DEVELOPMENT OF (Na+‐K+)‐ATPase IN RAT HINDBRAIN: INCREMENTS IN PARALLEL WITH Na+‐DEPENDENT PHOSPHORYLATION AND K+‐pNITROPHENYLPHOSPHATASE

John M. Bertoni, George J. Siegel

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Rat hindbrain NaI‐enriched microsomal (Na+‐K+)‐ATPase activity, K+‐pNPPase activity, and Na+‐dependent steady‐state phosphorylation levels all increase approx 10‐fold relative to microsomal protein between 5 days prenatally and 60 days postnatally. These activities, as well as the mean wet weight of the hindbrain, are at half of their 60 day values shortly after the 10th postnatal day. For all ages, these hindbrain activities average over twice those found in the forebrain in a companion paper (Bertoni & Siegel, 1978). Increases during development in the amount of the related phosphorylatable polypeptide, estimated by densitometry of stained polyacrylamide gels containing fixed amounts of microsomal protein dissolved in SDS, are in agreement with increases in steady state levels of Na+‐dependent phosphorylation. The fraction of total phosphorylation that is Na+‐dependent rises steadily during development consistent with, but not obligatorily due to, a conversion of some of the previously Na+‐independent portion. Mg2+‐ATPase and Mg2+ ‐pNPPase activities and steady‐state Na+,‐independent phosphorylation levels do not increase in parallel during development. These observations add further support to the proposed partial reaction scheme for (Na+‐ K+)‐ATPase. The major increments in (Na +‐K+)‐ATPase occur simultaneously with the deposition of specialized plasma membranes, particularly in the molecular layer of the cerebellum, as described in previous studies of rat hind brain.

Original languageEnglish (US)
Pages (from-to)573-580
Number of pages8
JournalJournal of Neurochemistry
Volume32
Issue number2
DOIs
StatePublished - Feb 1979
Externally publishedYes

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Rhombencephalon
Phosphorylation
Adenosine Triphosphatases
Rats
Ca(2+) Mg(2+)-ATPase
Densitometry
Cell membranes
Prosencephalon
Cerebellum
Brain
Proteins
Cell Membrane
Weights and Measures
Peptides
sodium-translocating ATPase

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

@article{a6f0790695d141d59a2bdacf3fadbdd7,
title = "DEVELOPMENT OF (Na+‐K+)‐ATPase IN RAT HINDBRAIN: INCREMENTS IN PARALLEL WITH Na+‐DEPENDENT PHOSPHORYLATION AND K+‐pNITROPHENYLPHOSPHATASE",
abstract = "Rat hindbrain NaI‐enriched microsomal (Na+‐K+)‐ATPase activity, K+‐pNPPase activity, and Na+‐dependent steady‐state phosphorylation levels all increase approx 10‐fold relative to microsomal protein between 5 days prenatally and 60 days postnatally. These activities, as well as the mean wet weight of the hindbrain, are at half of their 60 day values shortly after the 10th postnatal day. For all ages, these hindbrain activities average over twice those found in the forebrain in a companion paper (Bertoni & Siegel, 1978). Increases during development in the amount of the related phosphorylatable polypeptide, estimated by densitometry of stained polyacrylamide gels containing fixed amounts of microsomal protein dissolved in SDS, are in agreement with increases in steady state levels of Na+‐dependent phosphorylation. The fraction of total phosphorylation that is Na+‐dependent rises steadily during development consistent with, but not obligatorily due to, a conversion of some of the previously Na+‐independent portion. Mg2+‐ATPase and Mg2+ ‐pNPPase activities and steady‐state Na+,‐independent phosphorylation levels do not increase in parallel during development. These observations add further support to the proposed partial reaction scheme for (Na+‐ K+)‐ATPase. The major increments in (Na +‐K+)‐ATPase occur simultaneously with the deposition of specialized plasma membranes, particularly in the molecular layer of the cerebellum, as described in previous studies of rat hind brain.",
author = "Bertoni, {John M.} and Siegel, {George J.}",
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