acid-phosphatase and Thiamine-Deficiency

Vitamins are crucial components in the diet of animals and many other living organisms. One of these essential nutrients, thiamin, is known to be involved in several cell functions, including energy metabolism and the degradation of sugars and carbon skeletons. Other roles that are connected to this vitamin are neuronal communication, immune system activation, signaling and maintenance processes in cells and tissues, and cell-membrane dynamics. Because of the key functions of thiamin, uptake and transport through the body are crucial. Its uptake route is relatively complex, encompassing a variety of protein families, including the solute carrier anion transporters, the alkaline phosphatase transport system, and the human extraneuronal monoamine transporter family, some of which are multispecific proteins. There are two known structures of protein (subunits) involved in thiamin uptake in prokaryotes. Binding of thiamin to these proteins is strongly guided by electrostatic interactions. The lack of structural information about thiamin binding proteins for higher organisms remains a bottleneck for understanding the uptake process of thiamin in atomic detail. This review includes recent data on thiamin metabolism, related deficiencies and pathologies, and the latest findings on thiamin binding transporters.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Biological Transport; Brain; Energy Metabolism; Humans; Immune System; Membrane Transport Proteins; Organ Specificity; Thiamine; Thiamine Deficiency

In this study, we investigate the effects of dietary thiamin deficiency on immune responses, tight junctions, antioxidant capacity and related signaling molecules in the gills of young grass carp (Ctenopharyngodon idella). Fish were fed diets that contained 0.12-2.04 mg thiamin kg(-1) for 8 weeks. We found that dietary thiamin deficiency resulted in reduced complement 3 content, lysozyme and acid phosphatase activities, mRNA levels of hepcidin, liver-expressed antimicrobial peptides 2, transforming growth factor (TGF)-β1, interleukin (IL)-10, inhibitor protein-κBα (IκBα), ribosomal S6 protein kinase 1 and target of rapamycin (TOR) and increased expression of interferon-γ2, tumor necrosis factor-α, TGF-β2, IL-1β, IL-8, IκB kinases (IKKβ and IKKγ) and nuclear factor-κB p65 (NF-κB p65). Our findings showed that thiamin deficiency reduced the immune status of fish gills. Furthermore, thiamin deficiency resulted in reduced mRNA transcript levels of claudin b, claudin 3, claudin 12, zonula occludens 1 (ZO-1) and occludin and increased mRNA transcript levels of claudin 15a, myosin light-chain kinase (MLCK) and p38 mitogen-activated protein kinase (p38 MAPK) in fish gill tissues. These data suggested that thiamin deficiency disrupted tight junction-mediated fish gill barrier function. Additionally, reactive oxygen species, malondialdehyde and protein carbonyl levels and both the activities and expression levels of Cu/Zn superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferases and glutathione reductase, as well as NF-E2-related factor 2 gene expression in fish gills, were lower in fish fed a thiamin-deficient diet. By contrast, thiamin deficiency increased levels of Kelch-like-ECH-associated protein 1a (Keap1a) and Keap1b mRNA transcript expression in fish gills. Taken together, our findings indicated that thiamin deficiency impaired fish gill health by effects on the expression of genes encoding cytokines, tight junction proteins, antioxidant enzymes, NF-κB p65, MLCK and Nrf2.

Topics: Acid Phosphatase; Animals; Carps; Catalase; Complement C3; Cytokines; Fish Proteins; Gills; Glutathione Peroxidase; Glutathione Reductase; Glutathione Transferase; Kelch-Like ECH-Associated Protein 1; Muramidase; Myosin-Light-Chain Kinase; NF-E2-Related Factor 2; p38 Mitogen-Activated Protein Kinases; RNA, Messenger; Superoxide Dismutase; Thiamine Deficiency; Tight Junction Proteins; TOR Serine-Threonine Kinases; Transcription Factor RelA; Transforming Growth Factor beta

Histochemical and immunohistological examinations were carried out at different stages of thiamine-deficient encephalopathy in rats. The respiratory enzymatic activity decreased in the most damaged area correlating well with the neuropathological findings. There was an inverse relationship between the damaged area and its marginal zone; the latter showed an increase of the same enzymatic activity. The capillary network and the activity of the vessel walls seemed to be almost unimpaired. The immunohistological investigations showed only a moderate extravasation of the plasma proteins.

Topics: Acetylcholinesterase; Acid Phosphatase; Alkaline Phosphatase; Animals; Blood-Brain Barrier; Butyrylcholinesterase; Fluorescent Antibody Technique; Immunoenzyme Techniques; Oxidoreductases; Rats; Thalamus; Thiamine Deficiency

The influence of experimental thiamine deficiency in rats on enzyme-histochemical parameters was carried out in the diencephalon. The degree of thiamine deficiency was measured by the activity coefficient of transketolase in the red blood cells. The alpha-ETK of thiamine deficient animals was 1,45 +/- 0,36, of equal-fed animals 1,04 +/- 0.04 and of control animals 1,08 +/- 0,04. We got the following results: Lactatdehydrogenase, acid phosphatases and thiamine pyrophosphatase did not indicate any difference in enzyme activity between the groups of control, equal-fed and thiamine deficient rats. However, the enzyme activity of nonspecific lysosome-bound esterases in the tanycyte ependyma and in the investigated nuclear regions (nucleus supraopticus, ncl. paraventricularis, ncl. ventromedialis) of the thiamine deficient animals was significantly decreased in comparison to control and equal-fed animals. The possibility of a restriction of the hypophyseal-adrenal-cortex-system is discussed, since the results are similar to those obtained with bilaterally adrenalectomized rats.

Topics: Acid Phosphatase; Animals; Cerebral Ventricles; Diencephalon; Ependyma; Esterases; Histocytochemistry; Hydrolases; L-Lactate Dehydrogenase; Male; Oxidoreductases; Rats; Thiamine Deficiency; Thiamine Pyrophosphatase