Human growth hormone and

Figure 13.20 Ribbon diagram of the structure of a 1 2 complex between the human growth hormone and the extracellular domains of two receptor molecules. The two receptor molecules (blue) bind the hormone (red) with essentially the same loop regions (yellow).

De Vos, A.M., Ultsch, M., Kossiakoff, A.A. Human growth hormone and extracellular domain of its receptor crystal structure of the complex. Science 255 306-312,... 

M. Mumenthaler, C. C. Hsu, and R. Pearlman, Feasibility study on spray-drying protein pharmaceuticals recombinant human growth hormone and tissue-type plasminogen activator, Pharm. Res, 11(1), 12 (1994). 

J. L. Cleland and A. J. Jones, Stable formulations of recombinant human growth hormone and interferon-y for microencapsulation in biodegradable microspheres, Phar. Res, 13(10), 1464 (1996). 

Dupin, P., Galinou, R, and Bayol, A. (1995). Analysis of recombinant human growth-hormone and its related impurities by capillary electrophoresis. /. Chromatogr. A 707, 396-400. 

In some ways, the use of animals (almost always mammals) as substitutes for bacteria in the recombinant DNA production of drugs is a natural and obvious extension of the techniques originally developed for the manufacture of insulin, human growth hormone, and other pharmaceuticals. Live animals have a built-in production... 

Human prolactin is similar in structure to human growth hormone, and both are good lactogens. In women, prolactin acts with other hormones on the mammary gland during pregnancy to develop lactation and after birth to maintain it. Hyperprolactinemia causes impotence in men and amenorrhea and infertility in women. Chronically elevated levels of circulating prolactin are associated with suppression of 17-p-estradiol and testosterone production in the ovaries and testes. 

Type IV poly(ortho esters) are very similar in structure to type II poly(ortho esters), but they do not need to have excipients in the formulation due to the incorporation of no acidic moieties in the polymer backbone (Ng et al. 1997). Rods of poly(ortho ester) loaded with recombinant human-growth hormone and bovine serum albumin have been created. The rods are the products of polymer-protein mixture extrusion at a temperature between 50° and 70°C. Particles have also been produced from these rods (Heller et al. 2000). The size of these particles, >106 pm, was much larger than would be expected to be absorbed by the gastrointestinal lining (Florence 1997). If the particle size can be reduced, this type of polymer system may be made to be acceptable for oral administration. 

Demling RH. Comparison of the anabolic effects and complications of human growth hormone and the testosterone analogue, oxandrolone, after severe burn injury. Burns 1999 25(3) 215-21. 

Jostel A, Mukherjee A, Alenfall J, Smethurst L, Shalet S. A new sustained-release preparation of human growth hormone and its pharmacokinetic, pharmacodynamic and safety profile. Clin Endocrinol 2005 62 623-7. 

P. Oroszlan, S. Wicar, G. Teshima, S.-L. Wu, W. S. Hancock, and B. L. Karger, Conformational effects in the reversed-phase chromatographic behavior of recombinant human growth hormone and N-methionyl recombinant growth hormone, Anal. Chem., 64 1623 (1992). 

The authors wish to thank W. S. Hancock and J. Varga for the gift of human growth hormone and the allergen sample, respectively. Thanks are also due to D. Corradini and T. Ogawa for help in some of the experiments. This work was supported by the National Foundation for Cancer Research and by Grant GM 20993 from the National Institute of Health, US Department of Health and Human Services. 

Examples of the products that can be obtained through the processes include DNA vectors, such as plasmids, viruses, bacteriophages and cosmids synthetic genes transformed human viruses (e.g. the Epstein-Barr virus) transformed bacterial cells containing specific properties animal and plant cells and bacteria mAbs, tissue cells regulatory proteins such as human insulin, interferons and human growth hormones and transgenic plants and animals. 

Figure 12.5 Amino-terminal signal sequence of (A) human growth hormone and (B) bovine proalbumin. Hydrophobic core is within the box.

Tl. Teh, L. C., Murphy, L. J., Huq, N. L., Surus, A. S., Friesen, H. G., etal., Methionine oxidation in human growth hormone and human chorionic somatomammotropin. Effects on receptor binding and biological activities. J. Biol. Chem. 262, 6472-6477 (1987). 

Kossiakoff, A. A., Somers, W., Ultsch, M., Andow, K., Muller, Y, and De Vos, A. M. (1994). Comparison of the intermediate complexes of human growth hormone bound to the human growth hormone and prolacdn receptors. Protein Science 3, 1697-1705. 

As has been the case with conventional drugs, therapeutic proteins produced by biotechnology are also open to misuse as in the cases of the use of human growth hormone and erythropoietin by athletes to enhance their athletic performance. Their being identical to their counterparts produced in the body makes their detection in routine tests nearly impossible (Spalding, 1991). These concerns are also being addressed by the manufacturers of such drugs. 

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