PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 739798

Developmental changes in rat adrenocortical cell membrane potential.

J Lymangrover·M Saffran·E K Matthews
View original source ↗Export metadata ↓

Abstract

Resting membrane potentials of zona fasciculata-reticularis cells of the rat adrenal gland varied with age. The mean membrane potentials of newborn rat adrenal cells was -56.4 +/- 0.7 mV in the first week of life. The mean potential increased slightly to -61.9 +/- 0.8 mV in the second week and then decreased with age to a mean of -38.5 +/- 0.8 mV in 25--50 week old rats and of -25.9 +/- 1.9 mV in 100 week old rats. The changes in membrane potential may correlate with the indices of adrenocortical growth and activity.

Explore related subjects

Adrenal CortexAgingAnimalsAnimals, NewbornFemaleMaleMembrane PotentialsRatsJournal ArticleResearch Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J Lymangrover, M Saffran, E K Matthews. 1978. Developmental changes in rat adrenocortical cell membrane potential.. https://doi.org/10.1016/0047-6374(78)90036-2

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1979

Characterization of the lipoidal derivatives of pregnenolone prepared by incubation of the steroid with adrenal mitochondria.

Using mass spectrometric, radioisotopic, chromatographic and chemical techniques, five fatty acid esters of 3 beta-hydroxy-5-pregnen-20-one (pregnenolone) have been identified as components of the lipoidal derivatives biosynthesized in vitro with bovine adrenal mitochondria. The five compounds are: pregnenolone arachidonate, pregnenolone linoleate, pregnenolone oleate, pregnenolone palmitate, and pregnenolone stearate. The distribution of the fatty acids among these five esters is different from the previously reported (Cmelik, S.H.W., and Ley, H. (1977) Comp. Biochem. Physiol. 56B, 267-270) fatty acid composition of these organelles.

Adrenal Cortex↗
PubMed1979

Purification and properties of a phosphorylase (phosphoprotein) phosphatase associated with an alkaline phosphatase of Mr 35000 from bovine adrenal cortex.

A metal-ion-independent, nonspecific phosphoprotein phosphatase (Mr = 35000) which represents the major phosphorylase phosphatase activity in bovine adrenal cortex has been purified to apparent homogeneity. An alkaline phosphatase activity (p-nitrophenyl phosphate as a substrate) of the same molecular weight, which requires both a metal ion (Mg2+ greater than Mn2+ greater than Co2+) and a sulfhydryl compound for activity, has been found to co-purify with the phosphoprotein phosphatase throughout the purification procedures. Characterization of the phosphoprotein and the alkaline phosphatase activities with respect to their catalytic properties, substrate and metal ion specificities, relationship with large molecular forms of the enzymes and responses to various effectors has been carried out. The results indicate that the phosphoprotein phosphatase can be converted by pyrophosphoryl compounds (e.g. PPi and ATP) to a metal-ion-dependent form which, subsequently, can be reactivated by Co2+ greater than Mn2+ but not by Mg2+ or Zn2+. The results also indicate that, although the phosphoprotein and the alkaline phosphatase activities are closely associated, they exhibit distinct physical and catalytic properties. Discussions concerning whether these two activities represent two different forms of the same protein or two different yet very similar polypeptide chains have been presented.

Adrenal Cortex↗