Interaction of substance P with dispersed pancreatic acinar cells from the guinea pig. Relationships between structure, binding and biological activity.

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.

Statistics

0100200300'91'94'97'00'03'06'09'12'15
Citations per Year

183 Citations

Semantic Scholar estimates that this publication has 183 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Sjdin1984InteractionOS, title={Interaction of substance P with dispersed pancreatic acinar cells from the guinea pig. Relationships between structure, binding and biological activity.}, author={Linnea Sj{\"{o}din and Ernst Brodin and Ghanshyam Srivastava}, journal={Acta physiologica Scandinavica}, year={1984}, volume={120 1}, pages={21-6} }