Development of Na+-K+-ATPase in Neonatal Rat Brain Synaptosomes after Perinatal Protein Malnutrition

Kissane, J. Q.; Hawrylewicz, E. J.

doi:10.1203/00006450-197503000-00008

Cited by 15 publications

(8 citation statements)

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“…Other reports in the literature have demonstrated that perinatal undernutrition can retard the development of several enzymes involved in neurotransmitter metabolism and neuronal function (Sereni et al 1966;Adlard & Dobbing, 1971;Kissane & Hawrylewicz, 1975;Stern et al 1975;Vitiello & Gombos, 1987;Chanez et al 1988). The results of the present study demonstrated that undernutrition between birth and weaning can also decrease the activity of both ATP and ADP hydrolysis in fractions enriched in synaptosomes of 20-d-old rats.…”

Section: Discussionsupporting

confidence: 71%

“…Perinatal undernutrition impairs the generation of glial cells and myelin formation more than neuronal generation (Robain & Ponsot, 1978;Wiggins, 1982), impairing synaptogenesis and consequently the development of neuronal contacts (Cragg, 1972;Salas et al 1974;Dyson & Jones, 1976). Perinatal undernutrition can also cause a marked reduction in the activity of various enzymes involved in neurotransmitter and energy metabolism, changing neurotransmitter and neuromodulator systems (Sereni et al 1966;Adlard & Dobbing, 1971, 1972Kissane & Hawrylewicz, 1975;Miller et al 1977;Vanella et al 1983;Vitiello & Gombos, 1987;Chanez et al 1988;Vendite et al 1988).…”

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confidence: 99%

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Undernutrition during the preweaning period changes calcium ATPase and ADPase activities of synaptosomal fractions of weanling rats

et al. 1990

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The presence of activities that hydrolyse externally added ATP to adenosine in synaptosomal preparations from various sources is well demonstrated. The hydrolysis of ATP to AMP can be mediated either by the concerted action of enzymes or by an ATP-diphosphohydrolase (EC 3.6.1.5; apyrase).Undernutrition during the preweaning period can delay the development of several enzymes involved in the metabolism of neurotransmitters or neuronal function. In young rats, the presence of an apyrase in synaptosomal preparations from cerebral cortex was investigated. The results suggested that the hydrolysis of externally added ATP and ADP can be mediated by a single enzyme. The effects of preweaning undernutrition on the hydrolysis of ATP and ADP were also investigated. In weanling rats, previous undernutrition caused a decrease of about 20% in the hydrolysis of both substrates in synaptosomal fractions.

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Section: Discussionsupporting

confidence: 71%

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confidence: 99%

Undernutrition during the preweaning period changes calcium ATPase and ADPase activities of synaptosomal fractions of weanling rats

et al. 1990

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“…1967;COTE, 1964;GARCIA ARGIZ et al, 1967;VALCANA & TIMERAS, 1969;BANIK & DAVISON. 1969;MEDZIHRADSKY et al, 1972;TIRRI et al, 1973;MEI-SAMI & TIMERAS, 1974;KISSANE & HAWRYLEWICZ, 1975;MEISAMI & MANOOCHEHRI, 1977). Information on the kinetics of foetal rat brain (Na'-K+)-ATPase is sparse (WILSON & HUNT, 1974) and there have been no reports on the changes in enzyme protein in rat brain during development.…”

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confidence: 99%

DEVELOPMENT OF (Na⁺‐K⁺)‐ATPase IN RAT CEREBRUM: CORRELATION WITH Na ⁺ ‐DEPENDENT PHOSPHORYLATION AND K ⁺‐para NITROPHENYLPHOSPHATASE¹

Bertoni

Siegel

1978

Journal of Neurochemistry

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Abstract— The activities of (Na+ K+)‐ATPase and its proposed partial reactions, K +‐pNPPase and Na +‐dependent phosphorylation, all increase tenfold relative to microsomal protein between 5 days prior to birth and 60 days postnatally in NaI‐treated rat cerebral microsomes, and all reach half of their adult values between the fifth and tenth postnatal day. These increases are concurrent with the most rapid changes in cerebral wet weight. Increases in the amount of the related phosphorylatable polypeptide during development. as estimated by densitometry of Coomassie‐stained polyacrylamide gels after electrophoresis of constant amounts of microsomal protein dissolved in sodium dodecylsulfate, parallel the increments in levels of Na +‐dependent phosphorylation. The fraction of total phosphorylation that is Na +‐dependent increases steadily during development. suggesting a precursor role for some of the Na +‐independent fraction. The results are consistent with a single biosynthetic control for the enzymatic sites critical to the partial reactions of (Na +‐K +)‐ATPase. No changes in turnover number or affinity for substrate or ligands were found during development. Little similarity was noted among the age‐related changes of Mg 2+ ‐ATPase activity. Mg 2+ ‐paranitrophenylphosphatase activity, and Na+‐independent phosphorylation levels. The most rapid changes in (Na+‐K+)‐ATPase take place during the period corresponding to glial proliferation and neuronal arborization.

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“…, K ? -ATPase increases during development [30][31][32] due to enzyme accumulation [33][34][35]. It is possible that the greater IP accumulation in neonatal could be due to the relatively lower activity of the sodium pump.…”

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confidence: 99%

High-affinity Neurotensin Receptor is Involved in Phosphoinositide Turnover Increase by Inhibition of Sodium Pump in Neonatal Rat Brain

et al. 2008

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Phosphoinositide (PI) metabolism is enhanced in neonatal brain by activation of neurotransmitter receptors and by inhibition of the sodium pump with ouabain or endogenous inhibitor termed endobain E. Peptide neurotensin inhibits synaptosomal membrane Na(+), K(+)-ATPase activity, an effect blocked by SR 48692, a selective antagonist for high-affinity neurotensin receptor (NTS1). The purpose of this study was to evaluate potential participation of NTS1 receptor on PI hydrolysis enhancement by sodium pump inhibition. Cerebral cortex miniprisms from neonatal Wistar rats were preloaded with [(3)H]myoinositol in buffer during 60 min and further preincubated for 0 min or 30 min in the absence or presence of SR 48692. Then, ouabain or endobain E were added and incubation proceeded during 20 or 60 min. Reaction was stopped with chloroform/methanol and [(3)H]inositol-phosphates (IPs) accumulation was quantified in the water phase. After 60-min incubation with ouabain, IPs accumulation values reached roughly 500% or 860% in comparison with basal values (100%), if the preincubation was omitted or lasted 30 min, respectively. Values were reduced 50% in the presence of SR 48692. In 20-min incubation experiments, IPs accumulation by ouabain versus basal was 300% or 410% if preincubation was 0 min or 30 min, respectively, an effect blocked 23% or 32% with SR 48692. PI hydrolysis enhancement by endobain E was similarly blocked by SR 48692, being this effect higher when sample incubation with the endogenous inhibitor lasted 60 min versus 20 min. Present results indicate that PI hydrolysis increase by sodium pump inhibition with ouabain or endobain E is partially diminished by SR 48692. It is therefore suggested that NTS1 receptor may be involved in cell signaling system mediated by PI turnover.

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Development of Na+-K+-ATPase in Neonatal Rat Brain Synaptosomes after Perinatal Protein Malnutrition

Cited by 15 publications

References 8 publications

Undernutrition during the preweaning period changes calcium ATPase and ADPase activities of synaptosomal fractions of weanling rats

Undernutrition during the preweaning period changes calcium ATPase and ADPase activities of synaptosomal fractions of weanling rats

DEVELOPMENT OF (Na⁺‐K⁺)‐ATPase IN RAT CEREBRUM: CORRELATION WITH Na ⁺ ‐DEPENDENT PHOSPHORYLATION AND K ⁺‐para NITROPHENYLPHOSPHATASE¹

High-affinity Neurotensin Receptor is Involved in Phosphoinositide Turnover Increase by Inhibition of Sodium Pump in Neonatal Rat Brain

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Development of Na+-K+-ATPase in Neonatal Rat Brain Synaptosomes after Perinatal Protein Malnutrition

Cited by 15 publications

References 8 publications

Undernutrition during the preweaning period changes calcium ATPase and ADPase activities of synaptosomal fractions of weanling rats

Undernutrition during the preweaning period changes calcium ATPase and ADPase activities of synaptosomal fractions of weanling rats

DEVELOPMENT OF (Na+‐K+)‐ATPase IN RAT CEREBRUM: CORRELATION WITH Na + ‐DEPENDENT PHOSPHORYLATION AND K +‐para NITROPHENYLPHOSPHATASE1

High-affinity Neurotensin Receptor is Involved in Phosphoinositide Turnover Increase by Inhibition of Sodium Pump in Neonatal Rat Brain

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DEVELOPMENT OF (Na⁺‐K⁺)‐ATPase IN RAT CEREBRUM: CORRELATION WITH Na ⁺ ‐DEPENDENT PHOSPHORYLATION AND K ⁺‐para NITROPHENYLPHOSPHATASE¹