Thyrotropin-releasing hormone-induced depletion of G(q)alpha/G(11)alpha proteins from detergent-insensitive membrane domains
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
Wellcome Trust - United Kingdom
PubMed
10611479
DOI
10.1016/s0014-5793(99)01666-x
PII: S001457939901666X
Knihovny.cz E-resources
- MeSH
- Adenylyl Cyclases metabolism MeSH
- Alkaline Phosphatase metabolism MeSH
- Integrin beta1 metabolism MeSH
- CD55 Antigens metabolism MeSH
- CD59 Antigens metabolism MeSH
- Cell Membrane drug effects metabolism MeSH
- Cell Line MeSH
- Centrifugation, Density Gradient MeSH
- Detergents pharmacology MeSH
- Thyrotropin-Releasing Hormone pharmacology MeSH
- Immunoblotting MeSH
- Caveolin 1 MeSH
- Caveolins * MeSH
- Humans MeSH
- Membrane Proteins metabolism MeSH
- Octoxynol pharmacology MeSH
- GTP-Binding Protein alpha Subunits, Gq-G11 MeSH
- GTP-Binding Proteins chemistry metabolism MeSH
- Sodium-Potassium-Exchanging ATPase metabolism MeSH
- Protein Structure, Tertiary MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Adenylyl Cyclases MeSH
- Alkaline Phosphatase MeSH
- Integrin beta1 MeSH
- CD55 Antigens MeSH
- CD59 Antigens MeSH
- CAV1 protein, human MeSH Browser
- Detergents MeSH
- Thyrotropin-Releasing Hormone MeSH
- Caveolin 1 MeSH
- Caveolins * MeSH
- Membrane Proteins MeSH
- Octoxynol MeSH
- GTP-Binding Protein alpha Subunits, Gq-G11 MeSH
- GTP-Binding Proteins MeSH
- Sodium-Potassium-Exchanging ATPase MeSH
The role of detergent-insensitive membrane domains (DIMs) in desensitisation of the G protein-coupled receptor-mediated hormone response was studied in clone E2M11 of HEK293 cells which stably express high levels of both thyrotropin-releasing hormone (TRH) receptors and G(11)alpha G protein. DIMs were prepared by flotation in equilibrium sucrose density gradients and characterised by a panel of membrane markers representing peripheral, glycosylphosphatidylinositol-bound as well as integral membrane proteins (caveolin, CD29, CD55, CD59, CD147, the alpha subunit of Na, K-ATPase) and enzyme activities (alkaline phosphatase, adenylyl cyclase). Caveolin-containing DIMs represented only a small fraction of the overall pool of G(q)alpha/G(11)alpha-rich domains. Prolonged stimulation of E2M11 cells with TRH resulted in dramatic depletion of G(q)alpha/G(11)alpha from all DIMs, which was paralleled by a concomitant G(q)alpha/G(11)alpha increase in the high-density gradient fractions containing the bulk-phase membrane constituents soluble in 1% Triton X-100. Distribution of membrane markers was unchanged under these conditions. Membrane domains thus represent a substantial structural determinant of the G protein pool relevant to desensitisation of hormone action.
References provided by Crossref.org
Biochemical and physiological insights into TRH receptor-mediated signaling
