liu.seSearch for publications in DiVA
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Heterozygosity for a Loss-of-Function Mutation in GALNT2 Improves Plasma Triglyceride Clearance in Man
Department of Vascular Medicine, Academic Medical Center, Amsterdam 1105AZ, The Netherlands.
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Yrkes- och miljömedicin. Linköpings universitet, Hälsouniversitetet. Östergötlands Läns Landsting, Hjärt- och Medicincentrum, Arbets- och miljömedicin.
Section on Biological Chemistry, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA.
Section on Biological Chemistry, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA.
Vise andre og tillknytning
2011 (engelsk)Inngår i: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 14, nr 6, s. 811-8Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Genome-wide association studies have identified GALNT2 as a candidate gene in lipid metabolism, but it is not known how the encoded enzyme ppGalNAc-T2, which contributes to the initiation of mucin-type O-linked glycosylation, mediates this effect. In two probands with elevated plasma high-density lipoprotein cholesterol and reduced triglycerides, we identified a mutation in GALNT2. It is shown that carriers have improved postprandial triglyceride clearance, which is likely attributable to attenuated glycosylation of apolipoprotein (apo) C-III, as observed in their plasma. This protein inhibits lipoprotein lipase (LPL), which hydrolyses plasma triglycerides. We show that an apoC-III-based peptide is a substrate for ppGalNAc-T2 while its glycosylation by the mutant enzyme is impaired. In addition, neuraminidase treatment of apoC-III which removes the sialic acids from its glycan chain decreases its potential to inhibit LPL. Combined, these data suggest that ppGalNAc-T2 can affect lipid metabolism through apoC-III glycosylation, thereby establishing GALNT2 as a lipid-modifying gene.

sted, utgiver, år, opplag, sider
Elsevier, 2011. Vol. 14, nr 6, s. 811-8
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-73069DOI: 10.1016/j.cmet.2011.11.005ISI: 000298122400014PubMedID: 22152306OAI: oai:DiVA.org:liu-73069DiVA, id: diva2:465755
Merknad

Funding agencies|European Union| FP6-2005-LIFESCIHEALTH-6 037631 |Fondation Leducq Transatlantic Networks of Excellence||NWO| 40-00506-98-9001 |National Institute of Dental and Craniofacial Research (NIDCR), National Institutes of Health||Netherlands Organisation for Scientific Research| 021.001.035 |Netherlands Heart Foundation| 2010T082 |

Tilgjengelig fra: 2011-12-15 Laget: 2011-12-15 Sist oppdatert: 2017-12-08bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstPubMed

Personposter BETA

Karlsson, HelenLjunggren, StefanLindahl, Mats

Søk i DiVA

Av forfatter/redaktør
Karlsson, HelenLjunggren, StefanLindahl, Mats
Av organisasjonen
I samme tidsskrift
Cell Metabolism

Søk utenfor DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 222 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf