| pubmed-article:1482691 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1482691 | lifeskim:mentions | umls-concept:C0030281 | lld:lifeskim |
| pubmed-article:1482691 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:1482691 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:1482691 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:1482691 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1482691 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1482691 | pubmed:dateCreated | 1993-2-18 | lld:pubmed |
| pubmed-article:1482691 | pubmed:abstractText | (1) A new insulin-secreting cell line (INS-1; Asfari et al. (1992) Endocrinology 130, 167-178) has been used to study the regulation by Ca2+ of mitochondrial FAD-linked glycerol-phosphate dehydrogenase (FAD-GPDH) in situ. (2) Enzyme activity was examined on-line in electropermeabilized cells by a new, sensitive, assay. This involved the reduction of the artificial electron acceptor, 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide (MTT), monitored by the quenching of the fluorescence of rhodamine-18. Using this approach, similar total levels of FAD-GPDH activity (nmol/min per 10(6) cells) were measured in INS-1 cells (1.35 +/- 0.22) and isolated rat islet cells (1.63 +/- 0.02) (3) Ca2+ ions markedly activated the enzyme, lowering the apparent Km-value for added DL-glycerophosphate from 8.8 +/- 1.4 mM to 1.0 +/- 0.1 mM. Ca2+ had no effect on the apparent Vmax. The enzyme displayed cooperative kinetics with respect to DL-glycerophosphate (Hill coefficient of 2.0 +/- 0.2 and 1.6 +/- 0.2 in the absence and presence respectively of Ca2+). Half-maximal effects of Ca2+ were observed in the range 30-130 nM, depending on the concentration of glycerol phosphate. (4) Enzyme activity was weakly (30%) inhibited by diazoxide, but not by the diabetogenic drug, streptozotocin. (5) The data indicate that INS-1 cells represent an excellent model for studying the rôle of FAD-GPDH in the control of insulin secretion. | lld:pubmed |
| pubmed-article:1482691 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1482691 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1482691 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1482691 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1482691 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1482691 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1482691 | pubmed:author | pubmed-author:WollheimC BCB | lld:pubmed |
| pubmed-article:1482691 | pubmed:author | pubmed-author:RutterG AGA | lld:pubmed |
| pubmed-article:1482691 | pubmed:author | pubmed-author:PralongW FWF | lld:pubmed |
| pubmed-article:1482691 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1482691 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1482691 | pubmed:volume | 1175 | lld:pubmed |
| pubmed-article:1482691 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1482691 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1482691 | pubmed:pagination | 107-13 | lld:pubmed |
| pubmed-article:1482691 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:1482691 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1482691 | pubmed:articleTitle | Regulation of mitochondrial glycerol-phosphate dehydrogenase by Ca2+ within electropermeabilized insulin-secreting cells (INS-1). | lld:pubmed |
| pubmed-article:1482691 | pubmed:affiliation | Division de Biochemie Clinique, Centre Médical Universitaire, Geneva, Switzerland. | lld:pubmed |
| pubmed-article:1482691 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1482691 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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