Interaction of porcine vasoactive intestinal peptide with dispersed pancreatic acinar cells from the guinea pig. Structural requirements for effects of vasoactive intestinal peptide and secretin on cellular adenosine 3':5'-monophosphate.

Robberecht, Patrick; Conlon, Thomas P.; Gardner, Jerry D.

doi:10.1016/s0021-9258(17)33249-0

Cited by 193 publications

(22 citation statements)

References 16 publications

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“…by the ability of secretin fragments, deprived of the N-terminal extremity, to inhibit selectively the stimulatory effects of secretin on adenylate cyclase. The inhibitory effect of such secretin fragments is exerted on both high-and low-affinity secretin receptors interacting with adenylate cyclase in rat pancreatic membranes [2,3,4,8]. In the présent study, the activation of adenylate cyclase by Gila monster venom was inhibited by secretin-(4-27) and secretin-(7-27) as efficiently as that of secretin but it was not possible to discriminate the interaction of Gila monster venom with high-afTinity secretin receptors from that with low-affinity secretin receptors;…”

Section: Discussionmentioning

confidence: 99%

Interaction of Gila monster venom with secretin receptors in rat pancreatic membranes

et al. 1984

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The stimulatory effect of Gila monster venom on adenylate cyclase activity in rat pancreatic membranes was compared to that of porcine secretin and porcine VIP. The maximal effect exerted by the venom was identical to that of VIP but significantly lower than that of secretin. The effect of Gila monster venom could, however, be attributed to its interaction with secretin receptors rather than with VIP receptors, at variance with its previously described action on guinea pig pancreatic acini. Adenylate cyclase activation by both Gila monster venom and secretin in rat pancreatic membranes was, indeed: (1) dose-dependently inhibited by two secretin fragments secretin-(4-27) and secretin-(7-27), and (2) more severely depressed than VIP stimulation, after pretreating pancreatic membranes with dithiothreitol (DTT).

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Section: Discussionmentioning

confidence: 99%

Interaction of Gila monster venom with secretin receptors in rat pancreatic membranes

et al. 1984

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“…Secretin fragments lacking the N-terminal séquence His-Ser-Asp-Gly are usually inactive (8)(9)(10)(11) or only extremely weak partial agonists of secretin on other biological préparations (12). They can however recognize secretin receptors and inhibit the biological effect of secretin (13). For instance, secretin(5-27) and secretin(7-27) specifically inhibit the production of cyclic AMP in, respectively, pancreatic acinar cells from guinea pig (13) and rat pancreatic plasma membranes incubated in the présence of secretin (9).…”

Section: Discussionmentioning

confidence: 99%

“…They can however recognize secretin receptors and inhibit the biological effect of secretin (13). For instance, secretin(5-27) and secretin(7-27) specifically inhibit the production of cyclic AMP in, respectively, pancreatic acinar cells from guinea pig (13) and rat pancreatic plasma membranes incubated in the présence of secretin (9). Both fragments are by contrast without effect on VIP stimulations.…”

Section: Discussionmentioning

confidence: 99%

Specificity of receptors to vasoactive intestinal peptide in guinea pig brain

et al. 1979

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SumtïiaryThe spécifie binding of VIP to guinea pig brain membranes was tested by 1/ the ability of eight VIP and secretin analogs and fragments to inhibit the binding of 125IVIP and 2/ the eapacity of the same peptides to influence basai and VIP stimulated adenylate cyclase activities. Among ail peptides tested, only VIP , secretin, [ValS] secretin, and [Gln9, As n 15] secret in (5-27) were able to inhibit i25i-vip binding. The adenylate cyclase activity was stimulated by VIP , secretin and [Val5]secretin. [Gln9,Asn15]secretin (527) although inactive per se was able to inhibit the VIP stimulated adenylate cyclase activity competi tively.

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“…Although this provides for simple synthesis, the chemisorbed CCK was shown to dissociate from MION. Furthermore, the CCK receptor density on pancreas is not as high as that of other receptor systems, such as secretin receptors (8).…”

Section: Introductionmentioning

confidence: 90%

Magnetically Labeled Secretin Retains Receptor Affinity to Pancreas Acinar Cells

et al. 1996

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Previously, we have developed a colloidal dextran-stabilized monocrystalline iron oxide nanocompound (MION-46) as a magnetic label for magnetic resonance imaging (MRI). In an effort to use this magnetic label to visualize pancreatic receptor function by MRI in vivo, we investigated the potential of secretin as a vector molecule. Secretin receptors, abundant on exocrine pancreas cells, recognize secretin through its amidated carboxyl terminal. In order to conjugate secretin to MION, we utilized the specific interaction between biotin and streptavidin, since direct conjugation of human secretin to MION has previously resulted in low yields and low affinity of the conjugate (unpublished results). Initially, we biotinylated the N-terminal primary amino group of secretin (60% yield). In a separate step, streptavidin (SA) was immobilized onto the surface dextran molecules of MION (79% yield) by reductive amination. Each secretin molecule was conjugated to one biotin molecule and each MION particle to an average of two SA molecules. The biotinylated secretin was then conjugated to MION through the biotin-streptavidin interaction (90% yield). The secretin-biotin-streptavidin-MION construct thus contained approximately two secretin molecules per MION. An in vitro competitive binding assay of pancreatic acinar cells demonstrated that the magnetically labeled secretin retained affinity to the secretin receptors. In vivo distribution studies in rats showed a significantly higher pancreatic accumulation of the secretin-biotin-streptavidin-MION construct as compared to the control group that had received unmodified MION. Our data indicate that bioactive peptides can be attached to dextran-coated iron oxide particles through the biotin-streptavidin interaction while retaining receptor affinity. Such target-specific agents have potential use in MR imaging to probe for a variety of receptor systems.

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Interaction of porcine vasoactive intestinal peptide with dispersed pancreatic acinar cells from the guinea pig. Structural requirements for effects of vasoactive intestinal peptide and secretin on cellular adenosine 3':5'-monophosphate.

Cited by 193 publications

References 16 publications

Interaction of Gila monster venom with secretin receptors in rat pancreatic membranes

Interaction of Gila monster venom with secretin receptors in rat pancreatic membranes

Specificity of receptors to vasoactive intestinal peptide in guinea pig brain

Magnetically Labeled Secretin Retains Receptor Affinity to Pancreas Acinar Cells

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