Distribution of bombesin binding sites in the rat gastrointestinal tract

Moran, Timothy H.; Moody, Terry W.; Hostetler, Anne M.; Robinson, Paul H.; Goldrich, Michael S.; McHugh, Paul R.

doi:10.1016/0196-9781(88)90177-5

Cited by 76 publications

(35 citation statements)

References 16 publications

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“…1), confirming that the VOI used for quantification of BCM is indeed located in the pancreas. As previously described, the pancreas is the organ with the highest uptake of the bombesin analogue in the peritoneal cavity of rats [28], due to efficient binding to the gastrin-releasing peptide receptor, which is abundantly expressed in the pancreas [29,30]. Removal of both kidneys enabled more accurate visualisation of the pancreas, showing exact co-localisation of 99m Tc-labelled demobesin and 111 In-labelled exendin as an additional proof that the VOI used for quantification contained the pancreas (ESM Fig.…”

Section: Spect Of Dissected Tissuesmentioning

confidence: 99%

Non-invasive quantification of the beta cell mass by SPECT with 111In-labelled exendin

et al. 2014

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Aims/hypothesis A reliable method for in vivo quantification of pancreatic beta cell mass (BCM) could lead to further insight into the pathophysiology of diabetes. The glucagonlike peptide 1 receptor, abundantly expressed on beta cells, may be a suitable target for imaging. We investigated the potential of radiotracer imaging with the GLP-1 analogue exendin labelled with indium-111 for determination of BCM in vivo in a rodent model of beta cell loss and in patients with type 1 diabetes and healthy individuals. MethodsThe targeting of 111 In-labelled exendin was examined in a rat model of alloxan-induced beta cell loss. Rats were injected with 15 MBq 111 In-labelled exendin and single photon emission computed tomography (SPECT) acquisition was performed 1 h post injection, followed by dissection, biodistribution and ex vivo autoradiography studies of pancreatic sections. BCM was determined by morphometric analysis after staining with an anti-insulin antibody. For clinical evaluation SPECT was acquired 4, 24 and 48 h after injection of 150 MBq 111 In-labelled exendin in five patients with type 1 Maarten Brom and Wietske Woliner-van der Weg contributed equally to this study. Diabetologia (2014) 57:950-959 DOI 10.1007 diabetes and five healthy individuals. The tracer uptake was determined by quantitative analysis of the SPECT images. Results In rats, 111 In-labelled exendin specifically targets the beta cells and pancreatic uptake is highly correlated with BCM. In humans, the pancreas was visible in SPECT images and the pancreatic uptake showed high interindividual variation with a substantially lower uptake in patients with type 1 diabetes. Conclusions/interpretation These studies indicate that 111 Inlabelled exendin may be suitable for non-invasive quantification of BCM.

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Section: Spect Of Dissected Tissuesmentioning

confidence: 99%

Non-invasive quantification of the beta cell mass by SPECT with 111In-labelled exendin

et al. 2014

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“…'25I-GRP binding was performed using methods adapted from Moran et al (25) and Kris et al (26). Cryostat sections (10 Am thick) were warmed to room temperature and washed in CMRL media with aprotinin (400 kallikrein inhibitory units/ml; Sigma Chemical Co.) and 0.5% BSA for 30 min at 250C.…”

Section: Methodsmentioning

confidence: 99%

“…The common carboxy-terminal sequence is essential for receptor recognition and biological activity. Other GRP-related peptides include GRP [18][19][20][21][22][23][24][25][26][27] (GRP [10]; neuromedin C), and GRP [14][15][16][17][18][19][20][21][22][23][24][25][26][27] (GRP [14]; references 3 and 4). GRP is located in nerve fibers (1) and pulmonary neuroendocrine cells (1), and can be detected in plasma (5,6).…”

Section: Introductionmentioning

confidence: 99%

Gastrin-releasing peptide in human nasal mucosa.

Baraniuk¹,

Lundgren²,

Goff³

et al. 1990

J. Clin. Invest.

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Gastrin-releasing peptide (GRP), the 27 amino acid mammalian form of bombesin, was studied in human inferior turbinate nasal mucosa. The GRP content of the mucosa measured by radioimmunoassay was 0.60±0.25 pmol/g tissue (n = 9 patients; mean±SEM). GRP-immunoreactive nerves detected by the immunogold method of indirect immunohistochemistry were found predominantly in small muscular arteries, arterioles, venous sinusoids, and between submucosal gland acini.I25I-GRP binding sites determined by autoradiography were exclusively and specifically localized to nasal epithelium and submucosal glands. There was no binding to vessels. The effects of GRP on submucosal gland product release were studied in short-term explant culture. GRP (10 ALM) significantly stimulated the release of the serous cell-specific product lactoferrin, and [3Hlglucosamine-labeled glycoconjugates which are products of epithelial goblet cells and submucosal gland cells. These observations indicate that GRP released from nerve fibers probably acts on glandular GRP receptors to induce glycoconjugate release from submucosal glands and epithelium and lactoferrin release from serous cells, but that GRP would probably not affect vascular permeability. (J. Clin. Invest. 1990. 85:998-1005.) gastrin-releasing peptide -human inferior turbinate nasal mucosa * respiratory glycoconjugateslactoferrin * explant culture

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“…In adult animals, GRP-R and NMB-R are widely expressed in the central nervous system (10) and gastrointestinal tract (14,15), whereas BRS-3 shows limited expression in the hypothalamus but is expressed in secondary spermatocytes (12). In the central nervous system, GRP-R expression is most prominent in several hypothalamic nuclei that are associated with feeding behavior, thermoregulation, and glucose regulation, whereas NMB-R is absent from these regions (16).…”

mentioning

confidence: 99%

Loss of bombesin-induced feeding suppression in gastrin-releasing peptide receptor-deficient mice

Hampton

Ladenheim

Akeson

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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The gastrin-releasing peptide receptor (GRP-R) is one of three members of the mammalian bombesin subfamily of seven-transmembrane G protein-coupled receptors that mediate diverse biological responses including secretion, neuromodulation, chemotaxis, and growth. The X chromosome-linked GRP-R gene is expressed widely during embryonic development and predominantly in gastrointestinal, neuronal, and neuroendocrine systems in the adult. Surprisingly, gene-targeted mice lacking a functional GRP-R gene develop and reproduce normally and show no gross phenotypic abnormalities. However, peripheral administration of bombesin at dosages up to 32 nmol͞kg to such mice had no effect on the suppression of glucose intake, whereas normal mice showed a dose-dependent suppression of glucose intake. These data suggest that selective agonists for the GRP-R may be useful in inducing satiety.

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Distribution of bombesin binding sites in the rat gastrointestinal tract

Cited by 76 publications

References 16 publications

Non-invasive quantification of the beta cell mass by SPECT with 111In-labelled exendin

Non-invasive quantification of the beta cell mass by SPECT with 111In-labelled exendin

Gastrin-releasing peptide in human nasal mucosa.

Loss of bombesin-induced feeding suppression in gastrin-releasing peptide receptor-deficient mice

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