Recombinant pulmonary surfactant protein D. Post-translational modification and molecular assembly.
Identifieur interne : 002978 ( Ncbi/Merge ); précédent : 002977; suivant : 002979Recombinant pulmonary surfactant protein D. Post-translational modification and molecular assembly.
Auteurs : E. Crouch [États-Unis] ; D. Chang ; K. Rust ; A. Persson ; J. HeuserSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1994.
Descripteurs français
- KwdFr :
- Acides aminés (analyse), Agglutination, Animaux, Cartographie de restriction, Cellules CHO, Chromatographie sur gel, Cricetinae, Escherichia coli, Glycoprotéines (biosynthèse), Glycoprotéines (isolement et purification), Glycoprotéines (ultrastructure), Masse moléculaire, Maturation post-traductionnelle des protéines, Microscopie électronique, Protéine D associée au surfactant pulmonaire, Protéines recombinantes (biosynthèse), Protéines recombinantes (isolement et purification), Protéines recombinantes (ultrastructure), Rats, Surfactants pulmonaires (biosynthèse), Surfactants pulmonaires (isolement et purification), Surfactants pulmonaires (ultrastructure), Transfection, Vecteurs génétiques, Électrophorèse sur gel de polyacrylamide.
- MESH :
- analyse : Acides aminés.
- biosynthèse : Glycoprotéines, Protéines recombinantes, Surfactants pulmonaires.
- isolement et purification : Glycoprotéines, Protéines recombinantes, Surfactants pulmonaires.
- ultrastructure : Glycoprotéines, Protéines recombinantes, Surfactants pulmonaires.
- Agglutination, Animaux, Cartographie de restriction, Cellules CHO, Chromatographie sur gel, Cricetinae, Escherichia coli, Masse moléculaire, Maturation post-traductionnelle des protéines, Microscopie électronique, Protéine D associée au surfactant pulmonaire, Rats, Transfection, Vecteurs génétiques, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Agglutination, Amino Acids (analysis), Animals, CHO Cells, Chromatography, Gel, Cricetinae, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Genetic Vectors, Glycoproteins (biosynthesis), Glycoproteins (isolation & purification), Glycoproteins (ultrastructure), Microscopy, Electron, Molecular Weight, Protein Processing, Post-Translational, Pulmonary Surfactant-Associated Protein D, Pulmonary Surfactants (biosynthesis), Pulmonary Surfactants (isolation & purification), Pulmonary Surfactants (ultrastructure), Rats, Recombinant Proteins (biosynthesis), Recombinant Proteins (isolation & purification), Recombinant Proteins (ultrastructure), Restriction Mapping, Transfection.
- MESH :
- chemical , analysis : Amino Acids.
- chemical , biosynthesis : Glycoproteins, Pulmonary Surfactants, Recombinant Proteins.
- chemical , isolation & purification : Glycoproteins, Pulmonary Surfactants, Recombinant Proteins.
- chemical , ultrastructure : Glycoproteins, Pulmonary Surfactants, Recombinant Proteins.
- Agglutination, Animals, CHO Cells, Chromatography, Gel, Cricetinae, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Genetic Vectors, Microscopy, Electron, Molecular Weight, Protein Processing, Post-Translational, Pulmonary Surfactant-Associated Protein D, Rats, Restriction Mapping, Transfection.
Abstract
Pulmonary surfactant protein D (SP-D) is a member of a family of collagenous C-type lectins that includes the serum mannose binding proteins and surfactant protein A. Recent studies have shown that rat SP-D (rSP-D) molecules are assembled as tetramers of trimeric subunits (12 mers) and that dodecamers can participate in higher orders of molecular assembly involving interactions of the amino-terminal peptide domains. In order to further study the assembly of SP-D in vitro, Chinese hamster ovary K1 cells were transfected with a full-length rat SP-D cDNA, and stable transfectants with high levels of SP-D production (approximately 6 x 10(6) dodecamers/cell/24 h) were obtained using a glutamine synthetase selection system. The secreted molecules (RrSP-D), which were purified by affinity chromatography on maltosyl-agarose, comigrated with rSP-D on SDS-polyacrylamide gel electrophoresis in the presence and absence of reduction, and coeluted with rSP-D dodecamers from 4% agarose. The major bacterial collagenase-resistant peptide showed a decreased mobility on reduction consistent with the formation of intrachain disulfide bonds. A 17-kDa pepsin-resistant fragment was isolated following overnight digestion with pepsin at 27 degrees C, confirming the formation of a triple helical domain comparable in size and thermal stability to that of natural SP-D. The expressed protein contained sialylated endoglycosidase F-sensitive carbohydrate; amino acid analysis of acid and alkaline hydrolysates demonstrated essentially normal levels of hydroxyproline, hydroxylysine, and hydroxylysine-glycosides. Electron microscopic studies showed a molecular structure indistinguishable from lung SP-D, with a similar small subpopulation of molecules showing higher orders of multimerization. Solid-phase neoglycoprotein binding assays gave the same saccharide inhibition profile as natural rat SP-D, and both proteins showed efficient saccharide-dependent agglutination of Escherichia coli. These studies demonstrate that a single genetically distinct chain type can account for the various and complex molecular assemblies of SP-D, and further verify the potential physiologic significance of the disulfide-bonded multimers and higher aggregates isolated from rat, bovine, and human lung lavage.
PubMed: 8195236
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002876
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Links to Exploration step
pubmed:8195236Le document en format XML
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<term>Amino Acids (analysis)</term>
<term>Animals</term>
<term>CHO Cells</term>
<term>Chromatography, Gel</term>
<term>Cricetinae</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Escherichia coli</term>
<term>Genetic Vectors</term>
<term>Glycoproteins (biosynthesis)</term>
<term>Glycoproteins (isolation & purification)</term>
<term>Glycoproteins (ultrastructure)</term>
<term>Microscopy, Electron</term>
<term>Molecular Weight</term>
<term>Protein Processing, Post-Translational</term>
<term>Pulmonary Surfactant-Associated Protein D</term>
<term>Pulmonary Surfactants (biosynthesis)</term>
<term>Pulmonary Surfactants (isolation & purification)</term>
<term>Pulmonary Surfactants (ultrastructure)</term>
<term>Rats</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Recombinant Proteins (isolation & purification)</term>
<term>Recombinant Proteins (ultrastructure)</term>
<term>Restriction Mapping</term>
<term>Transfection</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (analyse)</term>
<term>Agglutination</term>
<term>Animaux</term>
<term>Cartographie de restriction</term>
<term>Cellules CHO</term>
<term>Chromatographie sur gel</term>
<term>Cricetinae</term>
<term>Escherichia coli</term>
<term>Glycoprotéines (biosynthèse)</term>
<term>Glycoprotéines (isolement et purification)</term>
<term>Glycoprotéines (ultrastructure)</term>
<term>Masse moléculaire</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Microscopie électronique</term>
<term>Protéine D associée au surfactant pulmonaire</term>
<term>Protéines recombinantes (biosynthèse)</term>
<term>Protéines recombinantes (isolement et purification)</term>
<term>Protéines recombinantes (ultrastructure)</term>
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<term>Surfactants pulmonaires (isolement et purification)</term>
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<term>Transfection</term>
<term>Vecteurs génétiques</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<term>Recombinant Proteins</term>
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<term>Pulmonary Surfactants</term>
<term>Recombinant Proteins</term>
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<term>Protéines recombinantes</term>
<term>Surfactants pulmonaires</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Glycoprotéines</term>
<term>Protéines recombinantes</term>
<term>Surfactants pulmonaires</term>
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<term>Protéines recombinantes</term>
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<term>Animals</term>
<term>CHO Cells</term>
<term>Chromatography, Gel</term>
<term>Cricetinae</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Escherichia coli</term>
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<term>Protein Processing, Post-Translational</term>
<term>Pulmonary Surfactant-Associated Protein D</term>
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<term>Restriction Mapping</term>
<term>Transfection</term>
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<term>Animaux</term>
<term>Cartographie de restriction</term>
<term>Cellules CHO</term>
<term>Chromatographie sur gel</term>
<term>Cricetinae</term>
<term>Escherichia coli</term>
<term>Masse moléculaire</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Microscopie électronique</term>
<term>Protéine D associée au surfactant pulmonaire</term>
<term>Rats</term>
<term>Transfection</term>
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<front><div type="abstract" xml:lang="en">Pulmonary surfactant protein D (SP-D) is a member of a family of collagenous C-type lectins that includes the serum mannose binding proteins and surfactant protein A. Recent studies have shown that rat SP-D (rSP-D) molecules are assembled as tetramers of trimeric subunits (12 mers) and that dodecamers can participate in higher orders of molecular assembly involving interactions of the amino-terminal peptide domains. In order to further study the assembly of SP-D in vitro, Chinese hamster ovary K1 cells were transfected with a full-length rat SP-D cDNA, and stable transfectants with high levels of SP-D production (approximately 6 x 10(6) dodecamers/cell/24 h) were obtained using a glutamine synthetase selection system. The secreted molecules (RrSP-D), which were purified by affinity chromatography on maltosyl-agarose, comigrated with rSP-D on SDS-polyacrylamide gel electrophoresis in the presence and absence of reduction, and coeluted with rSP-D dodecamers from 4% agarose. The major bacterial collagenase-resistant peptide showed a decreased mobility on reduction consistent with the formation of intrachain disulfide bonds. A 17-kDa pepsin-resistant fragment was isolated following overnight digestion with pepsin at 27 degrees C, confirming the formation of a triple helical domain comparable in size and thermal stability to that of natural SP-D. The expressed protein contained sialylated endoglycosidase F-sensitive carbohydrate; amino acid analysis of acid and alkaline hydrolysates demonstrated essentially normal levels of hydroxyproline, hydroxylysine, and hydroxylysine-glycosides. Electron microscopic studies showed a molecular structure indistinguishable from lung SP-D, with a similar small subpopulation of molecules showing higher orders of multimerization. Solid-phase neoglycoprotein binding assays gave the same saccharide inhibition profile as natural rat SP-D, and both proteins showed efficient saccharide-dependent agglutination of Escherichia coli. These studies demonstrate that a single genetically distinct chain type can account for the various and complex molecular assemblies of SP-D, and further verify the potential physiologic significance of the disulfide-bonded multimers and higher aggregates isolated from rat, bovine, and human lung lavage.</div>
</front>
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<Abstract><AbstractText>Pulmonary surfactant protein D (SP-D) is a member of a family of collagenous C-type lectins that includes the serum mannose binding proteins and surfactant protein A. Recent studies have shown that rat SP-D (rSP-D) molecules are assembled as tetramers of trimeric subunits (12 mers) and that dodecamers can participate in higher orders of molecular assembly involving interactions of the amino-terminal peptide domains. In order to further study the assembly of SP-D in vitro, Chinese hamster ovary K1 cells were transfected with a full-length rat SP-D cDNA, and stable transfectants with high levels of SP-D production (approximately 6 x 10(6) dodecamers/cell/24 h) were obtained using a glutamine synthetase selection system. The secreted molecules (RrSP-D), which were purified by affinity chromatography on maltosyl-agarose, comigrated with rSP-D on SDS-polyacrylamide gel electrophoresis in the presence and absence of reduction, and coeluted with rSP-D dodecamers from 4% agarose. The major bacterial collagenase-resistant peptide showed a decreased mobility on reduction consistent with the formation of intrachain disulfide bonds. A 17-kDa pepsin-resistant fragment was isolated following overnight digestion with pepsin at 27 degrees C, confirming the formation of a triple helical domain comparable in size and thermal stability to that of natural SP-D. The expressed protein contained sialylated endoglycosidase F-sensitive carbohydrate; amino acid analysis of acid and alkaline hydrolysates demonstrated essentially normal levels of hydroxyproline, hydroxylysine, and hydroxylysine-glycosides. Electron microscopic studies showed a molecular structure indistinguishable from lung SP-D, with a similar small subpopulation of molecules showing higher orders of multimerization. Solid-phase neoglycoprotein binding assays gave the same saccharide inhibition profile as natural rat SP-D, and both proteins showed efficient saccharide-dependent agglutination of Escherichia coli. These studies demonstrate that a single genetically distinct chain type can account for the various and complex molecular assemblies of SP-D, and further verify the potential physiologic significance of the disulfide-bonded multimers and higher aggregates isolated from rat, bovine, and human lung lavage.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Crouch</LastName>
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<MeshHeading><DescriptorName UI="D037663" MajorTopicYN="N">Pulmonary Surfactant-Associated Protein D</DescriptorName>
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<MeshHeading><DescriptorName UI="D011663" MajorTopicYN="N">Pulmonary Surfactants</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
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<MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName>
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<MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName>
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<tree><noCountry><name sortKey="Chang, D" sort="Chang, D" uniqKey="Chang D" first="D" last="Chang">D. Chang</name>
<name sortKey="Heuser, J" sort="Heuser, J" uniqKey="Heuser J" first="J" last="Heuser">J. Heuser</name>
<name sortKey="Persson, A" sort="Persson, A" uniqKey="Persson A" first="A" last="Persson">A. Persson</name>
<name sortKey="Rust, K" sort="Rust, K" uniqKey="Rust K" first="K" last="Rust">K. Rust</name>
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<country name="États-Unis"><region name="Missouri (État)"><name sortKey="Crouch, E" sort="Crouch, E" uniqKey="Crouch E" first="E" last="Crouch">E. Crouch</name>
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