Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01350 (gastrin)
 9,683 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Blood and gastrointestinal tissues of the sea hare Aplysia californica and the land snail Otala lactea contain immunoreactive gastrin in heterogeneous forms similar to those of mammals. The observation that blood concentrations in terms of porcine gastrin standard are comparable to those of pig, man, and dog suggests significant homology between the structures of molluscan and mammalian gastrins.
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PMID:Molluscan gastrin: concentration and molecular forms. 118 66

An immunocytochemical method was used for localization of various peptide-like substances in the Ascaris nervous system. Out of 45 antipeptide antisera, 12 demonstrated immunoreactivity in different subsets of neurons; these 12 antisera were raised against luteinizing hormone-releasing hormone (LHRH), Aplysia peptide L11 (L11), Aplysia peptide 12B (12B), small cardioactive peptide B (SCPB), neuropeptide Y (NPY), FMRFamide, gastrin-17, cholecystokinin octapeptide (CCK-8), alpha-melanocyte stimulating hormone (alpha MSH), calcitonin gene related peptide (CGRP), corticotropin releasing factor (CRF), and vasoactive intestinal peptide (VIP). Several peptide-like substances were colocalized to the same neuron. Our results suggest that Ascaris, like other organisms, contains multiple peptidergic systems.
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PMID:Neuropeptide diversity in Ascaris: an immunocytochemical study. 234 16

The identified neuron, B13, located bilaterally in the buccal ganglion of the marine mollusc Aplysia californica, contains a classical neurotransmitter (acetylcholine) and a cholecystokinin/gastrin-like (CCK/G-li) peptide. The following study demonstrates that B13 makes direct synaptic connections with several identifiable postsynaptic follower neurons. These follower neurons also receive convergent input from previously identified cholinergic neurons, B4 and B5, which do not contain a CCK/G-li peptide. The cholinergic responses mediated by B4/B5 and B13 are similar, including in at least one buccal follower, a two-component inhibitory response not seen in previous studies of the buccal ganglia circuits. However, when the cholinergic responses are blocked by appropriate antagonists, a residual, slow depolarizing, chemically-mediated response is observed in two of the identifiable followers when action potentials are evoked in B13 but not when action potentials are evoked in B4 or B5.
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PMID:Synaptic connections in the buccal ganglia of Aplysia mediated by an identified neuron containing a CCK/gastrin-like peptide co-localized with acetylcholine. 276 97

Immunohistochemical procedures were applied to wholemounts of the central nervous system and posterior intestine of the mollusc, Aplysia californica, to facilitate localization of cells that were immunoreactive to several antisera recognizing various epitopes of the peptides cholecystokinin and gastrin. Only antisera that recognized the carboxyl terminal sequence common to cholecystokinin and gastrin reacted with the Aplysia tissues tested. Intracellular electrophysiological studies of identified postsynaptic targets of immunoreactive neurons in the cerebral ganglia indicated that mammalian forms of gastrin 1-17, several cholecystokinin fragments, and the related peptide, amphibian caerulein, did not mimick the synaptic response mediated by the immunoreactive presynaptic neurons. Combinations of electrophysiological, immunohistochemical, and biochemical studies of several neurons in the buccal ganglia indicated that neurons B7 and B13 were immunoreactive to antisera against cholecystokinin and gastrin and that neuron B13 also contained a concentration of the neurotransmitter acetylcholine as high as in the identified cholinergic buccal neurons, B4 and B5. Several differences in the immunoreactivity of the various antisera were observed. Only one of the antisera was effective in staining neurons in the abdominal ganglia and another antiserum stained subsets of neurons that were immunoreactive to most of the other antisera recognizing the carboxyl terminus common to cholecystokinin and gastrin. The giant serotoninergic metacerebral neurons in Aplysia were not immunoreactive to the cholecystokinin/gastrin antisera even though it has been reported that the homologous neurons in a pulmonate mollusc contain cholecystokinin-like immunoreactivity. These studies demonstrated that there are many neurons with cholecystokinin/gastrin-like immunoreactivity in the Aplysia central and peripheral nervous system and suggested that the peptide may differ from vertebrate forms of cholecystokinin and gastrin. The identification of immunoreactive neurons with known postsynaptic target neurons and buccal neurons with acetylcholine co-localized with a cholecystokinin/gastrin-like peptide will facilitate elucidation of the functions of peptides in the nervous system since the Aplysia preparation is well known to be amenable to multidisciplinary studies.
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PMID:Localization and identification of neurons with cholecystokinin and gastrin-like immunoreactivity in wholemounts of Aplysia ganglia. 353 15

Gastrin/cholecystokinin-like immunoreactivity (G/CCK-LI) was localized by immunocytochemistry in neurons in the central nervous system of Aplysia californica. Neuronal cell bodies were specifically immunostained in the buccal, cerebral, pedal, and abdominal ganglia but not in the pleural ganglia. Neural G/CCK-LI processes were observed in the neuropil of all ganglia and connectives and in some but not all of the peripheral nerves examined. Somata containing G/CCK-LI ranged from 15 to 200 micron in diameter. Ganglionic G/CCK-LI was most efficiently extracted in neutral or basic solutions and consisted mainly of a substance eluting in a volume corresponding to a peptide of between 8 and 17 amino acid residues on gel filtration. This G/CCK-LI diluted in parallel to mammalian gastrin in radioimmunoassays using two antisera differing in their specificities for the bioactive COOH-terminal region of mammalian G/CCK. We conclude that G/CCK-LI is distributed widely in the central and peripheral nervous systems of Aplysia californica and that this immunoreactivity probably represents a small peptide which is similar but not identical to mammalian gastrins and cholecystokinins at the functionally critical COOH terminus.
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PMID:Localization and characterization of gastrin/cholecystokinin-like immunoreactivity in the central nervous system of Aplysia californica. 672 36

Twenty-six species of invertebrates representing eight phyla were surveyed for the presence of cholecystokinin/gastrin-like (CCK/gastrin-like) peptides by radioimmunoassay of various tissue extracts. This is the first report of the presence of CCK/gastrin-like peptides in representatives of the phylum Ectoprocta, the arthropodan classes Crustacea and Merostomata, and in the nervous systems of the gastropod mollusc Aplysia californica and the oligochaete annelid Lumbricus terrestris. It has been proposed that CCK/gastrin evolved in the invertebrates as a neural peptide and was subsequently exploited by the vertebrates as a regulatory peptide in both the nervous system and the gastrointestinal endocrine system. The present results indicate that some gastropod molluscs, a merostomatan arthropod, and an annelid have detectable CCK/gastrin in both nervous and gut tissue. However, extractable CCK/gastrin was found only in gut tissue and not in the central nervous system of a crustacean arthropod. The tissue origin of the extracted CCK/gastrin in Bugula (phylum Ectoprocta) was not determined. Final resolution of the question of the nervous versus gut endocrine cellular origin of CCK/gastrin in invertebrates awaits further investigation. CCK/gastrin-like peptides are widely distributed among the invertebrates, which thus provide a rich source of comparative material for study of these regulatory substances.
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PMID:Species and tissue distribution of cholecystokinin/gastrin-like substances in some invertebrates. 688 52