| pubmed-article:2165097 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2165097 | lifeskim:mentions | umls-concept:C0003323 | lld:lifeskim |
| pubmed-article:2165097 | lifeskim:mentions | umls-concept:C0023690 | lld:lifeskim |
| pubmed-article:2165097 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:2165097 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:2165097 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:2165097 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:2165097 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:2165097 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2165097 | pubmed:dateCreated | 1990-8-28 | lld:pubmed |
| pubmed-article:2165097 | pubmed:abstractText | The CD4R has been shown to exert variable effects on T cell activation responses. Depending on the manner of ligation, the CD4R has been demonstrated to have positive as well as negative effects on the generation of [Ca2+]i flux by the CD3R. Coaggregation of CD3 with CD4 enhanced Ca2+ flux while their independent ligation and aggregation diminished this response. To further elucidate these paradoxical CD4 effects, we studied induction of a microtubule-associated protein 2 kinase (MAP-2K) activity during ligation of the CD3R. Lymphoid MAP-2K activation by CD3 is an evanescent event that is dependent on phosphorylation of 43-kDa MAP-2K via a pathway that involves protein kinase C. Coaggregation of CD4 and CD3 with cross-linking antibodies and avidin enhanced the CD3-mediated MAP-2K response almost twofold. In contrast, independent ligation and cross-linking of CD4 reduced the CD3-induced MAP-2K response by approximately 50%. An important requirement for this inhibitory effect was that CD4 be ligated before stimulation with anti-CD3. The negative effect of anti-CD4 mAb was specific as other mAb failed to simulate this event. The PMA-induced MAP-2K response was not inhibited by anti-CD4. Intact 32P-labeled Jurkat and normal human T cells demonstrated the appearance of a single 43-kDa tyrosine phosphoprotein during stimulation with PMA and anti-CD3. When these crude cellular extracts were extensively fractionated across DEAE- and hydrophobic columns, MAP-2K was resolved into two peaks of activity, each containing a single tyrosine phosphoprotein around 43 kDa. In addition to tyrosine-specific labeling, mitogenic stimulation of normal human T cells also induced threonine-specific labeling of MAP-2K. These results imply that activation of lymphoid MAP-2K is a dual process requiring at least two independent kinases for optimal activity. Inasmuch as CD3 activates protein kinase C and CD4 is associated with a tyrosine kinase, pp56lck, we suggest that their coaggregation may create the conditions whereby MAP-2K may be activated by dual phosphorylation. Independent aggregation of these receptors may lead to physical separation and breakdown of this interactive mechanism. | lld:pubmed |
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| pubmed-article:2165097 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2165097 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:2165097 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2165097 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2165097 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:WilliamsKK | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:KatzRR | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:PollackSS | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:LedbetterJ... | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:NelA EAE | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:LandrethGG | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:AkerleyBB | lld:pubmed |
| pubmed-article:2165097 | pubmed:author | pubmed-author:HultinLL | lld:pubmed |
| pubmed-article:2165097 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2165097 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2165097 | pubmed:volume | 145 | lld:pubmed |
| pubmed-article:2165097 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2165097 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2165097 | pubmed:pagination | 971-9 | lld:pubmed |
| pubmed-article:2165097 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2165097 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2165097 | pubmed:articleTitle | CD-3-mediated activation of MAP-2 kinase can be modified by ligation of the CD4 receptor. Evidence for tyrosine phosphorylation during activation of this kinase. | lld:pubmed |
| pubmed-article:2165097 | pubmed:affiliation | Department of Medicine, UCLA School of Medicine 90024-1680. | lld:pubmed |
| pubmed-article:2165097 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2165097 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2165097 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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