GHRH Info – Biosynthetic Pathways are complex

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GHRH is a molecule that has been discovered in plants, mammals, bacteria, fungi and single cell organisms. Initially, it was discovered in molecular biology in 1958 in human genome studies. Because of the recent identification of this enzyme in other organism’s unrelated to human biology, it is now referred to only by the letters GHRH.
CJC 1295 is the synthetic version of GHRH. CJC 1295 just like GHRH allows certain albumins – a globular protein, which is stored in specific areas of the organisms body – to bind to cell receptors.

The Difference

GHRH and CJC 1295 is the duration length. GHRH is exuded in small spurts for short periods of time over a 24-hour period. CJC 1295 is also released in small bursts but has an extended half-life that continues the bursting action over a longer period during the same 24 hours. CJC 1295 was developed in order to have sufficient lengths of time to measure results, effects and responses that were impossible to do with GHRH.
Although it was first identified in mammalian cellular structure, it has since been detected in bacteria, macroalgae, and other invertabrates. In those few cases that are currently under study, it is becoming evident that CJC 125, aka GHRH, mimics the photoperiodic responses seen in other life forms.

GHRH Info

Expected Observations

One unexpected observation is that the biosynthetic pathways between simple cell and complex mammal use GHRH identically. Once scientists understand the manner in which GHRH works within bacteria, it is possible to modify the detrimental effects of strains dangerous to organisms. The other possibility is that certain diseases/disorders such as Alzheimer’s may be reversed in the future.
In studies on laboratory mice for the purpose of eliminating or including CJC 1295 as a possible corrective GHRH to treat dwarfism in offspring, initial findings report stated that normal growth was maintained in the mice treated with CJC 1295 treated once daily but that those mice treated more often than that failed to show similar results. In some instances, the mice treated more frequently and on different time scales actually deteriorated in growth.

Biosynthetic Pathways are complex

In an earlier study in Strasbourg, France done by molecular biologists, it was ascertained that the biosynthetic pathways that enables the pulsing release of GHRH is much more complicated than a simple ‘a to b to c’ routing mechanism. ICER – an inducible repressor – regulates an alternative binding protein and is tissue specific. This means that the amount and effects of CJC 1295 on any given organism, cell or molecular structure can be sidetracked by this repressor.

CJC 1295 with DAC is time released in a continuous stream instead of in short bursts as its counterpart, CJC 1295 NO DAC does. Thus far, CJC 1295 NO DAC is the only GHRH that has been tested in plants, microbes and organisms. Because there is insufficient evidence to know how it will modify the cell structure over extensive periods, there is no data determining that it is ready for commercial use.

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The protien Igf-1 Des1

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Igf-1 Des1 refers to insulin-like growth factor 1 or somattomedin C. This is a protein that has been encoded as the IGF1 gene when it appears in a natural setting. It is also often referred to as a sulfation factor which causes non-suppressible insulin-like activity when it is activated.

In a natural setting, this hormone mimics the structure of insulin. The synthetic version of this chemical is used as a mecasermin that may have factors that could be used to treat growth failure, though studies are still ongoing regarding the potential application of this synthetic chemical in a natural setting.

Mechanism of Action

The natural version of Igf-1 des-1 exists in a variety of types of tissues and cells.

  • When this chemical binds to IGF1R it creates a receptor tyrosine kinase which initiates intracellular signaling. The Igf-1 des1 chemical is one of the most potent activators within the AKT signaling pathway, stimulating proliferation and cell growth while inhibiting programmed cell death.
  • Once Igf-1 is produced in the body, it will affect every type of cell, particularly the nerve cells, while stimulating DNA synthesis.

The synthetic version of this chemical is largely designed to mimic these effects on tissues. Researchers hope that in time this synthetic chemical can be developed to a point where it could be used to treat deficiencies of GH in the animal body. Currently the synthetic version is applied to cattle to increase reproductive performance.

The protien Igf-1 Des1

Effects on Diet

Igf-1 des1 was studied to determine how it affects the quality and quantity of dietary proteins within plasma immunoreactive insulin in the livers of rats.

  • Plasma immunoreactive concentrations of Igf-1 were found to be higher in rats that followed a casein diet rather than those that followed a protein-free diet consisting of soya-bean proteins.
  • Throughout the study, four species of the Igf-1 hormone were found to have a different molecular weight when stored in the liver of the rat. Those on a gluten diet were found to have a decrease in the size of the chemicals in the liver compared to those on the casein diet.
  • The livers of the rats that were given the gluten, protein-free diet were around .4 compared to the rats that followed the casein diet.

It was found that applying a soya-bean protein diet to the rats did not have a marked effect on the mRNA version of Igf-1. This indicates that this version of the chemical and its sensitivity may be regulated by the nutritional quantity and quality of the dietary proteins in the system.

In more recent studies, a plant expression of Igf-1 des1 was developed in a transgenic rice grain that could produce the chemical in a recombinant natural setting, but additional study is needed to best determine the proper way to manufacture this version of the chemical.

Sources

http://journals.cambridge.org/action/displayAbstract?fromPage=online&aid=870596

 

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Insulin Growth Factors

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Insulin growth factors are the proteins that have sequence similarities to insulin. They are used to allow cells to communicate with the physiologic environment, a system commonly referred to as the IGF axis. In most animals, this hormone is secreted by the liver when it is stimulated.

If insulin growth factors are not secreted properly in animals, it can lead to a variety of diseases including cancers. When the hormone is functioning properly, it can stimulate proliferation of cells while inhibiting cell death.

The effects vary throughout the animal body because many different tissues will be affected by insulin growth factors. At high concentrations this chemical can activate insulin receptors to compliment the natural effects of insulin.

Insulin Growth Factors

Diseases that May affect Insulin Growth Factors in the Body

Recent studies imply that the healthy presence of insulin growth factors in the body of animals may have an important role in the aging process.

  • Studies using fruit flies and nematodes were used to determine how a life span could be increased when the gene that was the equivalent of what would produce insulin in mammals was knocked out.
  • These results were somewhat inconclusive as the studies focused on small organisms which had several genes that would mimic those of insulin growth factors in mammals.
  • These results were further complicated because mammals typically have a specific organ designated for the creation of insulin while other organisms did not.

While study results were inconclusive, these examinations determined that the absence of insulin growth factors could perturb aging. It is also shown that restricting the diet, which would impact insulin us,e would impact this status.

Effects on RNA Expression in Middle-Aged Rats

The activity of insulin-like receptors DAF-2 and reproductive growth was monitored during the adult life span of rats to better understand how insulin growth factors functioned in mammals.

  • Analysis revealed that 37 C. genes could be used to predict and incode insulin-like peptides. Many of these insulin genes are within the same superfamily and were clustered–which indicates that the diversification of this family is fairly recent.
  • These genes are largely expressed in neurons such as sensory neurons which are required for reproductive development. The predictions of these structures at cleavage sites indicate that the insulin receptors ins-1 are more closely related to insulin in mammals than they are in other animals.
  • In these types of animals, this implies that the penetrant arrest of these chemicals at the dauer state can enhance the weak daf-2 mutants, which implies that ins-s can be used to antagonize these receptors to signal inulin.

The coding regions for these genes implies that there is a redundancy as only one other ins gene can be used as a predicted C peptide for signaling das-2, but four of the genes do not. This indicated that there is still functional diversity within this gene family.

The specific effects of insulin growth factors in a variety of animals and how isolating or eliminating genes within these animals is expanding the understanding of how these chemicals function. However, additional study is necessary to determine how these methods could be applied to mammals.

Source:

http://www.ncbi.nlm.nih.gov/pubmed/9483550

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