CVD, Maastricht University

Categories

MGP ELISAs

MGP ELISAs

MGP Western Blots

MGP Western Blots

MGP Immunohistochemistry

MGP Immunohistochemistry

MGP Immunocytochemistry

MGP Immunocytochemistry

Cardiovascular Disease Risk and Mortality

Cardiovascular Disease Risk and Mortality

Welcome

MGP Center is a commercial division of VitaK Innovation in Life Science.

Worldwide we are the number one Laboratory in measuring Matrix Gla Protein (MGP), and we are unique in that we can discriminate between active and inactive MGP conformations. MGP is one of the strongest risk factors for cardiovascular disease and mortality presently known.

Since 2001 we have been experts in measuring biomarkers in blood samples generated in research projects, population-based studies and clinical trials in the field of cardiovascular disease and related diseases.

With our carefully selected panels of the most informative biomarkers we can distinguish between the underlying processes that are associated with cardiovascular disease. By combining classical risk markers with information on circulating MGP fractions, we are able to help researchers retrieve maximal information from their precious studies.

Scientific Background:


MGP is the most potent inhibitor of tissue calcification presently known. It consists of 84 amino acids and is synthesized by the vascular smooth muscle cells. MGP contains at least two sites for posttranslational modification: i.e. the phosphoserine (Pser) domain (aa 3-15) with three serine residues that may be phosphorylated, and the Gla-domain (aa 35-54) with four glutamate (Glu) residues that may undergo carboxylation transforming Glu into gamma-carboxyglutamate (Gla). Both Pser and Gla residues are negatively charged groups with a high affinity for calcium. In healthy individuals both modifications are exerted incompletely. This means that at least four different MGP species are formed (see figure 1). 

model_pser_gla

Figure 1. Four different conformations of MGP. Phosphoserine (Pser) residues are depicted as circles, carboxylated glutamate (Gla) residues as triangles.


Vitamin K is the cofactor for gammaglutamate carboxylation: dietary vitamin K insufficiency leads to Gla-deficient MGP, which has no calcification-inhibitory activity. Monoclonal antibodies have been prepared against each of these four conformations and are available for ELISA measurements, Western blotting, immunohistochemistry and immunocytochemistry (listed on the left).