Assessment of Thermal Performance of Textile Materials Modified with PCM Microcapsules Using Combination of DSC and Infrared Thermography Methods.

The aim of the study was the combination of two measurement methods, the differential scanning calorimetry (DSC) and infrared thermography to evaluate thermal performance of woven and knitted fabrics coated with acrylic pastes containing 20% (P/20) and 40% (P/40) of microcapsules of phase change materials (MPCM) with transition temperatures of 28 °C (MPCM28) and 43 °C (MPCM43). The DSC analysis showed that the phase transition processes for materials modified with pastes P/20 occur in a narrower temperature range than those modified with P/40 pastes. The initial temperatures and are higher for materials modified respectively with pastes P/20 and P/40.

Calmodulin effect on purified rat cortical plasma membrane Ca(2+)-ATPase in different phosphorylation states.

The plasma membrane Ca(2+)-ATPase in neuronal tissue plays an important role in fine tuning of the intracellular Ca(2+) concentration. The enzyme exhibits a high degree of tissue specificity and is regulated by several mechanisms. Here we analysed the relationship between separate modes of Ca(2+)-ATPase regulation, i.

Short-time effects of neuroactive steroids on rat cortical Ca2+-ATPase activity.

Recent experimental evidence indicates that some steroid hormones, apart from their well-documented genomic actions, could produce non-genomic rapid effects, and are potent modulators of the plasma membrane proteins, including voltage- and ligand-operated ion channels or G protein-coupled receptors. Neuroactive steroids, 17beta-estradiol, testosterone, pregnenolone sulfate and dehydroepiandrosterone sulfate, after a short-time incubation directly modulated the activity of plasma membrane Ca2+-ATPase purified from synaptosomal membranes of rat cortex. The sulfate derivatives of dehydroepiandrosterone and pregnenolone applied at concentrations of 10-11-10-6 M, showed an inverted U-shape potency in the regulation of Ca2+-ATPase activity.

Protein kinases A and C phosphorylate purified Ca2+-ATPase from rat cortex, cerebellum and hippocampus.

The plasma membrane Ca2+-ATPase (PMCA), the enzyme responsible for the maintenance of intracellular calcium homeostasis, is regulated by several independent mechanisms. In this paper we report that the protein kinases A and C differentially activate the Ca2+-ATPase purified from synaptosomal membranes of rat cortex, cerebellum and hippocampus. The effect of protein kinases was more pronounced for the cortical enzyme, whereas cerebellar and hippocampal Ca2+-ATPases were activated to a lesser degree.

Okadaic acid as a probe for regulation in vitro of Mg(2+), Ca(2+)-ATPase activity in rat cortical and cerebellar synaptosomal membranes.

The in vitro effect of okadaic acid on basal phorbol 12-myristate 13-acetate (PMA)-, and cyclic adenosine monophosphate (cAMP)-stimulated Mg(2+)-dependent Ca(2+)-adenosine triphosphatase (ATPase) activity in synaptosomal membranes isolated from rat brain cortex and cerebellum was investigated. The basal activity was enhanced by okadaic acid in both examined regions. This inhibitor differed in the regulation of Mg2+, Ca(2+)-ATPase activity in PMA- and cAMP-incubated membranes.

Neuroactive steroids modulate in vivo the Mg2+/Ca(2+)-ATPase activity in rat cortical and cerebellar synaptosomal membranes.

Estradiol and pregnenolone sulfate administered in vivo inhibited the Mg2+/Ca(2+)-ATPase activity in synaptosomal membranes from rat cortex by 20% and 30%, respectively. In cerebellum, estradiol decreased the activity up to 43%. The calmodulin-stimulated activity declined in cortex after treatment with estradiol and pregnenolone sulfate, but significantly increased in cerebellar membranes.

Vanadium inhibition of human parietal lobe ATPases.

In vitro influence of vanadate and vanadyl ions on the activities of Na,K- and Ca,Mg-ATPase from synaptosomal membranes of the parietal lobe of the human brain were compared. 1. Vanadate and vanadyl inhibit the enzymes activities in the investigated fraction.