MedlineTA><NlmUniqueID>8603310</NlmUniqueID><ISSNLinking>0282-0080</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018946">Chemokine CCL5</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C496453">FGF7 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005456">Fluorescent Dyes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006025">Glycosaminoglycans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C066855">HGF protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008024">Ligands</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>126469-10-1</RegistryNumber><NameOfSubstance UI="D051523">Fibroblast Growth Factor 7</NameOfSubstance></Chemical><Chemical><RegistryNumber>67256-21-7</RegistryNumber><NameOfSubstance UI="D017228">Hepatocyte Growth Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>81604-65-1</RegistryNumber><NameOfSubstance UI="D015844">Heparin Cofactor II</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-49-6</RegistryNumber><NameOfSubstance UI="D006493">Heparin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.2.-</RegistryNumber><NameOfSubstance UI="D002810">Chondroitinases and Chondroitin Lyases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.2.7</RegistryNumber><NameOfSubstance UI="D019763">Heparin Lyase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018946" MajorTopicYN="N">Chemokine CCL5</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002810" MajorTopicYN="N">Chondroitinases and Chondroitin Lyases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051523" MajorTopicYN="N">Fibroblast Growth Factor 7</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005456" MajorTopicYN="N">Fluorescent Dyes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006025" MajorTopicYN="N">Glycosaminoglycans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006493" MajorTopicYN="N">Heparin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015844" MajorTopicYN="N">Heparin Cofactor II</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019763" MajorTopicYN="N">Heparin Lyase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017228" MajorTopicYN="N">Hepatocyte Growth Factor</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D066298" MajorTopicYN="N">In Vitro Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046228" MajorTopicYN="N">Microarray Analysis</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009844" MajorTopicYN="N">Oligosaccharides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011817" 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2002 Sep;12(9):117R-25R</Citation><ArticleIdList><ArticleId IdType="pubmed">12213784</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1970 Sep 25;245(18):4770-83</Citation><ArticleIdList><ArticleId IdType="pubmed">5456149</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2001 May 29;40(21):6303-18</Citation><ArticleIdList><ArticleId IdType="pubmed">11371192</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Dec 14;276(50):47599-607</Citation><ArticleIdList><ArticleId IdType="pubmed">11598131</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 2001 Oct 1;297(1):42-51</Citation><ArticleIdList><ArticleId IdType="pubmed">11567526</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1978 Jun 10;253(11):3862-9</Citation><ArticleIdList><ArticleId IdType="pubmed">649611</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1990 Oct 25;265(30):18263-71</Citation><ArticleIdList><ArticleId IdType="pubmed">2211700</ArticleId></ArticleIdList></Reference><Reference><Citation>Dev Dyn. 1995 Jun;203(2):223-40</Citation><ArticleIdList><ArticleId IdType="pubmed">7655084</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Dec 21;276(51):48341-9</Citation><ArticleIdList><ArticleId IdType="pubmed">11590178</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Biotechnol. 2002 Oct;20(10):1011-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12219077</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Mol Cell Biol. 2004 Jul;5(7):582-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15232576</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1998 Oct 23;273(43):28116-21</Citation><ArticleIdList><ArticleId IdType="pubmed">9774430</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Feb 18;280(7):5300-6</Citation><ArticleIdList><ArticleId IdType="pubmed">15563459</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Jun 15;276(24):20959-65</Citation><ArticleIdList><ArticleId IdType="pubmed">11294849</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1993 Feb 1;208(2):397-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8095775</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1977 Oct 10;252(19):6687-94</Citation><ArticleIdList><ArticleId IdType="pubmed">893435</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1994;230:484-519</Citation><ArticleIdList><ArticleId IdType="pubmed">8139514</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1973 Sep 10;248(17):6019-28</Citation><ArticleIdList><ArticleId IdType="pubmed">4269443</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 2000 Mar;267(6):1795-804</Citation><ArticleIdList><ArticleId IdType="pubmed">10712612</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1998 Jan 2;273(1):271-8</Citation><ArticleIdList><ArticleId IdType="pubmed">9417075</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1982 May 25;257(10):5523-7</Citation><ArticleIdList><ArticleId IdType="pubmed">7068605</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1988 Dec 1;256(2):661-4</Citation><ArticleIdList><ArticleId IdType="pubmed">3223939</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1983 Jun 10;258(11):6713-6</Citation><ArticleIdList><ArticleId IdType="pubmed">6687888</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1994 Apr 15;269(15):11216-23</Citation><ArticleIdList><ArticleId IdType="pubmed">8157651</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Fukui, Shigeyuki" sort="Fukui, Shigeyuki" uniqKey="Fukui S" first="Shigeyuki" last="Fukui">Shigeyuki Fukui</name><name sortKey="Tamaki, Hirotoshi" sort="Tamaki, Hirotoshi" uniqKey="Tamaki H" first="Hirotoshi" last="Tamaki">Hirotoshi Tamaki</name></noCountry><country name="Japon"><noRegion><name sortKey="Yamaguchi, Keiko" sort="Yamaguchi, Keiko" uniqKey="Yamaguchi K" first="Keiko" last="Yamaguchi">Keiko Yamaguchi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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