Quantitative electron microscopy of endocrine cells in oxyntic mucosa of normal human stomach

D’Adda, Tiziana; Bertelè, A.; Pilato, Francesco Paolo; Bordi, Cesare

doi:10.1007/bf00229064

Cited by 51 publications

(43 citation statements)

References 21 publications

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“…These cells contained dense, round secretory granules about 140 ± 200 nm in diameter, preferentially grouped in the basal portion of the cell ( Figure 4). Other endocrine cell types with distinctive ultrastructural features, corresponding to those described for G, D, D 1 and ECL cells, 19,20 were negative.…”

Section: Immunoelectronmicroscopymentioning

confidence: 71%

“…The ultrastructure of the endocrine cell type containing gold-leptin particles suggests that it corresponds to the cell type described as P cell. 20,22 Interestingly, it has recently been shown that leptin interacts synergically with other short-term satiety peptides. 13 We did not ®nd PP, A or X cells (A and X are rare in man) in our samples, therefore we cannot exclude that also these cells show leptin reactivity.…”

Section: Discussionmentioning

confidence: 99%

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Secretory granules of endocrine and chief cells of human stomach mucosa contain leptin

et al. 2000

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BACKGROUND: Leptin plays an important role in the control of food intake and body weight homeostasis. In humans, leptin is produced by adipocytes, placental cells and secretory cells of the mammary epithelium. Recently, it has been reported that stomach glands produce leptin in rats. OBJECTIVE: To test the expression of leptin protein in human stomach and localize, by immunocytochemistry, the speci®c cell type producing leptin. DESIGN: Endoscopic stomach biopsies of six patients were used to investigate leptin production in the fundic epithelium using reverse transcription polymerase chain reaction (RT-PCR) of RNA. Leptin protein was detected by immunoblot analysis and localized by immunohistochemistry and ultrastructural immunocytochemistry (immunogold method). RESULTS: Human gastric epithelium expresses leptin mRNA and leptin protein. The cells in the lower half of the stomach glands were immunoreactive for leptin. Ultrastructural immunocytochemistry showed leptin immunoreactivity in the pepsinogen granules of chief cells, but the granules of a speci®c endocrine cell type in the basal portion of the glands were also positive. CONCLUSIONS: Our results suggest that gastric leptin could function in the short-term system to control feeding behaviour and is probably secreted in the stomach lumen by chief cells and into the stomach circulation by a special type of endocrine cell.

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Section: Immunoelectronmicroscopymentioning

confidence: 71%

Section: Discussionmentioning

confidence: 99%

Secretory granules of endocrine and chief cells of human stomach mucosa contain leptin

et al. 2000

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“…29 Osmication of tissues was omitted to avoid masking of antigenic sites as previously reported in the literature. 30 After exposure with a blocking agent (BSA 3% wt/vol in PBS), ultrathin sections were incubated overnight with anti-AR (diluted 1:200) and anti-SOD2 (diluted 1:50) antibodies.…”

Section: Electron Microscopymentioning

confidence: 99%

Autoimmunity in Membranous Nephropathy Targets Aldose Reductase and SOD2

Prunotto¹,

Carnevali²,

Candiano³

et al. 2010

Journal of the American Society of Nephrology

196

183

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Glomerular targets of autoimmunity in human membranous nephropathy are poorly understood. Here, we used a combined proteomic approach to identify specific antibodies against podocyte proteins in both serum and glomeruli of patients with membranous nephropathy (MN). We detected specific anti-aldose reductase (AR) and anti-manganese superoxide dismutase (SOD2) IgG 4 in sera of patients with MN. We also eluted high titers of anti-AR and anti-SOD2 IgG 4 from microdissected glomeruli of three biopsies of MN kidneys but not from biopsies of other glomerulonephritides characterized by IgG deposition (five lupus nephritis and two membranoproliferative glomerulonephritis). We identified both antigens in MN biopsies but not in other renal pathologies or normal kidney. Confocal and immunoelectron microscopy (IEM) showed co-localization of anti-AR and anti-SOD2 with IgG 4 and C5b-9 in electron-dense podocyte immune deposits. Preliminary in vitro experiments showed an increase of SOD2 expression on podocyte plasma membrane after treatment with hydrogen peroxide. In conclusion, our data support AR and SOD2 as renal antigens of human MN and suggest that oxidative stress may drive glomerular SOD2 expression.

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“…They contain a non-specific 3,4-dihydroxyphenylalanine (DOPA) decarboxylase [56] and are able to take up and utilize a number of aromatic amino acids [57]. Studies with both polyclonal and monoclonal antibodies clearly reveal these cells to be the major histamine source of the gastric mucosa [58, 59, 60, 61]. Immunocytochemical investigations indicate the presence of at least, histamine, pancreastatin, peptide tyrosyl-tyrosine (PYY), enteroglucagon, gastrocalcin, chromogranin and calbindin [62, 63].…”

Section: The Ecl Cellmentioning

confidence: 99%

Gastrin and the Enterochromaffin-Like Cell: An Acid Update

Kidd

Modlin²,

Tang³

1998

Dig Surg

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Gastrin is synthesized and secreted mostly in a heptadecapeptide form from neurocrine G cells located in the antrum. The biologically active sequence of the molecule is a C-terminal pentapeptide, which has been conserved across many species. Transcriptional regulation of gastrin mRNA synthesis is positively regulated by transforming growth factor-α (TGF-α) and inhibited by somatostatin (SST). The inactive precursor form is converted to the active molecule by several posttranslation processing steps which include cleavage, C-terminal amidation, glycosylation, phosphorylation and sulfation. Aberrations in processing steps generate incompletely processed forms, particularly glycosylated progastrin, which may act as autocrine growth factors for gastrointestinal neoplasms. Gastrin release is stimulated by luminal aromatic amino acids and inhibited by a decrease in luminal pH. Other gastrin agonists include β-adrenergic agents, acetylcholine, gastrin-releasing peptide (bombesin), TGF-α, and possibly the gastric pathogen, Helicobacter pylori. The principal peptide inhibitor of gastrin release is SST. The major physiological roles of gastrin include stimulation of acid secretion, regulation of mucosal cell lineage and mucosal cell proliferation. The fundic enterochromaffin-like (ECL) cell is the principal cellular transducer of the gastrin-acid signal. Activation of its gastrin/CCK_B receptor results in histamine synthesis and release with consequent activation of the fundic parietal cell H₂ receptor. An increase in luminal pH caused by acid inhibitory pharmacotherapy agents (particularly proton pump inhibitors) results in hypergastrinemia and ECL cell hyperplasia. Gastric carcinoids however appear occur in patients with multiple endocrine neoplasia type I syndrome, suggesting that an associated genomic defect is necessary. Gastrin is thus both a potent gastrointestinal trophic and histamine secretory agent. As a hormone it is a paradigm in the elucidation of both cellular secretory and growth factor induced cell proliferation.

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Quantitative electron microscopy of endocrine cells in oxyntic mucosa of normal human stomach

Cited by 51 publications

References 21 publications

Secretory granules of endocrine and chief cells of human stomach mucosa contain leptin

Secretory granules of endocrine and chief cells of human stomach mucosa contain leptin

Autoimmunity in Membranous Nephropathy Targets Aldose Reductase and SOD2

Gastrin and the Enterochromaffin-Like Cell: An Acid Update

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