Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1013912#aggregation> ?p ?o. }
Showing items 1 to 45 of
45
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B383078.
- aggregation creator B383079.
- aggregation creator B383080.
- aggregation creator B383081.
- aggregation creator B383082.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2010".
- aggregation format "application/pdf".
- aggregation hasFormat 1013912.bibtex.
- aggregation hasFormat 1013912.csv.
- aggregation hasFormat 1013912.dc.
- aggregation hasFormat 1013912.didl.
- aggregation hasFormat 1013912.doc.
- aggregation hasFormat 1013912.json.
- aggregation hasFormat 1013912.mets.
- aggregation hasFormat 1013912.mods.
- aggregation hasFormat 1013912.rdf.
- aggregation hasFormat 1013912.ris.
- aggregation hasFormat 1013912.txt.
- aggregation hasFormat 1013912.xls.
- aggregation hasFormat 1013912.yaml.
- aggregation isPartOf urn:issn:0023-6837.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Medicine and Health Sciences".
- aggregation title "Low serum vitamin K in PXE results in defective carboxylation of mineralization inhibitors similar to the GGCX mutations in the PXE-like syndrome".
- aggregation abstract "Soft-tissue mineralization is a tightly regulated process relying on the activity of systemic and tissue-specific inhibitors and promoters of calcium precipitation. Many of these, such as matrix gla protein (MGP) and osteocalcin (OC), need to undergo carboxylation to become active. This post-translational modification is catalyzed by the gammaglutamyl carboxylase GGCX and requires vitamin K (VK) as an essential co-factor. Recently, we described a novel phenotype characterized by aberrant mineralization of the elastic fibers resulting from mutations in GGCX. Because of the resemblance with pseudoxanthoma elasticum (PXE), a prototype disorder of elastic fiber mineralization, it was coined the PXE-like syndrome. As mutations in GGCX negatively affect protein carboxylation, it is likely that inactive inhibitors of calcification contribute to ectopic mineralization in PXE-like syndrome. Because of the remarkable similarities with PXE, we performed a comparative study of various forms of VK-dependent proteins in serum, plasma (using ELISA), and dermal tissues (using immunohistochemistry) of PXE-like and PXE patients using innovative, conformation-specific antibodies. Furthermore, we measured VK serum concentrations (using HPLC) in PXE-like and PXE samples to evaluate the VK status. In PXE-like patients, we noted an accumulation of uncarboxylated Gla proteins, MGP, and OC in plasma, serum, and in the dermis. Serum levels of VK were normal in these patients. In PXE patients, we found similar, although not identical results for the Gla proteins in the circulation and dermal tissue. However, the VK serum concentration in PXE patients was significantly decreased compared with controls. Our findings allow us to conclude that ectopic mineralization in the PXE-like syndrome and in PXE results from a deficient protein carboxylation of VK-dependent inhibitors of calcification. Although in PXE-like patients this is due to mutations in the GGCX gene, a deficiency of the carboxylation co-factor VK is at the basis of the decreased activity of calcification inhibitors in PXE. Laboratory Investigation (2010) 90, 895-905; doi:10.1038/labinvest.2010.68; published online 5 April 2010".
- aggregation authorList BK692427.
- aggregation endPage "905".
- aggregation issue "6".
- aggregation startPage "895".
- aggregation volume "90".
- aggregation aggregates 1016986.
- aggregation aggregates 1016987.
- aggregation aggregates 1016988.
- aggregation aggregates 1016989.
- aggregation aggregates 1016990.
- aggregation aggregates 1016991.
- aggregation isDescribedBy 1013912.
- aggregation similarTo labinvest.2010.68.
- aggregation similarTo LU-1013912.