Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.
Identifieur interne : 001893 ( PubMed/Checkpoint ); précédent : 001892; suivant : 001894Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.
Auteurs : Yan G. Fulcher [États-Unis] ; Raghavendar Reddy Sanganna Gari ; Nathan C. Frey ; Fuming Zhang ; Robert J. Linhardt ; Gavin M. King ; Steven R. Van DorenSource :
- ACS chemical biology [ 1554-8937 ] ; 2014.
Descripteurs français
- KwdFr :
- Activation enzymatique, Animaux, Humains, Héparinoïde (pharmacologie), Liaison aux protéines, Matrix metalloproteinase 7 (génétique), Matrix metalloproteinase 7 (métabolisme), Microscopie à force atomique, Modèles biologiques, Muqueuse (métabolisme), Peptide hydrolases (), Peptide hydrolases (métabolisme), Propriétés de surface, Rats, Régulation allostérique, Tumeurs (métabolisme).
- MESH :
- génétique : Matrix metalloproteinase 7.
- métabolisme : Matrix metalloproteinase 7, Muqueuse, Peptide hydrolases, Tumeurs.
- pharmacologie : Héparinoïde.
- Activation enzymatique, Animaux, Humains, Liaison aux protéines, Microscopie à force atomique, Modèles biologiques, Peptide hydrolases, Propriétés de surface, Rats, Régulation allostérique.
English descriptors
- KwdEn :
- Allosteric Regulation, Animals, Enzyme Activation, Heparinoids (pharmacology), Humans, Matrix Metalloproteinase 7 (genetics), Matrix Metalloproteinase 7 (metabolism), Microscopy, Atomic Force, Models, Biological, Mucous Membrane (metabolism), Neoplasms (metabolism), Peptide Hydrolases (drug effects), Peptide Hydrolases (metabolism), Protein Binding, Rats, Surface Properties.
- MESH :
- chemical , drug effects : Peptide Hydrolases.
- chemical , genetics : Matrix Metalloproteinase 7.
- chemical , metabolism : Matrix Metalloproteinase 7, Peptide Hydrolases.
- chemical , pharmacology : Heparinoids.
- metabolism : Mucous Membrane, Neoplasms.
- Allosteric Regulation, Animals, Enzyme Activation, Humans, Microscopy, Atomic Force, Models, Biological, Protein Binding, Rats, Surface Properties.
Abstract
Activation by glycosaminoglycans (GAGs) is an emerging trend among extracellular proteases important in disease. ProMMP-7, the zymogen of a matrix metalloproteinase secreted by mucosal epithelial and tumor cells, is activated at their surfaces by sulfated GAGs, but how? ProMMP-7 is activated in trans by representative heparin oligosaccharides in a length-dependent manner, with a large jump in activation at lengths of 16 monosaccharides. Imaging by atomic force microscopy visualized small complexes of proMMP-7 molecules linked by 8-mer lengths of heparinoids and extended assembles formed with 16-mer lengths of heparin. Complexes of proMMP-7 with polydisperse heparin or heparan sulfate were more diverse. Heparinoids evidently accelerate activation by tethering multiple proMMP-7 molecules together for proteolytic attack among neighbors. Removal of either the prodomain or C-terminal peptide sequence of KRSNSRKK from MMP-7 prevents formation of the long arrays induced by heparin 16-mers or heparan sulfate. The role of the C-terminus in activation assays suggests it contributes to remote, allosteric binding of GAGs. Enhancement of proteolytic velocity of MMP-by GAGs indicates them to be effectors of V-type allostery. GAGs from proteoglycans appear to assemble proMMP-7 molecules for activation, an event preceding its tumorigenic or antibacterial proteolytic activities at cell surfaces.
DOI: 10.1021/cb400898t
PubMed: 24495220
Affiliations:
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Frey</name></author><author><name sortKey="Zhang, Fuming" sort="Zhang, Fuming" uniqKey="Zhang F" first="Fuming" last="Zhang">Fuming Zhang</name></author><author><name sortKey="Linhardt, Robert J" sort="Linhardt, Robert J" uniqKey="Linhardt R" first="Robert J" last="Linhardt">Robert J. Linhardt</name></author><author><name sortKey="King, Gavin M" sort="King, Gavin M" uniqKey="King G" first="Gavin M" last="King">Gavin M. King</name></author><author><name sortKey="Van Doren, Steven R" sort="Van Doren, Steven R" uniqKey="Van Doren S" first="Steven R" last="Van Doren">Steven R. Van Doren</name></author></analytic><series><title level="j">ACS chemical biology</title><idno type="eISSN">1554-8937</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation</term><term>Animals</term><term>Enzyme Activation</term><term>Heparinoids (pharmacology)</term><term>Humans</term><term>Matrix Metalloproteinase 7 (genetics)</term><term>Matrix Metalloproteinase 7 (metabolism)</term><term>Microscopy, Atomic Force</term><term>Models, Biological</term><term>Mucous Membrane (metabolism)</term><term>Neoplasms (metabolism)</term><term>Peptide Hydrolases (drug effects)</term><term>Peptide Hydrolases (metabolism)</term><term>Protein Binding</term><term>Rats</term><term>Surface Properties</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique</term><term>Animaux</term><term>Humains</term><term>Héparinoïde (pharmacologie)</term><term>Liaison aux protéines</term><term>Matrix metalloproteinase 7 (génétique)</term><term>Matrix metalloproteinase 7 (métabolisme)</term><term>Microscopie à force atomique</term><term>Modèles biologiques</term><term>Muqueuse (métabolisme)</term><term>Peptide hydrolases ()</term><term>Peptide hydrolases (métabolisme)</term><term>Propriétés de surface</term><term>Rats</term><term>Régulation allostérique</term><term>Tumeurs (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Matrix Metalloproteinase 7</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Matrix Metalloproteinase 7</term><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Heparinoids</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Matrix metalloproteinase 7</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mucous Membrane</term><term>Neoplasms</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Matrix metalloproteinase 7</term><term>Muqueuse</term><term>Peptide hydrolases</term><term>Tumeurs</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Héparinoïde</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term><term>Animals</term><term>Enzyme Activation</term><term>Humans</term><term>Microscopy, Atomic Force</term><term>Models, Biological</term><term>Protein Binding</term><term>Rats</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Animaux</term><term>Humains</term><term>Liaison aux protéines</term><term>Microscopie à force atomique</term><term>Modèles biologiques</term><term>Peptide hydrolases</term><term>Propriétés de surface</term><term>Rats</term><term>Régulation allostérique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Activation by glycosaminoglycans (GAGs) is an emerging trend among extracellular proteases important in disease. ProMMP-7, the zymogen of a matrix metalloproteinase secreted by mucosal epithelial and tumor cells, is activated at their surfaces by sulfated GAGs, but how? ProMMP-7 is activated in trans by representative heparin oligosaccharides in a length-dependent manner, with a large jump in activation at lengths of 16 monosaccharides. Imaging by atomic force microscopy visualized small complexes of proMMP-7 molecules linked by 8-mer lengths of heparinoids and extended assembles formed with 16-mer lengths of heparin. Complexes of proMMP-7 with polydisperse heparin or heparan sulfate were more diverse. Heparinoids evidently accelerate activation by tethering multiple proMMP-7 molecules together for proteolytic attack among neighbors. Removal of either the prodomain or C-terminal peptide sequence of KRSNSRKK from MMP-7 prevents formation of the long arrays induced by heparin 16-mers or heparan sulfate. The role of the C-terminus in activation assays suggests it contributes to remote, allosteric binding of GAGs. Enhancement of proteolytic velocity of MMP-by GAGs indicates them to be effectors of V-type allostery. GAGs from proteoglycans appear to assemble proMMP-7 molecules for activation, an event preceding its tumorigenic or antibacterial proteolytic activities at cell surfaces. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24495220</PMID><DateCompleted><Year>2015</Year><Month>07</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1554-8937</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>4</Issue><PubDate><Year>2014</Year><Month>Apr</Month><Day>18</Day></PubDate></JournalIssue><Title>ACS chemical biology</Title><ISOAbbreviation>ACS Chem. Biol.</ISOAbbreviation></Journal><ArticleTitle>Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.</ArticleTitle><Pagination><MedlinePgn>957-66</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/cb400898t</ELocationID><Abstract><AbstractText>Activation by glycosaminoglycans (GAGs) is an emerging trend among extracellular proteases important in disease. ProMMP-7, the zymogen of a matrix metalloproteinase secreted by mucosal epithelial and tumor cells, is activated at their surfaces by sulfated GAGs, but how? ProMMP-7 is activated in trans by representative heparin oligosaccharides in a length-dependent manner, with a large jump in activation at lengths of 16 monosaccharides. Imaging by atomic force microscopy visualized small complexes of proMMP-7 molecules linked by 8-mer lengths of heparinoids and extended assembles formed with 16-mer lengths of heparin. Complexes of proMMP-7 with polydisperse heparin or heparan sulfate were more diverse. Heparinoids evidently accelerate activation by tethering multiple proMMP-7 molecules together for proteolytic attack among neighbors. Removal of either the prodomain or C-terminal peptide sequence of KRSNSRKK from MMP-7 prevents formation of the long arrays induced by heparin 16-mers or heparan sulfate. The role of the C-terminus in activation assays suggests it contributes to remote, allosteric binding of GAGs. Enhancement of proteolytic velocity of MMP-by GAGs indicates them to be effectors of V-type allostery. GAGs from proteoglycans appear to assemble proMMP-7 molecules for activation, an event preceding its tumorigenic or antibacterial proteolytic activities at cell surfaces. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fulcher</LastName><ForeName>Yan G</ForeName><Initials>YG</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and ‡Department of Physics and Astronomy, University of Missouri , Columbia, Missouri 65211, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sanganna Gari</LastName><ForeName>Raghavendar Reddy</ForeName><Initials>RR</Initials></Author><Author ValidYN="Y"><LastName>Frey</LastName><ForeName>Nathan C</ForeName><Initials>NC</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Fuming</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Linhardt</LastName><ForeName>Robert J</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>King</LastName><ForeName>Gavin M</ForeName><Initials>GM</Initials></Author><Author ValidYN="Y"><LastName>Van Doren</LastName><ForeName>Steven R</ForeName><Initials>SR</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM057289</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>S10 RR022341</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01GM057289</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR022341</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>02</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>ACS Chem Biol</MedlineTA><NlmUniqueID>101282906</NlmUniqueID><ISSNLinking>1554-8929</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006496">Heparinoids</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.23</RegistryNumber><NameOfSubstance UI="D020783">Matrix Metalloproteinase 7</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000494" MajorTopicYN="N">Allosteric Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006496" MajorTopicYN="N">Heparinoids</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020783" MajorTopicYN="N">Matrix Metalloproteinase 7</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018625" MajorTopicYN="N">Microscopy, Atomic Force</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="Y">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009092" MajorTopicYN="N">Mucous Membrane</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009369" MajorTopicYN="N">Neoplasms</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013499" MajorTopicYN="N">Surface Properties</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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Frey</name><name sortKey="King, Gavin M" sort="King, Gavin M" uniqKey="King G" first="Gavin M" last="King">Gavin M. King</name><name sortKey="Linhardt, Robert J" sort="Linhardt, Robert J" uniqKey="Linhardt R" first="Robert J" last="Linhardt">Robert J. Linhardt</name><name sortKey="Sanganna Gari, Raghavendar Reddy" sort="Sanganna Gari, Raghavendar Reddy" uniqKey="Sanganna Gari R" first="Raghavendar Reddy" last="Sanganna Gari">Raghavendar Reddy Sanganna Gari</name><name sortKey="Van Doren, Steven R" sort="Van Doren, Steven R" uniqKey="Van Doren S" first="Steven R" last="Van Doren">Steven R. Van Doren</name><name sortKey="Zhang, Fuming" sort="Zhang, Fuming" uniqKey="Zhang F" first="Fuming" last="Zhang">Fuming Zhang</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Fulcher, Yan G" sort="Fulcher, Yan G" uniqKey="Fulcher Y" first="Yan G" last="Fulcher">Yan G. Fulcher</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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