Objective: Intracellular calcium (Ca) is increased in obese humans, and magnesium (Mg)-ATPase activity is increased in monosodium glutamate-induced obese rats. The aims of this study were to test the hypotheses that Ca-ATPase activity is negatively correlated with BMI, and that Mg-ATPase activity is positively correlated with BMI and Ca-ATPase activity in obese women.
Research Methods And Procedures: Thirty healthy adult women, with BMIs of 20 to 40, donated a single sample of whole blood and were interviewed as to medical history and family history of obesity. Erythrocyte membranes were isolated and assayed for Ca-ATPase and Mg-ATPase. Weight and height were self-reported. Regression analysis was used to determine relationship between BMI and enzyme activity. Family history of obesity served as a covariant.
Results: Ca-ATPase was negatively correlated with increasing BMI (r = - 0.38, p = 0.02). The relationship between BMI and Ca-ATPase remained valid after controlling for family history of obesity (r = -0.36, p = 0.03). There was a positive correlation between Mg-ATPase activity and Ca-ATPase (r = 0.42, p = 0.024), and this relationship remained valid after controlling for BMI and family history of obesity (r = 0.41, p = 0.03).
Discussion: Ca-ATPase activity decreases as BMI increases. Decreased ATPase activity may contribute to increased intracellular calcium, previously reported in obese persons. Further studies are needed to determine whether a drop in Ca-ATPase activity can serve as a marker for the development of obesity.
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http://dx.doi.org/10.1038/oby.2004.229 | DOI Listing |
Ecotoxicology
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University of Cukurova, Faculty of Sciences and Arts, Department of Biology, Adana, Turkey.
Mussels are filter-feeding animals with a sedentary lifestyle and thus, they were accepted as good bioindicator animals to investigate environmental pollution. In this study, freshwater mussels (Unio tigridis) were exposed to cadmium (0, 30, 90, 270 µg Cd/L) for up to 21 days. Then, the responses of several biomarkers belonging to the antioxidant, osmoregulation and nervous systems, as well as the energy reserves of mussels were investigated.
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Universidad de Buenos Aires. Facultad de Odontología, Cátedra de Biofísica y Bioestadística. Buenos Aires, Argentina.
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Department of Vitamins and Coenzymes Biochemistry, Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, Kyiv, 01054, Ukraine.
Long-term studies have confirmed a causal relationship between the development of neurodegenerative processes and vitamin B (thiamine) deficiency. However, the biochemical mechanisms underlying the high neurotropic activity of thiamine are not fully understood. At the same time, there is increasing evidence that vitamin B, in addition to its coenzyme functions, may have non-coenzyme activities that are particularly important for neurons.
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Department of Cell and Molecular Physiology, Loyola University Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, USA.
In cardiac myocytes, the type 2a sarco/endoplasmic reticulum Ca-ATPase (SERCA2a) plays a key role in intracellular Ca regulation. Due to its critical role in heart function, SERCA2a activity is tightly regulated by different mechanisms, including micropeptides. While phospholamban (PLB) is a well-known SERCA2a inhibitor, dwarf open reading frame (DWORF) is a recently identified SERCA2a activator.
View Article and Find Full Text PDFSci Total Environ
July 2024
Leibniz Centre for Tropical Marine Research (ZMT), Fahrenheitstraße 6, 28359 Bremen, Germany; Faculty of Geosciences, University of Bremen, Klagenfurter Str. 2-4, 28359 Bremen, Germany.
Ocean acidification and warming affect marine ecosystems from the molecular scale in organismal physiology to broad alterations of ecosystem functions. However, knowledge of their combined effects on tropical-subtropical intertidal species remains limited. Pushing the environmental range of marine species away from the optimum initiates stress impacting biochemical metabolic characteristics, with consequences on lipid-associated and enzyme biochemistry.
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