期刊
MOLECULAR IMMUNOLOGY
卷 38, 期 16-18, 页码 1283-1288出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0161-5890(02)00076-7
关键词
mast cell; Ras guanine nucleotide releasing protein; guanine exchange factor; calcium; phorbol ester; diacylglycerol; signal transduction
资金
- NHLBI NIH HHS [HL-63284, HL-36110] Funding Source: Medline
- NIAID NIH HHS [AI-23483] Funding Source: Medline
We recently cloned a new mast cell (MC) restricted, Ras guanine nucleotide releasing protein (designated mRasGRP4) from IL-3-developed, mouse bone marrow-derived MCs that can activate varied members of the Ras superfamily of small GTP-binding proteins. We now describe the rat ortholog of this MC-specific guanine exchange factor. Using the mRasGRP4 gene and transcript in a homology-based cloning approach, the relevant transcript was isolated and sequenced from the spleen and lungs of Sprague-Dawley rats. Evidence for differential splicing of the rRasGRP4 transcript was obtained in the spleen. The rat basophilic leukemia 1 MC line was found to express rRasGRP4, as well as the MC-committed progenitors residing in the bone marrow and the mature MCs residing in varied tissues of Sprague-Dawley rats. Based on its deduced amino acid sequence, rRasGRP4 is 93% identical to mRasGRP4. rRasGRP4 contains all of the functional domains present in the RasGRP family of guanine nucleotide exchange factors. Like its mouse ortholog, rRasGRP4 is a MC-restricted guanine exchange factor that contains Ca2+ and phorbol ester/diacylglycerol-binding domains C-terminal of its CDC25-like catalytic domain. (C) 2002 Elsevier Science Ltd. All rights reserved.
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