The decrease in the short variant of gsalpha protein is associated with an increase in [3H]CGP12177 binding, [3H]ouabain binding and Na, K-ATPase activity in brown adipose tissue plasma membranes of cold-acclimated hamsters
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9924180
DOI
10.1677/jme.0.0220055
Knihovny.cz E-resources
- MeSH
- Acclimatization physiology MeSH
- Cell Membrane metabolism MeSH
- Centrifugation, Density Gradient MeSH
- Adipose Tissue, Brown metabolism MeSH
- Enzyme Inhibitors metabolism pharmacology MeSH
- Cricetinae MeSH
- Mesocricetus physiology MeSH
- Membrane Proteins metabolism MeSH
- Mitochondria metabolism MeSH
- Molecular Weight MeSH
- Cold Temperature * MeSH
- Ouabain metabolism pharmacology MeSH
- Propanolamines metabolism MeSH
- Protein Isoforms deficiency isolation & purification physiology MeSH
- GTP-Binding Protein alpha Subunits, Gs deficiency isolation & purification physiology MeSH
- Sodium-Potassium-Exchanging ATPase antagonists & inhibitors metabolism MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- CGP 12177 MeSH Browser
- Enzyme Inhibitors MeSH
- Membrane Proteins MeSH
- Ouabain MeSH
- Propanolamines MeSH
- Protein Isoforms MeSH
- GTP-Binding Protein alpha Subunits, Gs MeSH
- Sodium-Potassium-Exchanging ATPase MeSH
Sucrose density gradient purified plasma membranes isolated from brown adipose tissue of cold-acclimated hamsters (4-10 weeks at 0-4 degreesC) were analysed for the content of the short (GsalphaS) and long (GsalphaL) variants of Gsalpha protein (the alpha subunit of the stimulatory G protein) and compared with the membranes isolated from control animals. The relative ratio between the two variants (GsalphaS/GsalphaL) decreased from 0.48 to 0.24 (P<0.01). This result, obtained by electrophoretic resolution of membrane proteins by standard SDS-PAGE and an immunoblot analysis with an antiserum oriented against an internal sequence of Gsalpha, was verified by resolution on urea-containing gels and an antiserum oriented against the C-terminus decapeptide of Gsalpha. Under these conditions, the GsalphaS/GsalphaL ratio was decreased from 0.41 to 0.31 (P<0.05). The total amount of both isoforms (GsalphaS plus GsalphaL) decreased to 83% (P<0.05) or 68% (P<0.01) by standard or urea SDS-PAGE respectively. These data demonstrate that cold-acclimation of hamster brown adipose tissue is associated with preferential decrease in the plasma membrane density of the short variant of the Gsalpha protein.%This decrease was paralleled by an increase in the other plasma membrane constituents, [3H]CGP12177 binding sites, [3H]ouabain binding sites and Na,K-ATPase activity to 147%, 212% and 191% respectively.
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