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
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
9924180
DOI
10.1677/jme.0.0220055
Knihovny.cz E-zdroje
- MeSH
- aklimatizace fyziologie MeSH
- buněčná membrána metabolismus MeSH
- centrifugace - gradient hustoty MeSH
- hnědá tuková tkáň metabolismus MeSH
- inhibitory enzymů metabolismus farmakologie MeSH
- křečci praví MeSH
- křeček rodu Mesocricetus fyziologie MeSH
- membránové proteiny metabolismus MeSH
- mitochondrie metabolismus MeSH
- molekulová hmotnost MeSH
- nízká teplota * MeSH
- ouabain metabolismus farmakologie MeSH
- propanolaminy metabolismus MeSH
- protein - isoformy nedostatek izolace a purifikace fyziologie MeSH
- proteiny vázající GTP - alfa-podjednotky Gs nedostatek izolace a purifikace fyziologie MeSH
- sodíko-draslíková ATPasa antagonisté a inhibitory metabolismus MeSH
- zvířata MeSH
- Check Tag
- křečci praví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- CGP 12177 MeSH Prohlížeč
- inhibitory enzymů MeSH
- membránové proteiny MeSH
- ouabain MeSH
- propanolaminy MeSH
- protein - isoformy MeSH
- proteiny vázající GTP - alfa-podjednotky Gs MeSH
- sodíko-draslíková ATPasa 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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