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)

Adrenomedullin is a novel hypotensive adrenal polypeptide originally isolated from a human pheochromocytoma and is structurally related to calcitonin gene-related peptide and islet amyloid polypeptide. Using immunocytochemistry, the occurrence of adrenomedullin in the adrenal gland and gastro-entero-pancreatic region in the rat was examined and its effect on insulin secretion from isolated rat islets was determined. Adrenomedullin-like immunoreactivity occurred in noradrenaline- and adrenaline-producing cells in the adrenal gland. Gastrointestinal endocrine cells, with increased density distally, displayed adrenomedullin-like immunoreactivity; these cells constituted a subpopulation of the enterochromaffin (serotonin-containing) cells. Co-localization of adrenomedullin with somatostatin, glicentin, gastrin/cholecystokinin, peptide YY or islet amyloid polypeptide was not encountered. Adrenomedullin-immunoreactive cells were not observed in the pancreatic islets. At 1, 10 and 100 nmol/l, adrenomedullin stimulated insulin release from isolated rat islets in the presence of 3.3 mmol/l glucose (P < 0.05) and at 100 nmol/l, the peptide potentiated insulin secretion also in the presence of 8.3 mmol/l glucose (P < 0.05). These findings suggest that, besides being an adrenal hypotensive peptide, adrenomedullin may be a gut hormone with a potential insulinotropic function.
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PMID:Adrenomedullin: localization in the gastrointestinal tract and effects on insulin secretion. 879 72

Adrenomedullin (AM) and gastrin releasing peptide (GRP) are neuroendocrine peptides that have been previously implicated as regulators of angiogenesis and lymphangiogenesis. Using an immortalized human dermal microvascular lymphatic endothelial cell line stably transfected with red fluorescent protein (LEC/RFP), we demonstrate the ability of AM and GRP to augment tube formation complexity of this target cell in a dose-dependent manner. Maximum tube density was initiated at 1 nM for both peptides, and as concentrations exceeded 10 nM a decrease in tube formation was noted, hence following a classic rise/fall biological response curve. In addition, we show that appropriate small molecule mimetics to neutralizing monoclonal antibodies of AM or GRP, at 1 microM concentration, can function to either inhibit (antagonist) or enhance (super agonist) peptide-induced tube formation of LEC/RFP. Our small molecule reagents by themselves have no activity, but in the presence of their respective peptides can mediate a positive or negative response, hence the super agonist designation. These compounds represent new regulatory drugs of the lymphatic system with possible patient application in the clinical management of edema and metastatic disease.
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PMID:Non-peptide small molecule regulators of lymphangiogenesis. 2014 17