Expression of SNARE proteins in enteroendocrine cell lines and functional role of tetanus toxin‐sensitive proteins in cholecystokinin release

Némoz-Gaillard, Eric; Bosshard, A.; Regazzi, Romano; Bernard, Christine; Cuber, Jean‐Claude; Takahashi, Masami; Catsicas, Stefan; Chayvialle, Jean‐Alain; Abello, Jacques

doi:10.1016/s0014-5793(98)00209-9

Cited by 21 publications

(14 citation statements)

References 44 publications

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“…In accordance with a previous study in GLUTag and STC-1 cells (Drucker et al 1994), insulin was not detected in any of the cell lines. Our results also confirm data from other studies regarding the presence of GLP-2 in GLUTag and STC-1 cells, and the ability of GLUTag and in particular STC-1 cells, to produce and secrete CCK (Cordier-Bussat et al 1997, Hand et al 2010, Hand et al 2013, Nemoz-Gaillard et al 1998, Sidhu et al 2000.…”

Section: Discussionsupporting

confidence: 91%

Peptide production and secretion in GLUTag, NCI-H716, and STC-1 cells: a comparison to native L-cells

Kuhre¹,

Albrechtsen²,

Deacon³

et al. 2016

Journal of Molecular Endocrinology

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ResearchPeptide production in GLP1-producing cell lines r e kuhre and others 56:3 (2016) 56, 201-211 Journal of Molecular Endocrinology 201-211Key Words AbstractGLUTag, NCI-H716, and STC-1 are cell lines that are widely used to study mechanisms underlying secretion of glucagon-like peptide-1 (GLP-1), but the extent to which they resemble native L-cells is unknown. We used validated immunoassays for 14 different hormones to analyze peptide content (lysis samples; n = 9 from different passage numbers) or peptide secretion in response to buffer (baseline), and after stimulation with 50 mM KCl or 10 mM glucose + 10 µM forskolin/3-isobutyl-1-methylxanthine (n = 6 also different passage numbers). All cell lines produced and processed proglucagon into GLP-1, GLP-2, glicentin, and oxyntomodulin in a pattern (prohormone convertase (PC)1/3 dependent) similar to that described for human gut. All three cell lines showed basal secretion of GLP-1 and GLP-2, which increased after stimulation. In contrast to freshly isolated murine L-cells, all cell lines also expressed PC2 and secreted large amounts of pancreatic glucagon. Neurotensin and somatostatin storage was low and secretion was not consistently increased by stimulation. STC-1 cells released more glucose-dependent insulinotropic polypeptide than GLP-1 at baseline (P < 0.01) and KCl elevated its secretion (P < 0.05). Peptide YY, which normally co-localizes with GLP-1 in distal L-cells, was not detected in any of the cell lines. GLUTag and STC-1 cells also expressed vasoactive intestinal peptide, but none expressed pancreatic polypeptide or insulin. GLUTag contained and secreted large amounts of CCK, while NCI-H716 did not store this peptide and STC-1 contained low amounts. Our results show that hormone production in cell line models of the L-cell has limited similarity to the natural L-cells.

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Section: Discussionsupporting

confidence: 91%

Peptide production and secretion in GLUTag, NCI-H716, and STC-1 cells: a comparison to native L-cells

Kuhre¹,

Albrechtsen²,

Deacon³

et al. 2016

Journal of Molecular Endocrinology

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“…So, we used a toxin to interfere with uv1 cell function and measured effects on egg laying. We used the ocr-2 promoter and 39 regulatory region to express the light chain of tetanus toxin, a protease that cleaves synaptobrevin and prevents neurotransmitter release from neurons (Sweeney et al 1995) and endocrine cells (Nemoz-Gaillard et al 1998). The resulting transgenic animals exhibited premature egg-laying behavior (Figure 7C), suggesting that neurotransmitters released from uv1 or other cells that express ocr-2 inhibit egg laying.…”

Section: Resultsmentioning

confidence: 99%

A Specific Subset of Transient Receptor Potential Vanilloid-Type Channel Subunits inCaenorhabditis elegansEndocrine Cells Function as Mixed Heteromers to Promote Neurotransmitter Release

Jose¹,

Bany²,

Chase

et al. 2007

Genetics

106

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Transient receptor potential (TRP) channel subunits form homotetramers that function in sensory transduction. Heteromeric channels also form, but their physiological subunit compositions and functions are largely unknown. We found a dominant-negative mutant of the C. elegans TRPV (vanilloid-type) subunit OCR-2 that apparently incorporates into and inactivates OCR-2 homomers as well as heteromers with the TRPV subunits OCR-1 and -4, resulting in a premature egg-laying defect. This defect is reproduced by knocking out all three OCR genes, but not by any single knockout. Thus a mixture of redundant heteromeric channels prevents premature egg laying. These channels, as well as the G-protein Ga o , function in neuroendocrine cells to promote release of neurotransmitters that block egg laying until eggs filling the uterus deform the neuroendocrine cells. The TRPV channel OSM-9, previously suggested to be an obligate heteromeric partner of OCR-2 in sensory neurons, is expressed in the neuroendocrine cells but has no detectable role in egg laying. Our results identify a specific set of heteromeric TRPV channels that redundantly regulate neuroendocrine function and show that a subunit combination that functions in sensory neurons is also present in neuroendocrine cells but has no detectable function in these cells.

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“…The downstream events that follow the activation of MAPK and lead to CCK secretion are unknown. STC-1 cells express the three synaptic core complex proteins syntaxin-1, synaptosomal-associated protein-25 (SNAP-25), and vesicle-associated membrane protein 2, which plays a key role in vesicle exocytosis (23). Moreover, the activation of MAPK is associated with an increase in the phosphorylation of synapsin I in neuronal preparations (24,25).…”

Section: Discussionmentioning

confidence: 99%

Duodenal Leptin Stimulates Cholecystokinin Secretion

Guilmeau

Buyse²,

Tsocas³

et al. 2003

Diabetes

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Some of the actions of leptin depend on cholecystokinin (CCK). However, it is unknown whether leptin modulates the release of CCK. Here, we demonstrate in vitro that leptin induces the phosphorylation of extracellular signal-related kinase (ERK)-1/2 proteins and increases CCK release (EC 50 ‫؍‬ 0.23 nmol/l) in CCK-secreting STC-1 cells. We showed that rat duodenal juice contains leptin that circulates free and bound to macromolecules, suggesting that leptin has a lumenal action on the intestine. In vivo in the rat, duodenal infusion of leptin increased plasma CCK at levels comparable to those induced by feeding. Moreover, meal-induced increases in plasma CCK were markedly reduced in obese fa/fa rats, whereas the mobilization of the gastric leptin pool was similar in lean and obese Zucker rats. L eptin, the ob gene product, was initially reported to be produced by adipose cells (1). It is released into the bloodstream and transported across the blood-brain barrier into the hypothalamus, where it activates specific leptin receptors (2,3) and regulates energy homeostasis by altering energy intake and expenditure (4 -6). Leptin regulates food intake by mechanisms involving cross-talk between hypothalamic leptin receptors and various neuropeptides involved in the control of feeding. The leptin receptor (Ob-R) is a member of the gp130 family of cytokine receptors. It occurs in several isoforms resulting from the alternative splicing of the db leptin receptor gene (2,3). It is currently thought that the long isoform, Ob-Rb, can activate the signal transducers and activators of transcription (STAT) pathways, whereas both Ob-Rb and the short isoform (Ob-Ra) can transduce signals through insulin receptor substrates and through mitogen-activated protein kinase (MAPK) pathways (7).The signals that arise from the upper gastrointestinal tract upon feeding are transmitted to the brain by the vagus nerve. These signals are key components in the control of meal-induced satiety. Cholecystokinin (CCK) is secreted from duodenal endocrine I cells and typically functions as one of these short-term satiety signals (8,9). Interestingly, the leptin-induced inhibition of food intake (10) and the stimulation of pancreatic exocrine secretions (11) can be blocked by a CCK-1 receptor antagonist. These data suggest that endogenous CCK is involved in these effects, operating through CCK-1 receptors. However, it is not currently known whether leptin directly modulates the release of CCK.Leptin is also produced by the stomach (12-14) and is mainly secreted into the gastric juice after CCK in rats (12,15) and after secretin or vagal stimulation in humans (14,16). Some of the stomach-derived leptin is not fully degraded by proteolysis, indicating that it reaches the intestine in an active form and thus can initiate biological processes controlling functions of the intestinal tract. Indeed, lumenal leptin increases the activity of the brush border proton-dependent transporter, PepT1, which enhances the intestinal absorption of oligopeptides (17). T...

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Expression of SNARE proteins in enteroendocrine cell lines and functional role of tetanus toxin‐sensitive proteins in cholecystokinin release

Cited by 21 publications

References 44 publications

Peptide production and secretion in GLUTag, NCI-H716, and STC-1 cells: a comparison to native L-cells

Peptide production and secretion in GLUTag, NCI-H716, and STC-1 cells: a comparison to native L-cells

A Specific Subset of Transient Receptor Potential Vanilloid-Type Channel Subunits inCaenorhabditis elegansEndocrine Cells Function as Mixed Heteromers to Promote Neurotransmitter Release

Duodenal Leptin Stimulates Cholecystokinin Secretion

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