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L Zylińska

Publications and source records attributed to L Zylińska.

13 recordsLinked to original sources
PubMed2000

Plasma membrane Ca2+-ATPase in excitable and nonexcitable cells.

There is a significant number of data confirming that the maintenance of calcium homeostasis in a living cell is a complex, multiregulated process. Calcium efflux from excitable cells (i.e., neurons) occurs through two main systems--an electrochemically driven Na+/Ca2+ exchanger with a low Ca2+ affinity (K0.5 = 10-15 microM), and a plasmalemmal, specific Ca2+-ATPase, with a high Ca2+ affinity (K0.5 < 0.5-1 microM), whereas in nonexcitable cells (i.e., erythrocytes) the calcium pump is the sole system responsible for the extrusion of calcium ions. The plasma membrane Ca2+-ATPase (PMCA) is a ubiquitously expressed protein, and more than 26 transcripts of four PMCA genes are distributed in a tissue specific manner. Differences in the structure and localization of PMCA variants are thought to correlate with specific regulatory properties and may have consequences for proper cellular Ca2+ signaling. The regulatory mechanisms of calcium pump activity have been studied extensively, resulting in a new view of the functioning of this important molecule in the membranes.

Animals↗
PubMed1999

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. At physiologically relevant concentrations (10-8-10-9 M) a maximal enhancement of the basal activity reached 200%. Testosterone (10-11-10-6 M) and 17beta-estradiol (10-12-10-9 M) caused a dose-dependent increase in the hydrolytic ability of Ca2+-ATPase, and the activity with the highest concentration of steroids reached 470% and 200%, respectively. All examined steroids decreased the stimulatory effect of a naturally existing activator of the calcium pump, calmodulin. The present study strongly suggests that the plasma membrane calcium pump could be one of the possible membrane targets for a non-genomic neuroactive steroid action.

Animals↗
PubMed1998

Neuroactive steroids modulate in vitro the Mg(2+)-dependent Ca(2+)-ATPase activity in cultured rat neurons.

1. The in vitro effect of neuroactive steroids on the Mg(2+)-dependent Ca(2+)-ATPase activity in neuronal membranes isolated from primary cell culture of rat cortex was examined. 2. A 1-hr treatment of neuronal cell culture with 17-beta-estradiol (10 pM) and pregnenolone sulfate (1 microM) resulted in an increase in the enzyme activity of as much as 130% and 160%, respectively. 3. Neuroactive steroids moderately decreased the stimulation of the Mg(2+)-dependent Ca(2+)-ATPase activity by 72 nM calmodulin, by 20-30%. 4. The effects of hormones on the ATPase activity were irreversible after extensive washing of the membranes. 5. These results suggest that 17-beta-estradiol and pregnenolone sulfate at physiological concentrations could participate in the regulation of neuronal calcium homeostasis at a membrane level.

Animals↗
PubMed1997

Protein kinase C and calmodulin effects on the plasma membrane Ca2+-ATPase from excitable and nonexcitable cells.

We have purified Ca2+-ATPase from synaptosomal membranes (SM)1 from rat cerebellum by calmodulin affinity chromatography. The enzyme was identified as plasma membrane Ca2+-ATPase by its interaction with calmodulin and monoclonal antibodies produced against red blood cell (RBC) Ca2+-ATPase, and by thapsigargin insensitivity. The purpose of the study was to establish whether two regulators of the RBC Ca2+-ATPase, calmodulin and protein kinase C (PKC), affect the Ca2+-ATPase isolated from excitable cells and whether their effects are comparable to those on the RBC Ca2+-ATPase. We found that calmodulin and PKC activated both enzymes. There were significant quantitative differences in the phosphorylation and activation of the SM versus RBC Ca2+-ATPase. The steady-state Ca2+-ATPase activity of SM Ca2+-ATPase was approximately 3 fold lower and significantly less stimulated by calmodulin. The initial rate of PKC catalyzed phosphorylation (in the presence of 12-myristate 13-acetate phorbol) was approximately two times slower for SM enzyme. While phosphorylation of RBC Ca2+-ATPase approached maximum level at around 5 min, comparable level of phosphorylation of SM Ca2+-ATPase was observed only after 30 min. The PKC-catalyzed phosphorylation resulted in a statistically significant increase in Ca2+-ATPase activity of up to 20-40%, higher in the SM Ca2+-ATPase. The differences may be associated with diversities in Ca2+-ATPase function in erythrocytes and neuronal cells and different isoforms composition.

Animals↗
PubMed1995

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. Dehydroepiandrosterone sulfate had influence neither on enzyme activity, nor on stimulation by calmodulin in both examined rat brain regions.

Animals↗
PubMed1993

Serotonin, histamine and somatostatin modulation of PMA-stimulated phosphorylation of 130 kDa Ca2+ pump-like protein from rat cerebellum synaptosomal membranes.

1. Influence of some neurotransmitters and neuromodulators on the PMA-stimulated phosphorylation in vitro of calcium pump-like protein from rat cerebellum synaptosomal membranes was examined. 2. The prolonged time (up to 6 min) of synaptosomal membranes preincubation with 1 and 10 microM serotonin results in the increase of phosphorylation. The decrease of phosphorylation up to 80% of control value was observed for 100 microM serotonin. 3. The most stimulating effect on 130 kDa protein phosphorylation was observed with 1 microM of histamine (160% of control value). 4. 1 and 0.1 microM somatostatin triggered a short-time transient increase of 130 kDa phosphorylation (up to 135% of control value).

Animals↗
PubMed1992

Characterization of 130 kDa protein from rat cerebellum synaptosomal membranes phosphorylated by PKC.

1. The effect of endogenous PMA-stimulated phosphorylation of the protein in the molecular weight range of 130 kDa in rat cerebellum synaptosomal membranes was examined. 2. The 50% inhibition of the phosphorylation of 130 kDa protein by 5 microM polymyxin B was observed after 6 min of preincubation. 3. The sensitivity of 130 kDa protein for phosphorylation in the presence of exogenous protein kinase C suggests, that this protein could serve as a physiological substrate of protein kinase C. 4. Partial characterization of 130 kDa protein was performed. Upon incubation with [gamma-32P]ATP the 130 kDa protein formed Ca(2+)-dependent, hydroxylamine-sensitive phosphointermediate, which was inhibited by 50 microM vanadate, but not 0.5 mM vanadyl. 5. One-dimensional peptide mapping by proteolysis of 130 kDa protein with V8 protease was obtained.

Animals↗
PubMedDate not supplied

Can magnesium sulfate reduce the risk of cerebral injury after perinatal asphyxia?

Hypoxia-ischemia produces brain damage by processes that continue for many hours after reoxygenation/reperfusion. This provides a window of opportunity for therapy aimed at preventing further loss of brain cells. Sulfate magnesium can prevent posthypoxic brain injury by blocking glutamate receptors within the calcium (Ca++) ion channel. We used sulfate magnesium in nine newborn infant after perinatal hypoxia. We investigated the brain damage, by ultrasound examination, on third day, in first, second and third week, and third, sixth month of life. We have estimated the neurological development in the first week of life and third and twelfth month of life. We did not find deviations in ultrasound examination. We did not observe convulsions. We did not observe any side effect of this therapy. The examination at 1 of year of life in all of children was correct.

Asphyxia Neonatorum↗