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  • Title: Interaction of substance P with dispersed pancreatic acinar cells from the guinea pig. Relationships between structure, binding and biological activity.
    Author: Sjödin L, Brodin E, Srivastava G.
    Journal: Acta Physiol Scand; 1984 Jan; 120(1):21-6. PubMed ID: 6202096.
    Abstract:
    Binding of 125I-[Tyr8]-SP to isolated pancreatic acinar cells was inhibited in a concentration-dependent way by SP, [Tyr8]-SP and longer C-terminal fragments of SP. SP6-11 was the shortest sequence to bind significantly to SP-receptors as well as to stimulate amylase release from dispersed pancreatic acini. SP7-11 and shorter fragments did not inhibit binding of 125I-[Tyr8]-SP and did not stimulate secretion of amylase significantly. SP augmented the stimulatory effect of cholecystokinin on amylase release. Two SP-antagonists, [D-Pro2, D-Trp7,9]-SP and [D-Pro2,4, D-Lys3, D-Gln5,6, D-Trp7,9]-SP inhibited binding of 125I-[Tyr8]-SP in a concentration dependent manner and tended at a high concentration to reduce release of amylase evoked by submaximal concentrations of SP.
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