Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0031511 (pheochromocytoma)
 14,622 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Normal rodent adrenal chromaffin cells and the PC12 rat pheochromocytoma cell line produce IL-1 cytokines. The role, if any, of these cytokines is currently unknown. In PC12 cells, they induce the expression of the L-AA decarboxylase mRNA, a major step in the biosynthesis of catecholamines. Very little if any of these cytokines are detectable in normal human adrenal medulla, being confined mainly in the 17 alpha-hydroxylase-positive steroid cells of the zona reticularis. The aim of the present work was to find out if human pheochromocytomas produce IL-1 cytokines, in vitro, and to examine what local role they may exert. As a model, we have used the new KAT45 cell line, which emerged spontaneously from a primary human pheochromocytoma cell culture. We have found that the KAT45 cells secrete IL-1 beta at 47.8 +/- 9 pg/mg total cellular protein (n = 7, at 24 hours). IL-1 beta increased the concentration of norepinephrine in the KAT45 culture medium from 24.2 +/- 3.5 micrograms/mg protein (n = 6 controls, at 24 hours), to 33.2 +/- 3.5 (IL-1 beta 10 mg/ml) or to 42.9 +/- 8 (IL-1 beta 30 mg/ml). This effect was blocked by IL-1ra. The KAT45 cells also produce CRH and ACTH. IL-1 beta stimulated the secretion of CRH from 19.2 +/- 4 pg/mg protein (n = 5 at 36 hours) to 38.7 +/- 4, an effect blocked by IL-1ra in excess. IL-1 beta had no effect on ACTH secretion.
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PMID:KAT45 human pheochromocytoma cell line. A new model for the in vitro study of neuro-immuno-hormonal interactions. 962 69

Glut4-containing vesicles represent a regulated recycling compartment in insulin-sensitive fat and skeletal muscle cells, the nature and origin of which are not fully understood. In addition to Glut4 itself, these vesicles compartmentalize a number of proteins, at least one of which, insulin-responsive aminopeptidase, or IRAP, is completely colocalized with Glut4 in insulin-sensitive tissues. However, unlike Glut4, IRAP is expressed in a variety of other tissues and cell lines. Here, we explored the intracellular localization of IRAP in the rat pheochromocytoma cell line PC12. We found that this protein is present in a distinct population of slowly recycling light vesicles. By gradient centrifugations, immunoadsorption and double immunofluorescent staining, these vesicles are different from transferrin-containing endosomes, small synaptic vesicles and secretory granules and may thus represent a novel compartment in PC12 cells. Glut4-GFP chimera transiently expressed in PC12 cells is targeted to IRAP-containing vesicles indicating that cotargeting of Glut4 and IRAP is not specific for adipocytes and myocytes, but is faithful in a foreign cell type. We suggest that PC12 cells may possess a novel type of a vesicular carrier that may represent the homolog of Glut4-vesicles.
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PMID:A Glut4-vesicle marker protein, insulin-responsive aminopeptidase, is localized in a novel vesicular compartment in PC12 cells. 1148 15