Abstract
The interaction of glucagon with its receptor on the plasma membranes of liver cells has been the subject of intensive research (see Chap. 13), and it has been established that the initial step in the effect of glucagon on liver function is specific binding of glucagon to the outside of liver cell membranes. The work of Rodbell et al. (1971) showed that glucagon associated highly specifically with its receptor in a reversible manner, with an equilibrium constant for dissociation of approximately 4 X 10-9 M. Furthermore, it was found that very small changes in the structure of the glucagon molecule interfered markedly with its ability to activate the adenylate cyclase associated with the receptor on cell membranes. It was therefore conceivable, that a radioreceptorassay for glucagon, i.e., an assay based on the principles of competitive protein binding assays like radioimmunoassays, but utilizing the glucagon receptors as the binding reagent, might throw some light on the many specificity problems associated with the radioimmunologic determination of glucagon in biologic fluids (Holst 1978 b). Not only are substances with glucagon-like immunoreactivity produced in many tissues outside the pancreatic A-cells (Holst 1978 b), but also plasma contains peptides with glucagon-like immunoreactivity, which are not derived from the pancreas or differ in size from the originally isolated molecule (see Chap. 11). If any of these substances were capable of binding to the glucagon receptor and possibly activating adenylate cyclase, the radioreceptorassay might more accurately predict the total glucagon-like bioactivity in a given sample, and therefore be a more interesting biologic parameter than even the most restrictive and “specific” radioimmunoassay.
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Holst, J.J. (1983). Radioreceptorassays for Glucagon. In: Lefèbvre, P.J. (eds) Glucagon I. Handbook of Experimental Pharmacology, vol 66 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68866-9_12
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DOI: https://doi.org/10.1007/978-3-642-68866-9_12
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