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The binding of [125I]secretin to rat brain membranes was investigated. Radiolabeled secretin bound with high affinity (KD = 0.2 nM) to a single class of noninteracting sites. Binding was specific, saturable, and reversible. Regional distribution studies indicated that the specific binding was greatest in the cerebellum, intermediate in the cortex, thalamus, striatum, hippocampus, and hypothalamus, and lowest in the midbrain and medulla/pons. Pharmacological studies indicated that only secretin, but not other peptides, inhibits binding of [125I]secretin with high affinity. Also, certain guanine nucleotides inhibited high affinity binding. These data indicate that rat brain membranes possess high affinity binding sites specific for secretin and that with the use of [125I] secretin the kinetics, stoichiometry, specificity, and distribution of secretin receptors can be directly investigated.
R T Fremeau, and
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T L O'Donohue, and
T W Moody
November 1978,
Proceedings of the National Academy of Sciences of the United States of America,
R T Fremeau, and
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C G Charlton, and
R L Miller, and
T L O'Donohue, and
T W Moody
May 1977,
Proceedings of the National Academy of Sciences of the United States of America,
R T Fremeau, and
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C G Charlton, and
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T L O'Donohue, and
T W Moody
February 1979,
Proceedings of the National Academy of Sciences of the United States of America,
R T Fremeau, and
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T W Moody
December 1979,
Naunyn-Schmiedeberg's archives of pharmacology,
R T Fremeau, and
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August 1980,
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R T Fremeau, and
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May 1990,
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January 1989,
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R T Fremeau, and
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T W Moody
May 1980,
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R T Fremeau, and
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September 1983,
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R T Fremeau, and
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T W Moody
December 1976,
Life sciences,
