Tag Archives: vitamin B(1)
Scientific advancement on the way to molecular vitaminology at the Department of Vitamins and Coenzymes of the Palladin Institute of Biochemistry
M. Veliky, I. Shymanskyi, T. Kuchmerovska*, Yu. Parkhomenko
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine,
Department of Vitamins and Coenzymes, Kyiv;
*e-mail: tkuchmerovska@gmail.com
Received: 05 May 2025; Revised: 08 July 2025;
Accepted: 30 October 2025; Available on-line: 2025
Modern advances in molecular vitaminology are characterized by a marked expansion in understanding the molecular mechanisms underlying the actions of vitamins and their biologically active derivatives as highly effective compounds that ensure controlled interactions between cellular regulatory systems and metabolic processes. The molecular mechanisms of the pleiotropic effects of the hormonally active form of vitamin D3, calcitriol (1α,25(OH)2D3), are realized in target tissues through vitamin D3 receptors (VDR), which are present in virtually all cells. Our studies have focused on VDR-mediated effects, including modulation of the transcriptional activity of NF-κB, NFAT, HIF-1 and PPAR, as well as involvement of regulatory pathways such as HIF-1α/VEGF and RANK/NF-κB. We have also examined signaling through glucocorticoid and mineralocorticoid receptors, which play a key role in the antioxidant, anti-inflammatory, and anti-apoptotic effects of vitamin D3 under normal conditions and in pathology (osteoporosis, neurodegenerative disorders associated with glucocorticoid-induced neurotoxicity and type 2 diabetes mellitus). The mechanisms of the neurotropic effects of vitamin B3 (nicotinamide) and a derivative of nicotinic and amino butyric acid, nicotinoil-GABA (N-GABA), have also been studied. It has been demonstrated that nicotinamide (NAm) inhibits the development of diabetic neuropathy by reducing the activity and level of the PARP-1 enzyme, suppressing its fragmentation and preventing DNA damage in the brain tissue, and normalizing the nuclear levels of SIRT1 and SIRT2 proteins in neurons. One of the effective methodological approaches in our studies has been the investigation of thiamine-binding proteins in the brain and the effects of thiamine deficiency on the expression and state of neurospecific proteins. Based on our findings, we have formulated a working hypothesis regarding the molecular mechanisms of vitamin B1 involvement in the functioning of the cholinergic component of the nervous system. This hypothesis suggests that, in addition to the pool of thiamine diphosphate (ThDP) that binds to ThDP-dependent enzymes, nerve cells contain a rapidly exchangeable pool of thiamine derivatives that are involved in acetylcholine metabolism. The research achievements of our Department demonstrate the therapeutic potential of vitamins D3, B3, B1, and their biologically active derivatives in preventing the development of neurodegenerative complications under various pathological conditions and provide a scientific basis for the development of novel vitamin supplements.
Adenosine thiamine triphosphate and adenosine thiamine triphosphate hydrolase activity in animal tissues
A. F. Makarchikov1,2, T. V. Saroka3, T. G. Kudyrka1,2, I. K. Kolas1,2, T. A. Luchko2, I. M. Rusina1,2, V. A. Gurinovich2
1Grodno State Agrarian University, Belarus;
2Institute of Biochemistry of Biologically Active Compounds, National Academy of Sciences of Belarus;
3Yanka Kupala State University of Grodno, Belarus;
e-mail: a_makarchikov@yahoo.com
Adenosine thiamine triphosphate (AThTP), a vitamin B1 containing nucleotide with unknown biochemical role, was found previously to be present in various biological objects including bacteria, yeast, some human, rat and mouse tissues, as well as plant roots. In this study we quantify AThTP in mouse, rat, bovine and chicks. We also show that in animal tissues the hydrolysis of AThTP is catalyzed by a membrane-bound enzyme seemingly of microsomal origin as established for rat liver, which exhibits an alkaline pH optimum of 8.0-8.5 and requires no Mg2+ ions for activity. In liver homogenates, AThTP hydrolase obeys Michaelis-Menten kinetics with apparent Km values of 84.4 ± 9.4 and 54.6 ± 13.1 µМ as estimated from the Hanes plots for rat and chicken enzymes, respectively. The hydrolysis of AThTP has been found to occur in all samples examined from rat, chicken and bovine tissues, with liver and kidney being the most abundant in enzyme activity. In rat liver, the activity of AThTP hydrolase depends on the age of animals.