Prior to 1974, the ~adrenergic receptors were known only in-
directly as entities that responded to drugs in a selective manner
to mediate a variety of physiologically important responses. During
the intervening years, our view of ~adrenergic receptors has
changed dramatically. The availability of high affinity
125I-labeled radioligands selective for these receptors presaged an
explosion of experimenta- tion utilizing direct binding assays to
establish the biochemical properties of the receptor protein. In
the opening chapter, Stadel and Lefkowitz describe this development
and its impact on our under- standing of the molecular basis of
~adrenergic receptor function. The availability of
well-characterized receptor ligands, coupled with the development
of efficient methods for detergent solubilization, formed the basis
of receptor purification using affinity chromatography. The related
technique of photoaffinity labeling provided a means to estimate
the molecular mass of these receptors. The availability of
substantial amounts of purified ~2-adrenergic receptor allowed
determination of segments of its amino acid se- quence. This
information led to the production of polynucleotide probes and
eventually to cloning of the receptor gene and determi- nation of
the complete primary sequence of the receptor protein. Caron and
Lefkowitz review the investigations leading to this major
development and discuss the methods involved. They analyze our
current perception of the relation of receptor function to its
structure and discuss the general features of the G
protein-interacting receptor family, of which the ~-adrenergic
receptors are prototypes.
General
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