Membrane Reinsertion of a Myristoyl-Peptidyl Anchored Extracellular Domain Growth Hormone Receptor

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 myristoylat...

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Veröffentlicht in:	Endocrinology (Philadelphia) 2007-02, Vol.148 (2), p.824-830
Hauptverfasser:	Bowles, C. E, Wilkinson, I, Smith, R. A. G, Moir, A. J. G, Montgomery, H, Ross, R. J. M
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Bioassays Biological and medical sciences Cell Line Cell Membrane - metabolism Cell membranes Cell surface Cell surface receptors CHO Cells Cricetinae Cricetulus Cysteine DNA Transposable Elements E coli Escherichia coli Extracellular Space - metabolism Fundamental and applied biological sciences. Psychology Growth Hormone - genetics Growth hormones Humans Membranes Peptide Fragments - chemistry Peptide Fragments - drug effects Peptide Fragments - genetics Peptide Fragments - metabolism Phosphines - pharmacology Protein Engineering - methods Protein Structure, Tertiary Receptors Receptors, Somatotropin - chemistry Receptors, Somatotropin - drug effects Receptors, Somatotropin - genetics Receptors, Somatotropin - metabolism Recombinant Proteins - metabolism Transcription, Genetic Transfection Vertebrates: endocrinology
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