What question did this study set out to answer?

To investigate the regulatory effects of guanyl nucleotides and other nucleoside phosphates on glucagon receptor binding and dissociation in rat liver plasma membranes.

March 1, 1971Journal of Biological ChemistryOpen Access

The Glucagon-sensitive Adenyl Cyclase System in Plasma Membranes of Rat Liver

View Full Paper

Ask AI

Bookmark

Authors

MRMartin RodbellNational Institute of Environmental Health Sciences HKH. Michiel J. KransLeiden University Medical Center SPStephen L. PohlUniversity of Kentucky

Discussion

Member takes

Overview

In vitro study shows that guanyl nucleotides allosterically decrease glucagon binding affinity in rat liver membranes, highlighting a rapid mechanism for regulating hormone receptor interactions.

Key Points

To investigate the regulatory effects of guanyl nucleotides and other nucleoside phosphates on glucagon receptor binding and dissociation in rat liver plasma membranes.
Assayed the binding, uptake, and dissociation kinetics of iodine-125-labeled glucagon in isolated rat liver plasma membranes.
Tested concentration dependency, reversibility, temperature dependence (0°C and 30°C), ion requirements, and the effects of GTP analogues, sulfhydryl reagents, and adenyl cyclase activators.
GTP and GDP at concentrations as low as 0.05 µM rapidly and reversibly stimulated glucagon dissociation and decreased receptor affinity without requiring divalent metal ions.
A nonphosphorylating GTP analogue mimicked the natural guanyl nucleotides noncompetitively, while other nucleotides (ATP, ADP, UTP, CTP) required concentrations exceeding 0.1 mM to produce similar binding inhibition.

Cite This Study

Rodbell et al. (1971) studied this question.

synapsesocial.com/papers/6a659b2eeb7a5bf67ec4d5f9 https://doi.org/10.1016/s0021-9258(18)62389-0

View Full Paper

Ask AI

Bookmark

March 1, 1971Journal of Biological ChemistryOpen Access

The Glucagon-sensitive Adenyl Cyclase System in Plasma Membranes of Rat Liver

View Full Paper

Ask AI

Bookmark

Authors

MRMartin RodbellNational Institute of Environmental Health Sciences HKH. Michiel J. KransLeiden University Medical Center SPStephen L. PohlUniversity of Kentucky

Discussion

Member takes

Overview

In vitro study shows that guanyl nucleotides allosterically decrease glucagon binding affinity in rat liver membranes, highlighting a rapid mechanism for regulating hormone receptor interactions.

Key Points

To investigate the regulatory effects of guanyl nucleotides and other nucleoside phosphates on glucagon receptor binding and dissociation in rat liver plasma membranes.
Assayed the binding, uptake, and dissociation kinetics of iodine-125-labeled glucagon in isolated rat liver plasma membranes.
Tested concentration dependency, reversibility, temperature dependence (0°C and 30°C), ion requirements, and the effects of GTP analogues, sulfhydryl reagents, and adenyl cyclase activators.
GTP and GDP at concentrations as low as 0.05 µM rapidly and reversibly stimulated glucagon dissociation and decreased receptor affinity without requiring divalent metal ions.
A nonphosphorylating GTP analogue mimicked the natural guanyl nucleotides noncompetitively, while other nucleotides (ATP, ADP, UTP, CTP) required concentrations exceeding 0.1 mM to produce similar binding inhibition.

Cite This Study

Rodbell et al. (1971) studied this question.

synapsesocial.com/papers/6a659b2eeb7a5bf67ec4d5f9 https://doi.org/10.1016/s0021-9258(18)62389-0

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark