Bovine chromaffin granules: Immunological studies with antisera against neuropeptide Y, [Met]enkephalin and bombesin

Fischer‐Colbrie, Reiner; Díez-Guerra, J; Emson, P.C.; Winkler, Hans

doi:10.1016/0306-4522(86)90185-5

Cited by 45 publications

(11 citation statements)

References 35 publications

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“…All gastrinomas tested in one series were positve for chromogranin A screening [224]. Somatostatin and insulin producing cells produce little to no chromogranin A [225,226]. Both functioning and nonfunctioning tumors demonstrate elevated chromogranin A and no normal controls tested have exhibited these marker elevations [222,223,[227][228][229].…”

Section: Circulating Markers For Pancreatic Endocrine Tumorsmentioning

confidence: 99%

Pancreatic endocrine tumors

Mansour

Chen

2004

Journal of Surgical Research

137

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Section: Circulating Markers For Pancreatic Endocrine Tumorsmentioning

confidence: 99%

Pancreatic endocrine tumors

Mansour

Chen

2004

Journal of Surgical Research

137

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“…Splanchnic nerve stimulation of isolated perfused porcine adrenal glands elicits the release of catecholamines followed by secretion of adrenal steroids (15). In addition to catecholamines, chromaffin cells produce and secrete a wide variety of neurotransmitters, neuropeptides, and proteins (16). The major soluble proteins in chromaffin vesicles are the chromogranins, with chromogranin B being the dominant chromogranin in mice (17).…”

mentioning

confidence: 99%

Deletion of tyrosine hydroxylase gene reveals functional interdependence of adrenocortical and chromaffin cell system in vivo

Bornstein

Tian

Haidan

et al. 2000

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

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Catecholamines are produced in the medulla of the adrenal gland and may participate in the intraglandular regulation of its cortex. We analyzed the adrenal structure and function of albino tyrosine hydroxylase-null (TH-null) mice that are deficient in adrenal catecholamine production. Adrenal catecholamines were markedly reduced, and catecholamine histofluorescence was abrogated in 15-day-old TH-null mice. Chromaffin cell structure was strikingly altered at the ultrastructural level with a depletion of chromaffin vesicles and an increase in rough endoplasmic reticulum compared with wild-type mice. Remaining chromaffin vesicles lined up proximally to the cell membrane in preparation for exocytosis providing a ''string-ofpearls'' appearance. There was a 5-fold increase in the expression of proenkephalin mRNA (502.8 ؎ 142% vs. 100 ؎ 17.5%, P ‫؍‬ 0.016) and a 2-fold increase in the expression of neuropeptide Y (213.4 ؎ 41.2% vs. 100 ؎ 59.9%, P ‫؍‬ 0.014) in the TH-null animals as determined by quantitative TaqMan (Perkin-Elmer) PCR. Accordingly, immunofluorescence for met-enkephalin and neuropeptide tyrosine in these animals was strongly enhanced. The expression of phenylethanolamine N-methyl transferase and chromogranin B mRNA was similar in TH-null and wild-type mice. In TH-null mice, adrenocortical cells were characterized by an increase in liposomes and by tubular mitochondria with reduced internal membranes, suggesting a hypofunctional state of these steroid-producing cells. In accordance with these findings, plasma corticosterone levels were decreased. Plasma ACTH levels were not significantly different in TH-null mice. In conclusion, both the adrenomedullary and adrenocortical systems demonstrate structural and functional changes in catecholaminedeficient TH-null mice, underscoring the great importance of the functional interdependence of these systems in vivo.

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“…There exists no direct evidence for this yet. However, evidence for vesicular colocalization of different peptides has been found, e.g., for somatostatin and NPY in the cortex (De Quidt et al, 1985); for somatostatin and enkephalin in the median eminence (Beauvillain et al, 1984); or NPY, enkephalin, and chromogranins in the adrenal medulla (Fischer-Colbrie et al, 1986). Furthermore, to our knowledge no sorting out mechanism allowing differential packing of the freshly synthesized prepropeptides (Eipper et al, 1986) has been found yet.…”

Section: Discussionmentioning

confidence: 91%

Effect of Local Injection of Cysteamine and Cystamine on Somatostatin and Neuropeptide Y Levels in the Rat Striatum

Widmann

Maas

Sperk

1988

Journal of Neurochemistry

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Cysteamine and its dimeric form cystamine have been applied to the rat striatum by local injection. Both compounds resulted in a dose-dependent decrease of somatostatin levels. Maximal reduction of somatostatin (by about 50%) was obtained at a dose of 50 micrograms of cysteamine or cystamine after about 6 h. All three molecular weight forms of somatostatin--somatostatin-14, somatostatin-28, and the 13,000 molecular weight form of somatostatin--were reduced, as shown by size exclusion HPLC. Injection of radiolabeled cystamine revealed a fast conversion of the compound to cysteamine, suggesting it is active in the monomeric form. The levels of neuropeptide Y, which is colocalized with somatostatin in striatal neurons, failed to be changed by local or intraperitoneal injection of cysteamine, suggesting that this treatment does not affect vesicles of somatostatin/neuropeptide Y neurons.

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Bovine chromaffin granules: Immunological studies with antisera against neuropeptide Y, [Met]enkephalin and bombesin

Cited by 45 publications

References 35 publications

Pancreatic endocrine tumors

Pancreatic endocrine tumors

Deletion of tyrosine hydroxylase gene reveals functional interdependence of adrenocortical and chromaffin cell system in vivo

Effect of Local Injection of Cysteamine and Cystamine on Somatostatin and Neuropeptide Y Levels in the Rat Striatum

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