Matches in SemOpenAlex for { <https://semopenalex.org/work/W2952696651> ?p ?o ?g. }
- W2952696651 endingPage "12578" @default.
- W2952696651 startingPage "12567" @default.
- W2952696651 abstract "Atrial natriuretic peptide (ANP) is a peptide hormone that in response to atrial stretch is secreted from atrial myocytes into the circulation, where it stimulates vasodilatation and natriuresis. ANP is an important biomarker of heart failure where low plasma concentrations exclude cardiac dysfunction. ANP is a member of the natriuretic peptide (NP) family, which also includes the B-type natriuretic peptide (BNP) and the C-type natriuretic peptide. The proforms of these hormones undergo processing to mature peptides, and for proBNP, this process has previously been demonstrated to be regulated by O-glycosylation. It has been suggested that proANP also may undergo post-translational modifications. Here, we conducted a targeted O-glycoproteomics approach to characterize O-glycans on NPs and demonstrate that all NP members can carry O-glycans. We identified four O-glycosites in proANP in the porcine heart, and surprisingly, two of these were located on the mature bioactive ANP itself. We found that one of these glycans is located within a conserved sequence motif of the receptor-binding region, suggesting that O-glycans may serve a function beyond intracellular processing and maturation. We also identified an O-glycoform of proANP naturally occurring in human circulation. We demonstrated that site-specific O-glycosylation shields bioactive ANP from proteolytic degradation and modifies potency at its cognate receptor in vitro. Furthermore, we showed that ANP O-glycosylation attenuates acute renal and cardiovascular ANP actions in vivo. The discovery of novel glycosylated ANP proteoforms reported here significantly improves our understanding of cardiac endocrinology and provides important insight into the etiology of heart failure. Atrial natriuretic peptide (ANP) is a peptide hormone that in response to atrial stretch is secreted from atrial myocytes into the circulation, where it stimulates vasodilatation and natriuresis. ANP is an important biomarker of heart failure where low plasma concentrations exclude cardiac dysfunction. ANP is a member of the natriuretic peptide (NP) family, which also includes the B-type natriuretic peptide (BNP) and the C-type natriuretic peptide. The proforms of these hormones undergo processing to mature peptides, and for proBNP, this process has previously been demonstrated to be regulated by O-glycosylation. It has been suggested that proANP also may undergo post-translational modifications. Here, we conducted a targeted O-glycoproteomics approach to characterize O-glycans on NPs and demonstrate that all NP members can carry O-glycans. We identified four O-glycosites in proANP in the porcine heart, and surprisingly, two of these were located on the mature bioactive ANP itself. We found that one of these glycans is located within a conserved sequence motif of the receptor-binding region, suggesting that O-glycans may serve a function beyond intracellular processing and maturation. We also identified an O-glycoform of proANP naturally occurring in human circulation. We demonstrated that site-specific O-glycosylation shields bioactive ANP from proteolytic degradation and modifies potency at its cognate receptor in vitro. Furthermore, we showed that ANP O-glycosylation attenuates acute renal and cardiovascular ANP actions in vivo. The discovery of novel glycosylated ANP proteoforms reported here significantly improves our understanding of cardiac endocrinology and provides important insight into the etiology of heart failure. Sweet rescue or surrender of the failing heart?Journal of Biological ChemistryVol. 294Issue 34PreviewNatriuretic peptides (NPs) are hormones involved in maintaining heart health that undergo proteolytic cleavage to become activated. Previous work has shown that O-GalNAc glycans affect their processing and activation. Here, Goetze, Schjoldager, and colleagues now provide comprehensive characterization of O-glycosylation of NPs, revealing that all members of the NP family can be modified by O-GalNAc glycans. Intriguingly, the study discovers glycans in the receptor-binding region of the A-type natriuretic peptide (ANP), demonstrating that they affect both stability and activity of ANP. Full-Text PDF Open AccessCorrection: Discovery of O-glycans on atrial natriuretic peptide (ANP) that affect both its proteolytic degradation and potency at its cognate receptor.Journal of Biological ChemistryVol. 294Issue 48PreviewVOLUME 294 (2019) PAGES 12567–12578 Full-Text PDF Open Access" @default.
- W2952696651 created "2019-06-27" @default.
- W2952696651 creator A5004749753 @default.
- W2952696651 creator A5014193048 @default.
- W2952696651 creator A5020819058 @default.
- W2952696651 creator A5030965826 @default.
- W2952696651 creator A5033121898 @default.
- W2952696651 creator A5050737891 @default.
- W2952696651 creator A5051362053 @default.
- W2952696651 creator A5058714848 @default.
- W2952696651 creator A5064422018 @default.
- W2952696651 creator A5085229618 @default.
- W2952696651 creator A5085537512 @default.
- W2952696651 creator A5088428038 @default.
- W2952696651 creator A5091343644 @default.
- W2952696651 date "2019-08-01" @default.
- W2952696651 modified "2023-09-30" @default.
- W2952696651 title "Discovery of O-glycans on atrial natriuretic peptide (ANP) that affect both its proteolytic degradation and potency at its cognate receptor" @default.
- W2952696651 cites W128566464 @default.
- W2952696651 cites W1524757395 @default.
- W2952696651 cites W1599602246 @default.
- W2952696651 cites W1836315310 @default.
- W2952696651 cites W1912014122 @default.
- W2952696651 cites W1968740258 @default.
- W2952696651 cites W1970052428 @default.
- W2952696651 cites W1972059691 @default.
- W2952696651 cites W1977091587 @default.
- W2952696651 cites W1982655905 @default.
- W2952696651 cites W1994035387 @default.
- W2952696651 cites W1994968159 @default.
- W2952696651 cites W1995901724 @default.
- W2952696651 cites W2004160810 @default.
- W2952696651 cites W2004795993 @default.
- W2952696651 cites W2016870770 @default.
- W2952696651 cites W2020888535 @default.
- W2952696651 cites W2031522662 @default.
- W2952696651 cites W2044657479 @default.
- W2952696651 cites W2050254620 @default.
- W2952696651 cites W2050934730 @default.
- W2952696651 cites W2062489834 @default.
- W2952696651 cites W2064439430 @default.
- W2952696651 cites W2067878343 @default.
- W2952696651 cites W2070387845 @default.
- W2952696651 cites W2070988759 @default.
- W2952696651 cites W2072918899 @default.
- W2952696651 cites W2076863893 @default.
- W2952696651 cites W2080132669 @default.
- W2952696651 cites W2082073015 @default.
- W2952696651 cites W2093359457 @default.
- W2952696651 cites W2093885131 @default.
- W2952696651 cites W2108050723 @default.
- W2952696651 cites W2112486118 @default.
- W2952696651 cites W2113407718 @default.
- W2952696651 cites W2113698123 @default.
- W2952696651 cites W2126836757 @default.
- W2952696651 cites W2131202471 @default.
- W2952696651 cites W2133828435 @default.
- W2952696651 cites W2135521686 @default.
- W2952696651 cites W2137548222 @default.
- W2952696651 cites W2143094666 @default.
- W2952696651 cites W2145706297 @default.
- W2952696651 cites W2145949970 @default.
- W2952696651 cites W2150124834 @default.
- W2952696651 cites W2151296542 @default.
- W2952696651 cites W2155400583 @default.
- W2952696651 cites W2160117282 @default.
- W2952696651 cites W2174724991 @default.
- W2952696651 cites W2318095071 @default.
- W2952696651 cites W2336203885 @default.
- W2952696651 cites W2417864863 @default.
- W2952696651 cites W2501970118 @default.
- W2952696651 cites W2552004905 @default.
- W2952696651 cites W2586116403 @default.
- W2952696651 cites W2591498323 @default.
- W2952696651 cites W2615422437 @default.
- W2952696651 cites W2745266801 @default.
- W2952696651 cites W2762697433 @default.
- W2952696651 cites W2778043429 @default.
- W2952696651 cites W2790360534 @default.
- W2952696651 cites W2838250877 @default.
- W2952696651 cites W2896143972 @default.
- W2952696651 cites W2929395653 @default.
- W2952696651 doi "https://doi.org/10.1074/jbc.ra119.008102" @default.
- W2952696651 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6885629" @default.
- W2952696651 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31784477" @default.
- W2952696651 hasPublicationYear "2019" @default.
- W2952696651 type Work @default.
- W2952696651 sameAs 2952696651 @default.
- W2952696651 citedByCount "39" @default.
- W2952696651 countsByYear W29526966512019 @default.
- W2952696651 countsByYear W29526966512020 @default.
- W2952696651 countsByYear W29526966512021 @default.
- W2952696651 countsByYear W29526966512022 @default.
- W2952696651 countsByYear W29526966512023 @default.
- W2952696651 crossrefType "journal-article" @default.
- W2952696651 hasAuthorship W2952696651A5004749753 @default.
- W2952696651 hasAuthorship W2952696651A5014193048 @default.
- W2952696651 hasAuthorship W2952696651A5020819058 @default.