Membrane reinsertion of a myristoyl-peptidyl anchored extracellular domain growth hormone receptor
Endocrinology, ISSN: 0013-7227, Vol: 148, Issue: 2, Page: 824-830
2007
- 6Citations
- 8Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations6
- Citation Indexes6
- CrossRef6
- Captures8
- Readers8
Article Description
The actions of GH are mediated through a cell surface cytokine receptor. We previously demonstrated that naturally occurring truncated membrane bound GH receptors (GHRs) can block GH receptor signaling. We have now investigated whether recombinant extracellular GHR can be conjugated to a myristoylated-peptide (mp) tail and inserted into cell membranes to modulate GHR signaling. Recombinant human extracellular domain (1-241) GHR was expressed in Escherichia coli, purified, and refolded from cell lysate. The free C-terminal cysteine was then reduced and conjugated to an activated preformed mp tail. The properties of the purified tailed GHR (GHR-mp) were then compared with those of the untailed purified GHR 1-241. Fluorescence-activated cell sorter analysis and cell surface binding assays demonstrated that GHR-mp inserted into the cell surface membranes of CHO cells, whereas untailed GHR 1-241 showed no insertion. In a cell-based bioassay GHR-mp partially inhibited wild-type GHR signaling, whereas GHR 1-241 had no effect. Truncated extracellular domain GHR can, when specifically modified with a membrane-localizing mp unit, insert into cell surface membranes and modulate GHR signaling. Copyright © 2007 by The Endocrine Society.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33846461386&origin=inward; http://dx.doi.org/10.1210/en.2006-1002; http://www.ncbi.nlm.nih.gov/pubmed/17095595; https://academic.oup.com/endo/article/148/2/824/2501814; https://dx.doi.org/10.1210/en.2006-1002; https://academic.oup.com/endo/article-abstract/148/2/824/2501814?redirectedFrom=fulltext
The Endocrine Society
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