The Impact of Chain Length and Flexibility in the Interaction between Sulfated Alginates and HGF and FGF-2.
Identifieur interne : 001458 ( PubMed/Corpus ); précédent : 001457; suivant : 001459The Impact of Chain Length and Flexibility in the Interaction between Sulfated Alginates and HGF and FGF-2.
Auteurs : Ystein Arlov ; Finn L. Aachmann ; Emadoldin Feyzi ; Anders Sundan ; Gudmund Skj K-Br KSource :
- Biomacromolecules [ 1526-4602 ] ; 2015.
English descriptors
- KwdEn :
- Alginates (chemistry), Cell Line, Tumor, Fibroblast Growth Factor 2 (metabolism), Glucuronic Acid (chemistry), Glycosaminoglycans (chemistry), Heparitin Sulfate (chemistry), Hepatocyte Growth Factor (metabolism), Hexuronic Acids (chemistry), Hexuronic Acids (pharmacology), Humans, Multiple Myeloma (drug therapy), Oligosaccharides (chemistry), Oligosaccharides (pharmacology), Sulfates (chemistry).
- MESH :
- chemical , chemistry : Alginates, Glucuronic Acid, Glycosaminoglycans, Heparitin Sulfate, Hexuronic Acids, Oligosaccharides, Sulfates.
- chemical , metabolism : Fibroblast Growth Factor 2, Hepatocyte Growth Factor.
- chemical , pharmacology : Hexuronic Acids, Oligosaccharides.
- drug therapy : Multiple Myeloma.
- Cell Line, Tumor, Humans.
Abstract
Alginate is a promising polysaccharide for use in biomaterials as it is biologically inert. One way to functionalize alginate is by chemical sulfation to emulate sulfated glycosaminoglycans, which interact with a variety of proteins critical for tissue development and homeostasis. In the present work we studied the impact of chain length and flexibility of sulfated alginates for interactions with FGF-2 and HGF. Both growth factors interact with defined sequences of heparan sulfate (HS) at the cell surface or in the extracellular matrix. Whereas FGF-2 interacts with a pentasaccharide sequence containing a critical 2-O-sulfated iduronic acid, HGF has been suggested to require a highly sulfated HS/heparin octasaccharide. Here, oligosaccharides of alternating mannuronic and guluronic acid (MG) were sulfated and assessed by their relative efficacy at releasing growth factor bound to the surface of myeloma cells. 8-mers of sulfated MG (SMG) alginate showed significant HGF release compared to shorter fragments, while the maximum efficacy was achieved at a chain length average of 14 monosaccharides. FGF-2 release required a higher concentration of the SMG fragments, and the 14-mer was less potent compared to an equally sulfated high-molecular weight SMG. Sulfated mannuronan (SM) was subjected to periodate oxidation to increase chain flexibility. To assess the change in flexibility, the persistence length was estimated by SEC-MALLS analysis and the Bohdanecky approach to the worm-like chain model. A high degree of oxidation of SM resulted in approximately twice as potent HGF release compared to the nonoxidized SM alginate. The release of FGF-2 also increased with the degree of oxidation, but to a lower degree compared to that of HGF. It was found that the SM alginates were more efficient at releasing FGF-2 than the SMG alginates, indicating a greater dependence on monosaccharide identity and charge orientation over chain flexibility and charge density.
DOI: 10.1021/acs.biomac.5b01125
PubMed: 26406104
Links to Exploration step
pubmed:26406104Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Impact of Chain Length and Flexibility in the Interaction between Sulfated Alginates and HGF and FGF-2.</title><author><name sortKey="Arlov, Ystein" sort="Arlov, Ystein" uniqKey="Arlov " first=" Ystein" last="Arlov"> Ystein Arlov</name><affiliation><nlm:affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Aachmann, Finn L" sort="Aachmann, Finn L" uniqKey="Aachmann F" first="Finn L" last="Aachmann">Finn L. Aachmann</name><affiliation><nlm:affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Feyzi, Emadoldin" sort="Feyzi, Emadoldin" uniqKey="Feyzi E" first="Emadoldin" last="Feyzi">Emadoldin Feyzi</name><affiliation><nlm:affiliation>K.G. Jebsen Center for Myeloma Research and Centre of Molecular Inflammation Research (CEMIR), Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology , Prinsesse Kristinas gate 1, 7030 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Sundan, Anders" sort="Sundan, Anders" uniqKey="Sundan A" first="Anders" last="Sundan">Anders Sundan</name><affiliation><nlm:affiliation>K.G. Jebsen Center for Myeloma Research and Centre of Molecular Inflammation Research (CEMIR), Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology , Prinsesse Kristinas gate 1, 7030 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Skj K Br K, Gudmund" sort="Skj K Br K, Gudmund" uniqKey="Skj K Br K G" first="Gudmund" last="Skj K-Br K">Gudmund Skj K-Br K</name><affiliation><nlm:affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26406104</idno><idno type="pmid">26406104</idno><idno type="doi">10.1021/acs.biomac.5b01125</idno><idno type="wicri:Area/PubMed/Corpus">001458</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001458</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The Impact of Chain Length and Flexibility in the Interaction between Sulfated Alginates and HGF and FGF-2.</title><author><name sortKey="Arlov, Ystein" sort="Arlov, Ystein" uniqKey="Arlov " first=" Ystein" last="Arlov"> Ystein Arlov</name><affiliation><nlm:affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Aachmann, Finn L" sort="Aachmann, Finn L" uniqKey="Aachmann F" first="Finn L" last="Aachmann">Finn L. Aachmann</name><affiliation><nlm:affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Feyzi, Emadoldin" sort="Feyzi, Emadoldin" uniqKey="Feyzi E" first="Emadoldin" last="Feyzi">Emadoldin Feyzi</name><affiliation><nlm:affiliation>K.G. Jebsen Center for Myeloma Research and Centre of Molecular Inflammation Research (CEMIR), Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology , Prinsesse Kristinas gate 1, 7030 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Sundan, Anders" sort="Sundan, Anders" uniqKey="Sundan A" first="Anders" last="Sundan">Anders Sundan</name><affiliation><nlm:affiliation>K.G. Jebsen Center for Myeloma Research and Centre of Molecular Inflammation Research (CEMIR), Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology , Prinsesse Kristinas gate 1, 7030 Trondheim, Norway.</nlm:affiliation></affiliation></author><author><name sortKey="Skj K Br K, Gudmund" sort="Skj K Br K, Gudmund" uniqKey="Skj K Br K G" first="Gudmund" last="Skj K-Br K">Gudmund Skj K-Br K</name><affiliation><nlm:affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Biomacromolecules</title><idno type="eISSN">1526-4602</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alginates (chemistry)</term><term>Cell Line, Tumor</term><term>Fibroblast Growth Factor 2 (metabolism)</term><term>Glucuronic Acid (chemistry)</term><term>Glycosaminoglycans (chemistry)</term><term>Heparitin Sulfate (chemistry)</term><term>Hepatocyte Growth Factor (metabolism)</term><term>Hexuronic Acids (chemistry)</term><term>Hexuronic Acids (pharmacology)</term><term>Humans</term><term>Multiple Myeloma (drug therapy)</term><term>Oligosaccharides (chemistry)</term><term>Oligosaccharides (pharmacology)</term><term>Sulfates (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alginates</term><term>Glucuronic Acid</term><term>Glycosaminoglycans</term><term>Heparitin Sulfate</term><term>Hexuronic Acids</term><term>Oligosaccharides</term><term>Sulfates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fibroblast Growth Factor 2</term><term>Hepatocyte Growth Factor</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hexuronic Acids</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Multiple Myeloma</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Alginate is a promising polysaccharide for use in biomaterials as it is biologically inert. One way to functionalize alginate is by chemical sulfation to emulate sulfated glycosaminoglycans, which interact with a variety of proteins critical for tissue development and homeostasis. In the present work we studied the impact of chain length and flexibility of sulfated alginates for interactions with FGF-2 and HGF. Both growth factors interact with defined sequences of heparan sulfate (HS) at the cell surface or in the extracellular matrix. Whereas FGF-2 interacts with a pentasaccharide sequence containing a critical 2-O-sulfated iduronic acid, HGF has been suggested to require a highly sulfated HS/heparin octasaccharide. Here, oligosaccharides of alternating mannuronic and guluronic acid (MG) were sulfated and assessed by their relative efficacy at releasing growth factor bound to the surface of myeloma cells. 8-mers of sulfated MG (SMG) alginate showed significant HGF release compared to shorter fragments, while the maximum efficacy was achieved at a chain length average of 14 monosaccharides. FGF-2 release required a higher concentration of the SMG fragments, and the 14-mer was less potent compared to an equally sulfated high-molecular weight SMG. Sulfated mannuronan (SM) was subjected to periodate oxidation to increase chain flexibility. To assess the change in flexibility, the persistence length was estimated by SEC-MALLS analysis and the Bohdanecky approach to the worm-like chain model. A high degree of oxidation of SM resulted in approximately twice as potent HGF release compared to the nonoxidized SM alginate. The release of FGF-2 also increased with the degree of oxidation, but to a lower degree compared to that of HGF. It was found that the SM alginates were more efficient at releasing FGF-2 than the SMG alginates, indicating a greater dependence on monosaccharide identity and charge orientation over chain flexibility and charge density. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26406104</PMID><DateCompleted><Year>2016</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1526-4602</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>11</Issue><PubDate><Year>2015</Year><Month>Nov</Month><Day>09</Day></PubDate></JournalIssue><Title>Biomacromolecules</Title><ISOAbbreviation>Biomacromolecules</ISOAbbreviation></Journal><ArticleTitle>The Impact of Chain Length and Flexibility in the Interaction between Sulfated Alginates and HGF and FGF-2.</ArticleTitle><Pagination><MedlinePgn>3417-24</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biomac.5b01125</ELocationID><Abstract><AbstractText>Alginate is a promising polysaccharide for use in biomaterials as it is biologically inert. One way to functionalize alginate is by chemical sulfation to emulate sulfated glycosaminoglycans, which interact with a variety of proteins critical for tissue development and homeostasis. In the present work we studied the impact of chain length and flexibility of sulfated alginates for interactions with FGF-2 and HGF. Both growth factors interact with defined sequences of heparan sulfate (HS) at the cell surface or in the extracellular matrix. Whereas FGF-2 interacts with a pentasaccharide sequence containing a critical 2-O-sulfated iduronic acid, HGF has been suggested to require a highly sulfated HS/heparin octasaccharide. Here, oligosaccharides of alternating mannuronic and guluronic acid (MG) were sulfated and assessed by their relative efficacy at releasing growth factor bound to the surface of myeloma cells. 8-mers of sulfated MG (SMG) alginate showed significant HGF release compared to shorter fragments, while the maximum efficacy was achieved at a chain length average of 14 monosaccharides. FGF-2 release required a higher concentration of the SMG fragments, and the 14-mer was less potent compared to an equally sulfated high-molecular weight SMG. Sulfated mannuronan (SM) was subjected to periodate oxidation to increase chain flexibility. To assess the change in flexibility, the persistence length was estimated by SEC-MALLS analysis and the Bohdanecky approach to the worm-like chain model. A high degree of oxidation of SM resulted in approximately twice as potent HGF release compared to the nonoxidized SM alginate. The release of FGF-2 also increased with the degree of oxidation, but to a lower degree compared to that of HGF. It was found that the SM alginates were more efficient at releasing FGF-2 than the SMG alginates, indicating a greater dependence on monosaccharide identity and charge orientation over chain flexibility and charge density. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Arlov</LastName><ForeName>Øystein</ForeName><Initials>Ø</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aachmann</LastName><ForeName>Finn L</ForeName><Initials>FL</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Feyzi</LastName><ForeName>Emadoldin</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>K.G. Jebsen Center for Myeloma Research and Centre of Molecular Inflammation Research (CEMIR), Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology , Prinsesse Kristinas gate 1, 7030 Trondheim, Norway.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Hematology, St. Olav University Hospital , Erling Skjalgsons Gate 1, 7030 Trondheim, Norway.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sundan</LastName><ForeName>Anders</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>K.G. Jebsen Center for Myeloma Research and Centre of Molecular Inflammation Research (CEMIR), Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology , Prinsesse Kristinas gate 1, 7030 Trondheim, Norway.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Skjåk-Bræk</LastName><ForeName>Gudmund</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Norwegian University of Science and Technology , Sem Sælands vei 6/8, 7034 Trondheim, Norway.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>10</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biomacromolecules</MedlineTA><NlmUniqueID>100892849</NlmUniqueID><ISSNLinking>1525-7797</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000464">Alginates</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="D006603">Hexuronic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013431">Sulfates</NameOfSubstance></Chemical><Chemical><RegistryNumber>103107-01-3</RegistryNumber><NameOfSubstance UI="D016222">Fibroblast Growth Factor 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>15769-56-9</RegistryNumber><NameOfSubstance UI="C007896">guluronic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>67256-21-7</RegistryNumber><NameOfSubstance UI="D017228">Hepatocyte Growth Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>8A5D83Q4RW</RegistryNumber><NameOfSubstance UI="D020723">Glucuronic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>9050-30-0</RegistryNumber><NameOfSubstance UI="D006497">Heparitin Sulfate</NameOfSubstance></Chemical><Chemical><RegistryNumber>980IT47Y34</RegistryNumber><NameOfSubstance UI="C008324">mannuronic acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000464" MajorTopicYN="N">Alginates</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016222" MajorTopicYN="N">Fibroblast Growth Factor 2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020723" MajorTopicYN="N">Glucuronic Acid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006025" MajorTopicYN="N">Glycosaminoglycans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006497" MajorTopicYN="N">Heparitin Sulfate</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017228" MajorTopicYN="N">Hepatocyte Growth Factor</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006603" MajorTopicYN="N">Hexuronic Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009101" MajorTopicYN="N">Multiple Myeloma</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009844" MajorTopicYN="N">Oligosaccharides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013431" MajorTopicYN="N">Sulfates</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>9</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26406104</ArticleId><ArticleId IdType="doi">10.1021/acs.biomac.5b01125</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001458 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 001458 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:26406104
|texte= The Impact of Chain Length and Flexibility in the Interaction between Sulfated Alginates and HGF and FGF-2.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:26406104" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |