Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A).
Identifieur interne : 004B71 ( Main/Exploration ); précédent : 004B70; suivant : 004B72Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A).
Auteurs : R. Malhotra [Royaume-Uni] ; J. Haurum ; S. Thiel ; J C Jensenius ; R B SimSource :
- Bioscience reports [ 0144-8463 ] ; 1993.
Descripteurs français
- KwdFr :
- Calcium (métabolisme), Humains (MeSH), Liaison aux protéines (MeSH), Lignée cellulaire (MeSH), Macrophages alvéolaires (métabolisme), Pollen (métabolisme), Protéine A associée au surfactant pulmonaire (MeSH), Protéines associées au surfactant pulmonaire (MeSH), Protéolipides (métabolisme), Surfactants pulmonaires (métabolisme).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Calcium, Proteolipids, Pulmonary Surfactants.
- metabolism : Macrophages, Alveolar, Pollen.
- Cell Line, Humans, Protein Binding, Pulmonary Surfactant-Associated Protein A, Pulmonary Surfactant-Associated Proteins.
Abstract
Lung surfactant protein A (SP-A) is the most abundant surfactant-associated protein present in the lung. A receptor for SP-A has been shown to be present on A549 alveolar type II cells and on other cell types, including alveolar macrophage. The SP-A receptor on A549 cells has been identified as the collection receptor, or C1q receptor, which binds several structurally-related ligands. SP-A contains C-type lectin domains, but the role of carbohydrate binding by SP-A in physiological and pathological phenomena is not yet established. In this paper we report the binding of SP-A to pollen from Populus nigra italica (Lombardy Poplar), Poa pratensis (Kentucky blue grass), Secale cerale (cultivated rye) and Ambrosia elatior (short ragweed). Saturable and concentration dependent binding of SP-A to pollen grains was observed. Interaction of SP-A with pollen grains takes place through water-extractable components, in which the major species present, in Lombardy polar pollen, are 57 kD and 7 kD (glyco)proteins. The binding of SP-A to pollen grains and their aqueous extracts was calcium ion dependent and was inhibited by mannose, and is therefore mediated by the lectin domain. Binding of SP-A to pollen grains was found to mediate adhesion of pollen grains to A549 cells. The results suggest that pollen grains or other carbohydrate-bearing particles (e.g. microorganisms) could potentially interact with different cell types via the collection receptor (C1q Receptor) in the presence of SP-A.
DOI: 10.1007/BF01145960
PubMed: 8374060
Affiliations:
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Thiel</name></author><author><name sortKey="Jensenius, J C" sort="Jensenius, J C" uniqKey="Jensenius J" first="J C" last="Jensenius">J C Jensenius</name></author><author><name sortKey="Sim, R B" sort="Sim, R B" uniqKey="Sim R" first="R B" last="Sim">R B Sim</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8374060</idno><idno type="pmid">8374060</idno><idno type="doi">10.1007/BF01145960</idno><idno type="wicri:Area/Main/Corpus">004B78</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004B78</idno><idno type="wicri:Area/Main/Curation">004B78</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004B78</idno><idno type="wicri:Area/Main/Exploration">004B78</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A).</title><author><name sortKey="Malhotra, R" sort="Malhotra, R" uniqKey="Malhotra R" first="R" last="Malhotra">R. Malhotra</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, University of Oxford, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biochemistry, University of Oxford</wicri:regionArea><placeName><settlement type="city">Oxford</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Oxfordshire</region></placeName><orgName type="university">Université d'Oxford</orgName></affiliation></author><author><name sortKey="Haurum, J" sort="Haurum, J" uniqKey="Haurum J" first="J" last="Haurum">J. Haurum</name></author><author><name sortKey="Thiel, S" sort="Thiel, S" uniqKey="Thiel S" first="S" last="Thiel">S. Thiel</name></author><author><name sortKey="Jensenius, J C" sort="Jensenius, J C" uniqKey="Jensenius J" first="J C" last="Jensenius">J C Jensenius</name></author><author><name sortKey="Sim, R B" sort="Sim, R B" uniqKey="Sim R" first="R B" last="Sim">R B Sim</name></author></analytic><series><title level="j">Bioscience reports</title><idno type="ISSN">0144-8463</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Calcium (metabolism)</term><term>Cell Line (MeSH)</term><term>Humans (MeSH)</term><term>Macrophages, Alveolar (metabolism)</term><term>Pollen (metabolism)</term><term>Protein Binding (MeSH)</term><term>Proteolipids (metabolism)</term><term>Pulmonary Surfactant-Associated Protein A (MeSH)</term><term>Pulmonary Surfactant-Associated Proteins (MeSH)</term><term>Pulmonary Surfactants (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Calcium (métabolisme)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Macrophages alvéolaires (métabolisme)</term><term>Pollen (métabolisme)</term><term>Protéine A associée au surfactant pulmonaire (MeSH)</term><term>Protéines associées au surfactant pulmonaire (MeSH)</term><term>Protéolipides (métabolisme)</term><term>Surfactants pulmonaires (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Proteolipids</term><term>Pulmonary Surfactants</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Macrophages, Alveolar</term><term>Pollen</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calcium</term><term>Macrophages alvéolaires</term><term>Pollen</term><term>Protéolipides</term><term>Surfactants pulmonaires</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Protein Binding</term><term>Pulmonary Surfactant-Associated Protein A</term><term>Pulmonary Surfactant-Associated Proteins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéine A associée au surfactant pulmonaire</term><term>Protéines associées au surfactant pulmonaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lung surfactant protein A (SP-A) is the most abundant surfactant-associated protein present in the lung. A receptor for SP-A has been shown to be present on A549 alveolar type II cells and on other cell types, including alveolar macrophage. The SP-A receptor on A549 cells has been identified as the collection receptor, or C1q receptor, which binds several structurally-related ligands. SP-A contains C-type lectin domains, but the role of carbohydrate binding by SP-A in physiological and pathological phenomena is not yet established. In this paper we report the binding of SP-A to pollen from Populus nigra italica (Lombardy Poplar), Poa pratensis (Kentucky blue grass), Secale cerale (cultivated rye) and Ambrosia elatior (short ragweed). Saturable and concentration dependent binding of SP-A to pollen grains was observed. Interaction of SP-A with pollen grains takes place through water-extractable components, in which the major species present, in Lombardy polar pollen, are 57 kD and 7 kD (glyco)proteins. The binding of SP-A to pollen grains and their aqueous extracts was calcium ion dependent and was inhibited by mannose, and is therefore mediated by the lectin domain. Binding of SP-A to pollen grains was found to mediate adhesion of pollen grains to A549 cells. The results suggest that pollen grains or other carbohydrate-bearing particles (e.g. microorganisms) could potentially interact with different cell types via the collection receptor (C1q Receptor) in the presence of SP-A.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8374060</PMID><DateCompleted><Year>1993</Year><Month>10</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>06</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0144-8463</ISSN><JournalIssue CitedMedium="Print"><Volume>13</Volume><Issue>2</Issue><PubDate><Year>1993</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Bioscience reports</Title><ISOAbbreviation>Biosci Rep</ISOAbbreviation></Journal><ArticleTitle>Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A).</ArticleTitle><Pagination><MedlinePgn>79-90</MedlinePgn></Pagination><Abstract><AbstractText>Lung surfactant protein A (SP-A) is the most abundant surfactant-associated protein present in the lung. A receptor for SP-A has been shown to be present on A549 alveolar type II cells and on other cell types, including alveolar macrophage. The SP-A receptor on A549 cells has been identified as the collection receptor, or C1q receptor, which binds several structurally-related ligands. SP-A contains C-type lectin domains, but the role of carbohydrate binding by SP-A in physiological and pathological phenomena is not yet established. In this paper we report the binding of SP-A to pollen from Populus nigra italica (Lombardy Poplar), Poa pratensis (Kentucky blue grass), Secale cerale (cultivated rye) and Ambrosia elatior (short ragweed). Saturable and concentration dependent binding of SP-A to pollen grains was observed. Interaction of SP-A with pollen grains takes place through water-extractable components, in which the major species present, in Lombardy polar pollen, are 57 kD and 7 kD (glyco)proteins. The binding of SP-A to pollen grains and their aqueous extracts was calcium ion dependent and was inhibited by mannose, and is therefore mediated by the lectin domain. Binding of SP-A to pollen grains was found to mediate adhesion of pollen grains to A549 cells. The results suggest that pollen grains or other carbohydrate-bearing particles (e.g. microorganisms) could potentially interact with different cell types via the collection receptor (C1q Receptor) in the presence of SP-A.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Malhotra</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Oxford, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Haurum</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Thiel</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Jensenius</LastName><ForeName>J C</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Sim</LastName><ForeName>R B</ForeName><Initials>RB</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>England</Country><MedlineTA>Biosci Rep</MedlineTA><NlmUniqueID>8102797</NlmUniqueID><ISSNLinking>0144-8463</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011510">Proteolipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037662">Pulmonary Surfactant-Associated Protein A</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037661">Pulmonary Surfactant-Associated Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011663">Pulmonary Surfactants</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016676" MajorTopicYN="N">Macrophages, Alveolar</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011058" MajorTopicYN="N">Pollen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011510" MajorTopicYN="N">Proteolipids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D037662" MajorTopicYN="N">Pulmonary Surfactant-Associated Protein A</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037661" MajorTopicYN="N">Pulmonary Surfactant-Associated Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011663" MajorTopicYN="N">Pulmonary Surfactants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>4</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8374060</ArticleId><ArticleId IdType="doi">10.1007/BF01145960</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Oxfordshire</li></region><settlement><li>Oxford</li></settlement><orgName><li>Université d'Oxford</li></orgName></list><tree><noCountry><name sortKey="Haurum, J" sort="Haurum, J" uniqKey="Haurum J" first="J" last="Haurum">J. Haurum</name><name sortKey="Jensenius, J C" sort="Jensenius, J C" uniqKey="Jensenius J" first="J C" last="Jensenius">J C Jensenius</name><name sortKey="Sim, R B" sort="Sim, R B" uniqKey="Sim R" first="R B" last="Sim">R B Sim</name><name sortKey="Thiel, S" sort="Thiel, S" uniqKey="Thiel S" first="S" last="Thiel">S. Thiel</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Malhotra, R" sort="Malhotra, R" uniqKey="Malhotra R" first="R" last="Malhotra">R. Malhotra</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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