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Human Growth Hormone, is a naturally occurring complex protein hormone, comprising of 191 amino acids with a molecular weight of 22,000 Daltons. This naturally occurring hormone is referred to as Somatotropin. On the other hand, Somatropin, is a biosynthetically prepared recombinant Human Growth Hormone (rHGH), which is identical to the natural hormone and performs similar functions.
Different techniques for HGH replacement used over time
Synthetic HGH or Somatropin, was first used in an attempt to treat Growth Hormone Deficiency way back in 1920s. At this time, Bovine Growth Hormone (rBGH), was purified and used for the treatment. However, as the molecular structure of bovine growth hormone is different compared to Human Growth hormone, this treatment was abandoned.
Subsequently, in the later part of 1950s, endocrinologists from the Tufts University, Boston, used Human Growth Hormone from cadavers to treat GH deficiency. After the first few successful attempts, this technique was used across the United States. However, over a period to time it was realized that the extracted HGH from cadavers could get contaminated and result in a disease called the ‘Creutzfeldt-Jakob disease’, which is a progressive degenerative disorder of the brain which ends in death. Subsequently this treatment was stopped too.
Finally towards the beginning of 1980s, an American Pharmaceutical company developed the first biosynthetic human growth hormone. This biosynthetic hormone, referred to as Somatropin, is now used across the world for treatment of Growth Hormone Deficiency.
How is Somatropin Manufactured?
In 1981, Genentech Pharmaceuticals developed the first biosynthetic form of Human Growth Hormone. This recombinant Growth Hormone (rHGH) was produced using a technique called as Inclusion Body Technique. This is a complex biosynthetic process that involves the artificial synthesis of the DNA fragment, by encoding the first 24 amino acids of the 191 amino acid chain. The remaining amino acids are obtained by complimentary DNA copies of the messenger RNAs.
Following this technology, various scientists synthesized Human Growth Hormone, from a genetically engineered and special strain of E. Coli (a bacterium normally found in the human intestine, which aids in the absorption of Vitamin K and B complex). This strain of bacterium helped in the production of synthetic recombinant Human Growth Hormone in a culture medium.
The most advanced technique used today, is referred to as the Protein Secretion Technology. This technology is a more improved version of the use of E coli for the synthesis of recombinant Human Growth Hormone, using a protein free media. The recombinant protein is secreted by adding the initial secretary sequence onto the nitrogenterminal of the GH amino acid chain, synthesized in the culture media. This process helps in simpler purification and avoids re-solubalization of the protein and inclusion bodies.