What question did this study set out to answer?

To investigate whether receptor aggregation is required to couple insulin binding with the activation of soluble insulin receptor kinase.

January 1, 1986Journal of Biological ChemistryOpen Access

Receptor aggregation is necessary for activation of the soluble insulin receptor kinase.

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Authors

DHD HeffetzWeizmann Institute of Science YZYehiel ZickWeizmann Institute of Science

Discussion

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Implication

In vitro assay reveals receptor aggregation triggers soluble insulin receptor kinase activation in rat liver extracts, suggesting receptor cross-linking drives transmembrane signaling.

Key Points

To investigate whether receptor aggregation is required to couple insulin binding with the activation of soluble insulin receptor kinase.
Treated solubilized, partially purified insulin receptors from rat liver with human anti-receptor polyclonal antibodies (anti-R IgG), bivalent F(ab')2 fragments, or monovalent Fab' fragments.
Measured the competitive inhibition of insulin binding and assessed kinase activation across antibody forms, including after cross-linking monovalent Fab' fragments with anti-Fab' antibodies.
Anti-R IgG, F(ab')2, and Fab' fragments all competitively inhibited insulin binding to solubilized rat liver receptor preparations.
Only bivalent anti-R IgG and F(ab')2 fragments stimulated receptor kinase activity, whereas monovalent Fab' fragments showed no kinase stimulatory activity.
Cross-linking monovalent Fab' fragments using goat anti-human Fab' fully restored their ability to stimulate receptor kinase activity.

Cite This Study

Heffetz et al. (1986) studied this question.

synapsesocial.com/papers/6a6f5583a528af2d65c2efbb https://doi.org/10.1016/s0021-9258(17)36180-x

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January 1, 1986Journal of Biological ChemistryOpen Access

Receptor aggregation is necessary for activation of the soluble insulin receptor kinase.

View Full Paper

Ask AI

Bookmark

Authors

DHD HeffetzWeizmann Institute of Science YZYehiel ZickWeizmann Institute of Science

Discussion

Member takes

Implication

In vitro assay reveals receptor aggregation triggers soluble insulin receptor kinase activation in rat liver extracts, suggesting receptor cross-linking drives transmembrane signaling.

Key Points

To investigate whether receptor aggregation is required to couple insulin binding with the activation of soluble insulin receptor kinase.
Treated solubilized, partially purified insulin receptors from rat liver with human anti-receptor polyclonal antibodies (anti-R IgG), bivalent F(ab')2 fragments, or monovalent Fab' fragments.
Measured the competitive inhibition of insulin binding and assessed kinase activation across antibody forms, including after cross-linking monovalent Fab' fragments with anti-Fab' antibodies.
Anti-R IgG, F(ab')2, and Fab' fragments all competitively inhibited insulin binding to solubilized rat liver receptor preparations.
Only bivalent anti-R IgG and F(ab')2 fragments stimulated receptor kinase activity, whereas monovalent Fab' fragments showed no kinase stimulatory activity.
Cross-linking monovalent Fab' fragments using goat anti-human Fab' fully restored their ability to stimulate receptor kinase activity.

Cite This Study

Heffetz et al. (1986) studied this question.

synapsesocial.com/papers/6a6f5583a528af2d65c2efbb https://doi.org/10.1016/s0021-9258(17)36180-x

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