| pubmed-article:10990531 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C0006685 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:10990531 | lifeskim:mentions | umls-concept:C0445254 | lld:lifeskim |
| pubmed-article:10990531 | pubmed:dateCreated | 2000-11-14 | lld:pubmed |
| pubmed-article:10990531 | pubmed:abstractText | The small G-protein Ras, a critical component in the signalling pathways regulating cell growth, is involved in the tonic upregulation of voltage-dependent calcium channels (VDCCs) in rat sensory neurones. To investigate which downstream effector(s) of Ras is involved in this process, a series of Ras mutant cDNAs were co-expressed with green fluorescent protein (GFP) in primary cultured rat dorsal root ganglion neurones (DRGs). Constitutively active V12Ras (glycine 12 to valine) markedly increased basal calcium current density by 41 % compared with control cells (GFP alone). In contrast, a farnesylation-defective mutant, V12S186Ras (cysteine 186 to serine; activates no downstream effectors), significantly reduced calcium current density by 47 %. Ras effector region mutants V12C40 (tyrosine 40 to cysteine; activates the p110 alpha-subunit of phosphatidylinositol 3-kinase) and V12G37 (glutamic acid 37 to glycine; activates Ral guanine nucleotide dissociation stimulator) had no significant effect on VDCC current. However, V12S35Ras (threonine 35 to serine; activates Raf-1 and the mitogen-activated protein kinase (MAPK) pathway) markedly increased basal calcium current density by 67 %, suggesting that Raf-1 activation is sufficient for Ras enhancement of calcium current in these cells. Raf-1 activates MEK (MAPK kinase) in the MAPK pathway, and the MEK inhibitor U0126 reduced calcium current by 45 % after 10-15 min, whereas the inactive analogue U0124 had no effect. This rapid time course for MEK inhibition suggests direct modulation of VDCCs via the Ras-MAPK pathway rather than gene expression-mediated effects. The relative proportions of omega-conotoxin GVIA- and nicardipine-sensitive N- ( approximately 40 %) and L- ( approximately 40 %) type currents were unaffected by either V12S35Ras expression or U0126 pre-treatment, suggesting that all components of calcium current in DRGs, are enhanced via this pathway. | lld:pubmed |
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| pubmed-article:10990531 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10990531 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10990531 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10990531 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10990531 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10990531 | pubmed:issn | 0022-3751 | lld:pubmed |
| pubmed-article:10990531 | pubmed:author | pubmed-author:FitzgeraldE... | lld:pubmed |
| pubmed-article:10990531 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10990531 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10990531 | pubmed:volume | 527 Pt 3 | lld:pubmed |
| pubmed-article:10990531 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10990531 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10990531 | pubmed:pagination | 433-44 | lld:pubmed |
| pubmed-article:10990531 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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