The Active Isoforms of MGP Are Expressed in Healthy and Varicose Veins without Calcification

S.R. Gheorghe, C. Vermeer, G. Olteanu, C.N. Silaghi*, A.M. Craciun

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review


Matrix Gla protein (MGP), a local inhibitor of tissue mineralization, is associated with vascular calcification. Depending on the carboxylation and phosphorylation status, MGP has active conformations, e.g., carboxylated MGP (cMGP) and phosphorylated MGP (pMGP), but also inactive conformations, e.g., uncarboxylated MGP (ucMGP) and dephosphorylated MGP (dpMGP). Our purpose was to assess the presence of all MGP conformations in healthy veins (HV) and varicose veins (VV), concurrently with the analysis of circulating total MGP (tMGP) before and after the surgical stripping of VV. We collected samples from the great saphenous vein, considered as control group, and tissue from VV, designated as VV group. Plasma levels of tMGP were significantly decreased after the surgical removal of the VV (before 59.5 +/- 17.2 vs. after 38.1 +/- 11.3, p < 0.001). By using immunohistochemistry staining, we identified local cMGP and pMGP in the control and VV groups, both without calcification, while ucMGP and dpMGP were absent. cMGP was observed in the nucleus and cytoplasm and pMGP in the nucleus of cells belonging to the tunica media, tunica intima and vasa vasorum. Therefore, the active conformations of MGP (cMGP and pMGP) are prevalent in HV and VV without calcification, affirming their anti-calcifying role in veins.
Original languageEnglish
Article number5896
Number of pages9
JournalJournal of Clinical Medicine
Issue number24
Publication statusPublished - 1 Dec 2021


  • varicose veins
  • matrix Gla protein
  • calcification
  • immunohistochemistry


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