title: ECL cell morphology.
abstract: Using immunohistochemistry at the conventional light, confocal and electron microscopic levels, we have demonstrated that rat stomach ECL cells store histamine and pancreastatin in granules and secretory vesicles, while histidine decarboxylase occurs in the cytosol. Furthermore the ECL cells display immunoreactivity for vesicular monoamine transporter type 2 (VMAT-2), synaptophysin, synaptotagmin III, vesicle-associated membrane protein-2, cysteine string protein, synaptosomal-associated protein of 25 kDa, syntaxin and Munc-18. Using electron microscopy in combination with stereological methods, we have evidence to suggest the existence of both an exocytotic and a crinophagic pathway in the ECL cells. The process of exocytosis in the ECL cells seems to involve a class of proteins that promote or participate in the fusion between the granule/vesicle membrane and the plasma membrane. The granules take up histamine by VMAT-2 from the cytosol during transport from the Golgi zone to the more peripheral parts of the cells. As a result, they turn into secretory vesicles. As a consequence of stimulation (e.g., by gastrin), the secretory vesicles fuse with the cell membrane to release their contents by exocytosis. The crinophagic pathway was studied in hypergastrinemic rats. In the ECL cells of such animals, the secretory vesicles were found to fuse not only with the cell membrane but also with each other to form vacuoles. Subsequent lysosomal degradation of the vacuoles and their contents resulted in the development of lipofuscin bodies.
authors.affiliation: Department of Pharmacology, University of Lund, Sweden.
authors.forename: D
authors.initials: D
authors.lastname: Chen
authors.forename: C M
authors.initials: CM
authors.lastname: Zhao
authors.forename: K
authors.initials: K
authors.lastname: Andersson
authors.forename: B
authors.initials: B
authors.lastname: Meister
authors.forename: P
authors.initials: P
authors.lastname: Panula
authors.forename: R
authors.initials: R
authors.lastname: Håkanson
mesh_terms: D000818:Animals; D002135:Calcium-Binding Proteins; D053379:Chromogranin A; D006224:Cricetinae; D003594:Cytoplasmic Granules / Q000648:ultrastructure; D019861:Enterochromaffin-like Cells / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005753:Gastric Mucosa / Q000166:cytology / Q000378:metabolism; D005755:Gastrins / Q000494:pharmacology; D006632:Histamine / Q000378:metabolism; D006640:Histidine Decarboxylase / Q000037:antagonists & inhibitors / Q000378:metabolism; D008062:Lipofuscin / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008762:Methylhistidines / Q000494:pharmacology; D051379:Mice; D008853:Microscopy; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009853:Omeprazole / Q000494:pharmacology; D015388:Organelles / Q000145:classification; D010187:Pancreatic Hormones / Q000378:metabolism; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D051381:Rats; D012110:Reserpine / Q000494:pharmacology; D050825:Synaptosomal-Associated Protein 25; D050857:Synaptotagmins; D014617:Vacuoles / Q000378:metabolism / Q000648:ultrastructure*
chemical_list: D002135:Calcium-Binding Proteins; D053379:Chromogranin A; D004791:Enzyme Inhibitors; D005755:Gastrins; D008062:Lipofuscin; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D008762:Methylhistidines; D009419:Nerve Tissue Proteins; D010187:Pancreatic Hormones; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; C494209:Snap25 protein, mouse; C494210:Snap25 protein, rat; D050825:Synaptosomal-Associated Protein 25; C494289:Syt3 protein, mouse; C494291:Syt3 protein, rat; C050836:pancreastatin; D050857:Synaptotagmins; C028309:alpha-fluoromethylhistidine; D006632:Histamine; D012110:Reserpine; D006640:Histidine Decarboxylase; D009853:Omeprazole