Growth hormone expression

USA somatropin peptide Humatrope Crescormon, Genotropin, Genotropin Miniquick, Umatrope, Genetonorm Recombinant human growth hormone expressed in E. coli Hormone... 

Goeddel D.V., Heyneker H.L., Hoxumi T., Arentzen R, Itakura K., Yansura D.G, Ross M.J., Miozzari G, Crea R Seeburg P.H. (1979) Expression in Escherichia coli of a DNA sequence coding from human growth hormone. Nature, 281, 544-548. 

Slater MD, Murphy CR. Co-expression of interleukin-6 and human growth hormone in apparently normal prostate biopsies that ultimately progress to prostate cancer using low pH, high temperature antigen retrieval. /. Mol. Histol. 2006 37 37-41. 

Add an aliquot of the DSS or BS3 solution to the reaction medium to obtain a final concentration of 0.5-5mM. Note Simons et al. (1999) successfully used a concentration of 0.5 mM BS3 with Madin-Darby canine kidney (MDCK) cells permanently expressing a GPI-anchored form of growth hormone decay accelerating factor (GH-DAF) to crosslink the protein interaction complexes on the cell surfaces. 

Human serum albumin was the first full-length human protein to be expressed in the leaves of a transgenic plant (both tobacco and potato leaves were shown to express the protein). This report was published in 1990 [18]. Four years earlier, Barta and colleagues had demonstrated the expression of human growth hormone in tobacco and sunflower callus, and the protein was expressed as a fusion with the Agrohacterium tumefaciens nopaline synthase enzyme [17]. 

Human growth hormone was expressed as fusion with the Agrobacterium tumefaciens nopaline synthase enzyme but only transcript was detectable... 

Several cell types, including keratinocytes, myoblasts and fibroblasts, have been studied in this regard. It has been shown, for example, that myoblasts, into which the factor IX gene and the growth hormone gene have been introduced, could express their protein products and secrete them into the circulation. 

Pannell, C., Simonian, S. X., Gillies, G. E., Luscher, B., and Herbison, A. E. (2002) Hypothalamic somatostatin and growth hormone-releasing hormone mRNA expression depend... 

Lastly, it has been shown that in rare cases trisulfide bridges (Cys-SSS-Cys) can be found as hydrophobic variants of recombinant proteins. The experimental mass of such a trisulfide-bridged peptide would be increased by 32 amu. Andersson et al.125 have described this phenomenon for recombinant human growth hormone during expression in E. coli. However, the receptor binding properties were not affected by this trisulfide modification. 

Andersson C., Edlund P.O., Gellerfors P, Hansson Y., Holmberg E., Hult C., Johansson S., Kordel J., Lundin R., Mendel-Hartvig I., Noren B., Wehler T., Wid-malm G., and Ohman J. (1996), Isolation and characterization of a trisulfide variant of recombinant human growth hormone formed during expression in Escherichia coli, Int. J. Peptide Protein Res. 47(4), 311-321. 

Finally, continuous exposure of certain receptors to their macromolecular ligands can lead to rapid downregulation of cell surface receptors, especially if receptor recycling within the cells is incomplete. Fortunately, expression of many receptors, for example for certain cytokines, growth hormones and adhesion factors, can be extensively upregulated in the disease process and this can result in disease-induced drug-targeting. 

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