| pubmed-article:1500712 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C1518997 | lld:lifeskim |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C0035253 | lld:lifeskim |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C1416797 | lld:lifeskim |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1500712 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:1500712 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1500712 | pubmed:dateCreated | 1992-9-14 | lld:pubmed |
| pubmed-article:1500712 | pubmed:abstractText | Op18 is a highly conserved major cytosolic phosphoprotein that has been implicated in signal transduction in a wide variety of cell types. Freshly isolated peripheral blood lymphocytes (PBL) constitutively express low levels of mostly unphosphorylated Op18. After mitogenic stimulation of PBL, Op18 synthesis is induced at a time when cells are entering S-phase. In this study, we have examined the phosphorylation of Op18 in freshly isolated PBL after activation of the T cell receptor by OKT3. Quantitative analysis of Op18 phosphorylation was undertaken by metabolic labeling with 32Pi and PhosphorImager analysis of two-dimensional gels. After 10 or 15 min of activation by OKT3, one of the three major phosphorylated forms of Op18, designated Op18c, increased approximately 10-fold, which represented a most pronounced change among a large number of phosphoproteins analyzed. In time course experiments, increased Op18 phosphorylation to yield Op18c was observed as early as 2 min. Continued OKT3-induced activation for 20 to 72 h resulted in a further increase in phosphorylated Op18 forms, which paralleled new Op18 synthesis and occurred at a time when cells were entering S-phase, as determined by [3H]-thymidine incorporation. Inhibitors of lymphoid proliferation, cyclosporin A and RPM, had no effect on early (less than 15 min) phosphorylation. Addition of calphostin C, a specific inhibitor of protein kinase C, 1 min prior to stimulation of resting T cells with OKT3 completely inhibited further phosphorylation of Op18. Incubation of PBL with calphostin C for 75 min decreased constitutive levels of phosphorylated Op18. In contrast, inhibition of cyclic nucleotide-dependent protein kinases with HA1004 had no effect on Op18 phosphorylation. Activation of cAMP-dependent protein kinase with Forskolin or 8Br-cAMP did not increase Op18 phosphorylation. Our results suggest that Op18 phosphorylation is mediated by protein kinase C activation as an early event in T cell activation through the T cell receptor. | lld:pubmed |
| pubmed-article:1500712 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1500712 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1500712 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1500712 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1500712 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:ZiaMM | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:OTAM IMI | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:HailatNN | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:LambB JBJ | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:StrahlerJ RJR | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:KuickR DRD | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:MelhemR FRF | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:KeimD RDR | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:RogersK PKP | lld:pubmed |
| pubmed-article:1500712 | pubmed:author | pubmed-author:UnderhillJ... | lld:pubmed |
| pubmed-article:1500712 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1500712 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1500712 | pubmed:volume | 149 | lld:pubmed |
| pubmed-article:1500712 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1500712 | pubmed:authorsComplete | N | lld:pubmed |
| pubmed-article:1500712 | pubmed:pagination | 1191-8 | lld:pubmed |
| pubmed-article:1500712 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
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| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:meshHeading | pubmed-meshheading:1500712-... | lld:pubmed |
| pubmed-article:1500712 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1500712 | pubmed:articleTitle | Activation of resting peripheral blood lymphocytes through the T cell receptor induces rapid phosphorylation of Op18. | lld:pubmed |
| pubmed-article:1500712 | pubmed:affiliation | University of Michigan Medical School, Department of Pediatrics, Ann Arbor 48109. | lld:pubmed |
| pubmed-article:1500712 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1500712 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1500712 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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