High impact information on GC

• The compounds showed a decreased metabolic stability in rat liver homogenates and had a 50-fold lower affinity for the vitamin D-binding protein than calcitriol, which suggests that calcitriol analogues are metabolized more rapidly after systemic uptake or application [1].
• For this purpose, the affinities and the maximum binding capacities (Bmax) of the plasma vitamin D-binding protein (DBP) and of the intestinal 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3) receptor for vitamin D3, 25-hydroxyvitamin D3 (25-OHD3) and 1,25-(OH)2D3, were investigated in normal piglets and in rachitic piglets that suffered from PVDRI [2].
• Binding properties of plasma vitamin D-binding protein and intestinal 1,25-dihydroxyvitamin D3 receptor in piglets with pseudo-vitamin D-deficiency rickets, type I: treatment effects with pharmacological doses of vitamin D3 [2].
• Plasma vitamin D-binding protein and free 1,25-dihydroxyvitamin D3 index in pregnant ewes and their fetuses in the last month of gestation [3].
• In addition it has been observed that the absence of ginkgolide C (GC) in plasma samples (in human and animals) was due to its rapid methylation [4].

Biological context of GC

• Genetic polymorphism of the vitamin D binding protein (Gc protein) in pig plasma determined by agarose isoelectrofocusing [5].
• Changes of G-actin localisation in the mitotic spindle region or nucleus during mitosis and after heat shock: a histochemical study of G-actin in various cell lines with fluorescent labelled vitamin D-binding protein [6].

Anatomical context of GC

• The uptake and metabolism of 25-hydroxyvitamin D3 and vitamin D binding protein by cultured porcine kidney cells (LLC-PK1) [7].
• The presence and localisation of G-actin in various cell lines was studied using the highly G-actin specific, fluorescence-labelled vitamin D-binding protein [6].
• The biological activity of 3-epi-1alpha,25(OH)2D3 was found to be lower than the native 1alpha,25(OH)2D3 in suppressing of proliferation of HL-60 cells, while the affinity of 3-epi-1alpha,25(OH)2D3 for vitamin D-binding protein was 2.5-fold higher than that of 1alpha,25(OH)2D3 [8].

Analytical, diagnostic and therapeutic context of GC

• Genetic polymorphism of the pig plasma vitamin D binding protein Gc was demonstrated by agarose isoelectrofocusing followed by either autoradiography or immunofixation with specific human Gc antiserum [5].
• Chromatofocusing was used to purify the vitamin D-binding protein (DBP) from pig plasma in a procedure that consisted of an initial DEAE-cellulose chromatography followed by DEAE-Sephadex chromatography, with final purification by chromatofocusing [9].
• A radioimmunoassay for ovine vitamin D-binding protein (DBP) has been developed [3].
• Legumain from bovine kidney: its purification, molecular cloning, immunohistochemical localization and degradation of annexin II and vitamin D-binding protein [10].

References