Processing of Pro-Brain Natriuretic Peptide Is Suppressed by O-Glycosylation in the Region Close to the Cleavage Site
Processing of the brain natriuretic peptide (BNP) precursor, proBNP, is a convertase-dependent reaction that produces 2 molecules--the active BNP hormone and the N-terminal part of proBNP (NT-proBNP). Although proBNP was first described more than 15 years ago, very little is known about the cellular...
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| Veröffentlicht in: | Clinical chemistry (Baltimore, Md.) Md.), 2009-03, Vol.55 (3), p.489-498 |
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| creator | Semenov, Alexander G Postnikov, Alexander B Tamm, Natalia N Seferian, Karina R Karpova, Natalia S Bloshchitsyna, Marina N Koshkina, Ekaterina V Krasnoselsky, Mihail I Serebryanaya, Daria V Katrukha, Alexey G |
| description | Processing of the brain natriuretic peptide (BNP) precursor, proBNP, is a convertase-dependent reaction that produces 2 molecules--the active BNP hormone and the N-terminal part of proBNP (NT-proBNP). Although proBNP was first described more than 15 years ago, very little is known about the cellular mechanism of its processing. The study of proBNP processing mechanisms is important, because processing impairments could be associated with the development of heart failure (HF).
The biochemical properties of recombinant proBNP and NT-proBNP and the same molecules derived from the blood of HF patients were analyzed by gel-filtration chromatography, site-directed mutagenesis, and different immunochemical methods with a panel of monoclonal antibodies (MAbs).
Part of the proBNP molecule (amino acid residues 61-76) located near the cleavage site was inaccessible to specific MAbs because of the presence of O-glycans, whereas the same region in NT-proBNP was completely accessible. We demonstrated that a convertase (furin) could effectively cleave deglycosylated (but not intact) proBNP. Of several mutant proBNP forms produced in a HEK 293 cell line, only the T71A variant was effectively processed in the cell.
Only proBNP that was not glycosylated in the region of the cleavage site could effectively be processed into BNP and NT-proBNP. Site-directed mutagenesis enabled us to ascertain the unique suppressing role of T71-bound O-glycan in proBNP processing. |
| doi_str_mv | 10.1373/clinchem.2008.113373 |
| format | Article |
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The biochemical properties of recombinant proBNP and NT-proBNP and the same molecules derived from the blood of HF patients were analyzed by gel-filtration chromatography, site-directed mutagenesis, and different immunochemical methods with a panel of monoclonal antibodies (MAbs).
Part of the proBNP molecule (amino acid residues 61-76) located near the cleavage site was inaccessible to specific MAbs because of the presence of O-glycans, whereas the same region in NT-proBNP was completely accessible. We demonstrated that a convertase (furin) could effectively cleave deglycosylated (but not intact) proBNP. Of several mutant proBNP forms produced in a HEK 293 cell line, only the T71A variant was effectively processed in the cell.
Only proBNP that was not glycosylated in the region of the cleavage site could effectively be processed into BNP and NT-proBNP. Site-directed mutagenesis enabled us to ascertain the unique suppressing role of T71-bound O-glycan in proBNP processing.</description><identifier>ISSN: 0009-9147</identifier><identifier>EISSN: 1530-8561</identifier><identifier>DOI: 10.1373/clinchem.2008.113373</identifier><identifier>PMID: 19168558</identifier><identifier>CODEN: CLCHAU</identifier><language>eng</language><publisher>Washington, DC: Am Assoc Clin Chem</publisher><subject>Amino acids ; Animals ; Cell Line ; Cricetinae ; E coli ; Furin - metabolism ; Glycosylation ; Heart failure ; Humans ; Mice ; Mutagenesis ; Mutagenesis, Site-Directed ; Natriuretic Peptide, Brain - chemistry ; Natriuretic Peptide, Brain - genetics ; Natriuretic Peptide, Brain - immunology ; Natriuretic Peptide, Brain - metabolism ; Patients ; Protein Precursors - chemistry ; Protein Precursors - genetics ; Protein Precursors - immunology ; Protein Precursors - metabolism ; Studies</subject><ispartof>Clinical chemistry (Baltimore, Md.), 2009-03, Vol.55 (3), p.489-498</ispartof><rights>2009 INIST-CNRS</rights><rights>Copyright American Association for Clinical Chemistry Mar 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-9aa66bc557c5c01306bee6ec88e696434ae9411326006f4edf3ac16cca8eb5a33</citedby><cites>FETCH-LOGICAL-c504t-9aa66bc557c5c01306bee6ec88e696434ae9411326006f4edf3ac16cca8eb5a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21270034$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19168558$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Semenov, Alexander G</creatorcontrib><creatorcontrib>Postnikov, Alexander B</creatorcontrib><creatorcontrib>Tamm, Natalia N</creatorcontrib><creatorcontrib>Seferian, Karina R</creatorcontrib><creatorcontrib>Karpova, Natalia S</creatorcontrib><creatorcontrib>Bloshchitsyna, Marina N</creatorcontrib><creatorcontrib>Koshkina, Ekaterina V</creatorcontrib><creatorcontrib>Krasnoselsky, Mihail I</creatorcontrib><creatorcontrib>Serebryanaya, Daria V</creatorcontrib><creatorcontrib>Katrukha, Alexey G</creatorcontrib><title>Processing of Pro-Brain Natriuretic Peptide Is Suppressed by O-Glycosylation in the Region Close to the Cleavage Site</title><title>Clinical chemistry (Baltimore, Md.)</title><addtitle>Clin Chem</addtitle><description>Processing of the brain natriuretic peptide (BNP) precursor, proBNP, is a convertase-dependent reaction that produces 2 molecules--the active BNP hormone and the N-terminal part of proBNP (NT-proBNP). Although proBNP was first described more than 15 years ago, very little is known about the cellular mechanism of its processing. The study of proBNP processing mechanisms is important, because processing impairments could be associated with the development of heart failure (HF).
The biochemical properties of recombinant proBNP and NT-proBNP and the same molecules derived from the blood of HF patients were analyzed by gel-filtration chromatography, site-directed mutagenesis, and different immunochemical methods with a panel of monoclonal antibodies (MAbs).
Part of the proBNP molecule (amino acid residues 61-76) located near the cleavage site was inaccessible to specific MAbs because of the presence of O-glycans, whereas the same region in NT-proBNP was completely accessible. We demonstrated that a convertase (furin) could effectively cleave deglycosylated (but not intact) proBNP. Of several mutant proBNP forms produced in a HEK 293 cell line, only the T71A variant was effectively processed in the cell.
Only proBNP that was not glycosylated in the region of the cleavage site could effectively be processed into BNP and NT-proBNP. Site-directed mutagenesis enabled us to ascertain the unique suppressing role of T71-bound O-glycan in proBNP processing.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cricetinae</subject><subject>E coli</subject><subject>Furin - metabolism</subject><subject>Glycosylation</subject><subject>Heart failure</subject><subject>Humans</subject><subject>Mice</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Natriuretic Peptide, Brain - chemistry</subject><subject>Natriuretic Peptide, Brain - genetics</subject><subject>Natriuretic Peptide, Brain - immunology</subject><subject>Natriuretic Peptide, Brain - metabolism</subject><subject>Patients</subject><subject>Protein Precursors - chemistry</subject><subject>Protein Precursors - genetics</subject><subject>Protein Precursors - immunology</subject><subject>Protein Precursors - 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Md.)</jtitle><addtitle>Clin Chem</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>55</volume><issue>3</issue><spage>489</spage><epage>498</epage><pages>489-498</pages><issn>0009-9147</issn><eissn>1530-8561</eissn><coden>CLCHAU</coden><abstract>Processing of the brain natriuretic peptide (BNP) precursor, proBNP, is a convertase-dependent reaction that produces 2 molecules--the active BNP hormone and the N-terminal part of proBNP (NT-proBNP). Although proBNP was first described more than 15 years ago, very little is known about the cellular mechanism of its processing. The study of proBNP processing mechanisms is important, because processing impairments could be associated with the development of heart failure (HF).
The biochemical properties of recombinant proBNP and NT-proBNP and the same molecules derived from the blood of HF patients were analyzed by gel-filtration chromatography, site-directed mutagenesis, and different immunochemical methods with a panel of monoclonal antibodies (MAbs).
Part of the proBNP molecule (amino acid residues 61-76) located near the cleavage site was inaccessible to specific MAbs because of the presence of O-glycans, whereas the same region in NT-proBNP was completely accessible. We demonstrated that a convertase (furin) could effectively cleave deglycosylated (but not intact) proBNP. Of several mutant proBNP forms produced in a HEK 293 cell line, only the T71A variant was effectively processed in the cell.
Only proBNP that was not glycosylated in the region of the cleavage site could effectively be processed into BNP and NT-proBNP. Site-directed mutagenesis enabled us to ascertain the unique suppressing role of T71-bound O-glycan in proBNP processing.</abstract><cop>Washington, DC</cop><pub>Am Assoc Clin Chem</pub><pmid>19168558</pmid><doi>10.1373/clinchem.2008.113373</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0009-9147 |
| ispartof | Clinical chemistry (Baltimore, Md.), 2009-03, Vol.55 (3), p.489-498 |
| issn | 0009-9147 1530-8561 |
| language | eng |
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| source | MEDLINE; Oxford Journals |
| subjects | Amino acids Animals Cell Line Cricetinae E coli Furin - metabolism Glycosylation Heart failure Humans Mice Mutagenesis Mutagenesis, Site-Directed Natriuretic Peptide, Brain - chemistry Natriuretic Peptide, Brain - genetics Natriuretic Peptide, Brain - immunology Natriuretic Peptide, Brain - metabolism Patients Protein Precursors - chemistry Protein Precursors - genetics Protein Precursors - immunology Protein Precursors - metabolism Studies |
| title | Processing of Pro-Brain Natriuretic Peptide Is Suppressed by O-Glycosylation in the Region Close to the Cleavage Site |
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