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- Vakhrushev, Sergey YRemove Vakhrushev, Sergey Y filter
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Please choose a date range between 2018 and 2019.
Author
- Goth, Christoffer K2
- Schjoldager, Katrine T2
- Wandall, Hans H2
- Bennett, Eric P1
- Burnett, John C Jr1
- Chen, Yang1
- Clausen, Henrik1
- Dabelsteen, Sally1
- Dylander, August1
- Dzhoyashvili, Nina1
- Eckhard, Ulrich1
- Frödin, Morten1
- Goetze, Jens P1
- Hansen, Lars1
- Hansen, Lasse H1
- Haue, Amalie D1
- Haue, Amalie Dahl1
- Iyer, Seethalakshmi R1
- Joshi, Hiren J1
- King, Sarah L1
- Lavrsen, Kirstine1
- Levann, Asha MR1
- Madsen, Thomas Daugbjerg1
- Mandel, Ulla1
Keyword
- post-translational modification (PTM)2
- blood pressure1
- cancer biology1
- cardiovascular1
- cardiovascular disease1
- cell adhesion1
- colon cancer1
- differentiation1
- GalNAc1
- GalNAc-T21
- GalNAc-Ts1
- genetic engineering1
- glycoprotein1
- glycoproteomics1
- glycosylation1
- heart1
- heart failure1
- metalloprotease1
- natriuresis1
- natriuretic peptide1
- peptide hormone1
- protease inhibitor1
- Proteolytic processing1
- proteomics1
Glycobiology and Extracellular Matrices
3 Results
- Editors' PicksOpen Access
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 34p12567–12578Published online: August 23, 2019- Lasse H. Hansen
- Thomas Daugbjerg Madsen
- Christoffer K. Goth
- Henrik Clausen
- Yang Chen
- Nina Dzhoyashvili
- and others
Cited in Scopus: 34Atrial 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. - Cell BiologyOpen Access
TAILS N-terminomics and proteomics reveal complex regulation of proteolytic cleavage by O-glycosylation
Journal of Biological ChemistryVol. 293Issue 20p7629–7644Published online: March 28, 2018- Sarah L. King
- Christoffer K. Goth
- Ulrich Eckhard
- Hiren J. Joshi
- Amalie D. Haue
- Sergey Y. Vakhrushev
- and others
Cited in Scopus: 19Proteolytic processing is an irreversible post-translational modification functioning as a ubiquitous regulator of cellular activity. Protease activity is tightly regulated via control of gene expression, enzyme and substrate compartmentalization, zymogen activation, enzyme inactivation, and substrate availability. Emerging evidence suggests that proteolysis can also be regulated by substrate glycosylation and that glycosylation of individual sites on a substrate can decrease or, in rare cases, increase its sensitivity to proteolysis. - Editors' PicksOpen Access
De novo expression of human polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6) in colon adenocarcinoma inhibits the differentiation of colonic epithelium
Journal of Biological ChemistryVol. 293Issue 4p1298–1314Published online: November 29, 2017- Kirstine Lavrsen
- Sally Dabelsteen
- Sergey Y. Vakhrushev
- Asha M.R. Levann
- Amalie Dahl Haue
- August Dylander
- and others
Cited in Scopus: 45Aberrant expression of O-glycans is a hallmark of epithelial cancers. Mucin-type O-glycosylation is initiated by a large family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) that target different proteins and are differentially expressed in cells and organs. Here, we investigated the expression patterns of all of the GalNAc-Ts in colon cancer by analyzing transcriptomic data. We found that GalNAc-T6 was highly up-regulated in colon adenocarcinomas but absent in normal-appearing adjacent colon tissue.