Identification of Cryptosporidium felis in a cow by morphologic and molecular methods

Apicomplexan Cryptosporidium parasites infect a wide range of vertebrate hosts. While some species are limited to a single host group, such as Cryptosporidium baileyi, which infects chickens, other species of this genus, such as C. parvum, infect a wide range of mammalian species from mice to humans. During an investigation of Cryptosporidium infection in cattle on a farm in northern Poland, we identified an infection caused by C. felis, in addition to known infections with C. muris and C. parvum. This new infection was identified based on the size of the oocysts (mean size, 4.3 +/- 0.4 micrometer; range, 3.5 to 5.0 micrometer), as well as by analysis of the molecular sequence of the variable region of the small-subunit rRNA. This finding demonstrates the complex host specificity and circulation in the environment of Cryptosporidium species.     

Nonlinear system identification using a neo fuzzy neuron algorithm: electrical drive application

This work presents a Neo-Fuzzy-Neuron algorithm for the identification of nonlinear dynamic systems at the point of view of a rotor flux observer. The algorithm training is on-line, has low computational cost, does not require previous training and its convergence in one step is proved. The gradient descent method is used for its weights adjustment. Simulation and experimental results demonstrate the effectiveness of the algorithm for flux observer of induction motor drive system.     

Dietary intake of selenium and its concentration in breast milk

Selenium concentration was measured in the breast milk of 30 mothers at different stages of lactation and various body mass indices (BMI). For a maternal mean selenium intake meeting 100% of the Recommended Daily Allowance, mean milk selenium concentration was 14.06 ng/mL (range: 10.0–24.7 ng/mL). No significant correlation was found between the concentration of milk selenium with the stage of lactation, BMI, or dietary selenium intake.     

How acidic is the lumen?

Proton motive force (pmf), established across the thylakoid membrane by photosynthetic electron transfer, functions both to drive the synthesis of ATP and initiate processes that down-regulate photosynthesis. At the same time, excessively low lumen pH can lead to the destruction of some lumenal components and sensitization of the photosynthetic apparatus to photoinhibition. Therefore, in order to understand the energy budget of photosynthesis, its regulation and responses to environmental stresses, it is essential to know the magnitude of pmf, its distribution between pH and the electric field () as well as the relationships between these parameters and G_ATP, and down-regulatory and inhibitory processes. We review past estimates of lumen pH and propose a model that can explain much of the divergent data in the literature. In this model, in intact plants under permissive conditions, photosynthesis is regulated so that lumen pH remains mod erate (between 5.8 and 6.5), where it modulates the activity of the violaxanthin deepoxidase, does not significantly restrict the turnover of the cytochrome b₆f complex, and does not destabilize the oxygen evolving complex. Only under stressed conditions, where light input exceeds the capacity of both photosynthesis and down-regulatory processes, does lumen pH decrease below 5, possibly contributing to photoinhibition. A value of n = 4 for the stoichiometry of protons pumped through the ATP synthase per ATP synthesized, and a minor contribution of to pmf, will allow moderate lumen pH to sustain the observed levels of G_ATP.     

Molecular study of the rat liver NADH: Cytochrome c oxidoreductase complex during development and aging

The mechanisms involved in ageing are yet to be fully understood but it is thought that changes produced in energy transfer pathways occurring in the mitochondria may be responsible for the lack of energy typical of the later stages of life. The aim of the present investigation was to determine the enzymatic activity of the liver NADH cytochrome c oxidorectuctase complex (Complex I-III) in mitochondria isolated from the liver of rats of 3 different age groups: lactating, animals (15-17 days), adult females (3-5 months) and old animals (26-30 months). The activities of the unbound Complexes I and III were also determined.An increase in Complex I-III activity was detected during development (142 ± 10 vs. 447 ± 23 mol cyt. c/mg/min, p < 0.001) ang ageing (447 ± 23 vs. 713 ± 45 mol cyt. c/mg//min, p < 0.001). However, unbound Complex I showed a reduction in activity during the ageing period whilst Complex III activity moderately increased. Immunological studies indicated only a moderate increase in the amount of Complex I-III and studies on the purified complex suggested that the increase in activity was due to effects other than an increase in enzyme quantity. The analysis of protein bands and the quantification of prosthetic groups showed particular reductions in the relative concentrations of Complex I subunits including the 51 kDa unit, which binds FMN, confirmed by a similar reduction in levels of the nucleotide. In contrast, 4 of the 5 subunits which increased during the lifetime of the animals corresponded to those of Complex III. These subunits are responsible for the binding of catalytic groups. The results suggest that, in addition to the increase in the amount of enzyme, binding factors between Complexes I and III may also play an important role in the observed increase in Complex I-III activity.     

K+/Na+ antagonism at cytoplasmic sites of Na+-K+-ATPase: a tissue-specific mechanism of sodium pump regulation

Tissue-distinct interactions of theNa⁺-K⁺-ATPasewith Na⁺ andK⁺, independent ofisoform-specific properties, were reported previously (A. G. Therien,N. B. Nestor, W. J. Ball, and R. Blostein. J. Biol.Chem. 271: 7104-7112, 1996). In this paper, wedescribe a detailed analysis of tissue-specific kinetics particularlyrelevant to regulation of pump activity by intracellularK⁺, namelyK⁺ inhibition at cytoplasmicNa⁺ sites. Our results show thatthe order of susceptibilities of ₁ pumps of various rat tissuestoK⁺/Na⁺antagonism, represented by the ratio of the apparent affinity forNa⁺ binding at cytoplasmicactivation sites in the absence ofK⁺ to the affinity constant forK⁺ as a competitive inhibitor ofNa⁺ binding at cytoplasmic sites,is red blood cell < axolemma  rat₁-transfected HeLa cells < small intestine < kidney < heart. In addition, we havecarried out an extensive analysis of the kinetics ofK⁺ binding and occlusion to thecytoplasmic cation binding site and find that, for most tissues, thereis a relationship between the rate ofK⁺ binding/occlusion and theapparent affinity for K⁺ as acompetitive inhibitor of Na⁺activation, the order for both parameters being heart  kidney > small intestine  rat₁-transfected HeLa cells. Thenotion that modulations in cytoplasmicK⁺/Na⁺antagonism are a potential mode of pump regulation is underscored byevidence of its reversibility. Thus the relatively highK⁺/Na⁺antagonism characteristic of kidney pumps was reduced when rat kidneymicrosomal membranes were fused into the dog red blood cell.

     

NBD-cholesterol incorporation by rat macrophages and lymphocytes: a process dependent on the activation state of the cells

The time-course of incorporation of NBD-cholesterol by macrophages (Ma) and lymphocytes (LY) obtained from untreated and thioglycollate-injected (thio) rats was investigated. NBD-cholesterol incorporation was also examined in Ma obtained from untreated rats and stimulated in vitro by lipopolysaccharide (LPS) and phorbol-myristate acetate (PMA). The same measurement was performed in LY from untreated rats stimulated by addition of LPS and concanavalin A (Con A) into the culture medium. Thio-treated Ma showed high fluorescence intensity after 1 h of incubation with NBD-cholesterol. Ma submitted concomitant to LPS and NBD-cholesterol showed low fluorescence intensity, as well as Ma stimulated with PMA. Ma from untreated and LPS pre-treated rats showed a similar time-course of incorporation. LY from thio-treated rats showed lower incorporation of NBD-cholesterol in comparison to LY from untreated rats. Incorporation was reduced when LPS was added concomitantly with NBD-cholesterol. On the other hand, LY pre-treated with LPS for 48 h showed a very high incorporation of NBD-cholesterol. Con A treatment did not cause a significant effect on NBD-cholesterol incorporation. The findings presented herein led us to conclude that the uptake of NBD-cholesterol by Ma and LY is markedly affected by the activation state of the cells.