Secretion of neurotensin from a human pancreatic islet cell carcinoma cell line (QGP-1N)
| Autor: | Yuji Matsuoka, Kayoko Tateishi, Noboru Kitayama, Akihiro Funakoshi |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
medicine.medical_specialty
Carbachol Physiology G protein Clinical Biochemistry Neuropeptide Biology digestive system complex mixtures Biochemistry Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology Internal medicine Muscarinic acetylcholine receptor medicine Tumor Cells Cultured Humans Secretion Protein kinase C Neurotensin musculoskeletal neural and ocular physiology digestive oral and skin physiology Receptors Muscarinic Pancreatic Neoplasms chemistry Calcium Carcinoma Islet Cell Secretory Rate hormones hormone substitutes and hormone antagonists Acetylcholine medicine.drug |
| Zdroj: | Regulatory peptides. 49(2) |
| ISSN: | 0167-0115 |
| Popis: | Effects of various secretagogues on secretion of neurotensin from a pancreatic islet cell carcinoma cell line (QGP-1N) were examined. Carbachol stimulated secretion of neurotensin concentration-dependently in the range of 10 −6 –10 −4 M. The neurotensin secretion stimulated with 10 −5 M carbachol was completely inhibited by atropine at 10 −5 M. Phorbol ester and calcium ionophore (A23187) stimulated secretion of neurotensin. The removal of extracellular Ca 2+ suppressed the secretion through the stimulation with 10 −5 M carbachol. Fluoride, an activator of guanine nucleotide-binding (G) protein, stimulated secretion of neurotensin. Neurotensin released into culture medium through stimulation with carbachol coeluted with neurotensin 1–13 on a gelchromatography. Our results suggest that secretion of neurotensin from QGP-1N cells is mainly regulated by acetylcholine through muscarinic receptors coupled to G protein and that an increase in intracellular Ca 2+ and protein kinase C play an important role in stimulus-secretion coupling. |
| Databáze: | OpenAIRE |
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