Abstract
Vitamin K (VK) is a key nutrient for several biological processes (e.g., blood clotting and bone metabolism). To fulfill VK nutritional requirements, VK action as an activator of pregnane X receptor (Pxr) signaling pathway, and as a co-factor of γ-glutamyl carboxylase enzyme, should be considered. In this regard, VK recycling through vitamin K epoxide reductases (Vkors) is essential and should be better understood. Here, the expression patterns of vitamin K epoxide reductase complex subunit 1 (vkorc1) and vkorc1 like 1 (vkorc1l1) were determined during the larval ontogeny of Senegalese sole (Solea senegalensis), and in early juveniles cultured under different physiological conditions. Full-length transcripts for ssvkorc1 and ssvkorc1l1 were determined and peptide sequences were found to be evolutionarily conserved. During larval development, expression of ssvkorc1 showed a slight increase during absence or low feed intake. Expression of ssvkorc1l1 continuously decreased until 24 h post-fertilization, and remained constant afterwards. Both ssvkors were ubiquitously expressed in adult tissues, and highest expression was found in liver for ssvkorc1, and ovary and brain for ssvkorc1l1. Expression of ssvkorc1 and ssvkorc1l1 was differentially regulated under physiological conditions related to fasting and re-feeding, but also under VK dietary supplementation and induced deficiency. The present work provides new and basic molecular clues evidencing how VK metabolism in marine fish is sensitive to nutritional and environmental conditions.
Highlights
Increasing a sustainable animal production is essential to warrant world food security and nutrition in the nearest future [1,2]
The identification and characterization of the different molecular pathways where Vitamin K (VK) acts in vertebrates development and physiology, how they respond to relevant physiological conditions, still needs to be determined in order to identify potential suitable biomarkers of VK nutritional status [67–69]
vitamin K epoxide reductases (Vkors) orthologues have been detected in different taxa of eukaryotic organisms, being Vkor complex subunit 1 (Vkorc1) and Vkorc1l1 paralogues that probably originated through a duplication event occurring at the base of the vertebrate split from other metazoans [66]
Summary
Increasing a sustainable animal production is essential to warrant world food security and nutrition in the nearest future [1,2]. We hypothesized that vkorc and vkorc1l1 gene expression might be altered through larval development and will be tissue-specific, reflecting that dietary VK requirement might depend on fish development and biological process considered. A multi-sequence alignment, using T-coffee platform, of 7 protein sequences corresponding to Vkor sequence from sea squirt (Ciona intestinalis), and Vkorc and Vkorc1l1 sequences from Senegalese sole, human (Homo sapiens) and mouse (Mus musculus), showed a high degree of conservation of the characteristic four cysteines and the serine residues, the four transmembrane domains, the thiol redox (CXXC) site, and the warfarin binding motif (TYX; Figure S1). RReellaattiivvee ggeennee eexxpprreessssiioonn ooff SSeenneeggaalleessee ssoollee vviittaammiinn KK eeppooxxiiddee rreedduuccttaassee ccoommpplleexx ssuubbuunniitt 11 ((ssssvvkkoorrcc11))aanndd vvkkoorrcc lliikkee 11((ssssvvkkoorrcc11l1l1))ininadaduultlttistissuseuse.sT. After five days of feeding with 1250VK1 diet, expression was unaltered (1.9 ± 0.2 versus 1.4 ± 0.7 folds in Control group)
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