After 1-h incubation at room temperature, the plate was measured for baseline luminescence (TECAN). CCK-8 or gastrin-17 at different concentrations (10 μL) was added and incubated for 3–5 min at room temperature before the second measurement. Luminescence counts were normalized to ck444 download app download the initial count and fold-change signals over treatment of the lowest CCK-8 or gastrin-17 concentration were used to show G protein dissociation response. Span, sample size, and expression are provided in Supplementary Tables S3, S4, S7. After the discovery in 1928 (6), CCK became part of the classical troika of gut hormones together with secretin and gastrin.
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Moreover, CCK-8 (sulfated as well as non-sulfated) has been reported to exert a wide specter of stimulation and inhibition on lymphocytes, macrophages, and cytokine release, with ensuing anti-inflammatory effects (108–111). The field is complex due to the many players; but the clinical impact of CCK in inflammatory diseases and endotoxin shock may be significant. The distal part of the gut is as mentioned abundantly innervated with CCK neurons (42, 90). It is therefore likely that an increase of intestinal motor activity by exogenous CCK (91) reflects neuronal control of intestinal muscles by CCK peptide transmission. Neuronal CCK acts both indirectly via acetylcholine release from postganglionic parasympathetic nerves and directly on muscle cells (49). The observation that CCK peptides stimulate intestinal blood flow is in harmony with the occurrence of CCK nerve terminals around blood vessels in the basal lamina propria and the submucosa (42).
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There are species differences, so it is now assumed that CCK in man stimulates pancreatic enzyme secretion through a cholinergic pathway that is less significant in rodents (82–84). The homologous bioactive sequences of peptide systems belonging to the cholecystokinin (CCK) family (upper panel). CCK and the antral hormone, gastrin, are the only mammalian members of the family. Caerulein and phyllocaerulein are identified from frogskin extracts. Cionin is a neuropeptide isolated from the central ganglion of the protochord, ciona intestinalis.
The wild-type human CCK1R and CCK2R with C-terminal 15-residue depleted were subcloned into pFastBac vector with an N-terminal FLAG-tag and C-terminal 10× His-tag. A dominant-negative human Gαs (DNGαs) was generated by site-directed mutagenesis as previously described to limit G protein dissociation. Twenty-nine amino acids at the N-terminus of wild-type Gαq were replaced by the corresponding sequence in Gαi1 to facilitate the binding of scFv16. The constructs were cloned into both pcDNA3.1 and pFastBac vectors for functional assays in mammalian cells and protein expression in insect cells, respectively. All modifications of the receptor had no effect on ligand binding and receptor activation.
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