Month: June 2013

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HGH fragments refer to modified forms of amino acids, in this case amino acid 176-191. Studies indicate that this chemical has potential use in improving the lipid profile while increasing muscle mass.

Research studies are focusing on the effects of administering HGH fragment 176-191 to subjects that have HIV-associated lipodystrophy as a means of controlling excess abdominal fat which stems from such conditions. This chemical appears to have potential for such a purpose because it does not have an impact on glycemic control.

Effects of Amino Acid Sequence with Insulin

• Three systems have been studied to better understand these effects. These include how insulin binds to certain hepatic plasma membrane receptors or isolated hepatocytes, insulin intolerance tests at the intravenous level and the modulation of insulin-dependent glycogen phosphorylase or glycogen synthase in adipose or muscle tissue.

• Results of this monitoring establish that hexapeptide allows for the minimum active sequence. This strongly indicates that insulin potentiating actions in active peptides is designed to bind insulin to specific receptors.

• This system allows the body of the subject to modulate the actions of the phosphorylase and glycogen synthase to produce hypoglycemia. This increases the storage of glycogen within the adipose tissue, liver and muscles for further use as an animal’s body requires.

Hyperglycemic Action in Synthetic C-Terminal Fragments

• Various synthetic peptides are designed to correspond with amino acids, including 176-191 within the body to create necessary reactions.

• Studies have noted the reactions of these peptides and the in vivo effects they had on rats with normal health and size.

• Four such peptides including hgh fragment 176-191 were able to increase blood glucose levels for a short period of time. They were also able to achieve a longer lasting raise in the insulin levels in the plasma.

• The remaining peptides, hgh 180-191 and 179-191 were found to be inert in the systems that were tested. Single injections of peptides which contained 178-191 and the hgh molecule would reduce the animal’s sensitivity to insulin in the intravenous insulin tolerance tests by a significant level.

• These findings help to show how various amino acids work together to better manage insulin travel and use throughout the body of the subject, helping to achieve a balance. The findings also indicate that peptides which are biologically active, require a minimum of the appropriate informational sequence to be present in order to remain functional.

• This sequence must also have the proper physical configuration in order to elicit the desired response from the organism. These findings help researchers better understand how to administer synthetic 176-191 in an organic setting.

• Ongoing research into the appropriate solution of hgh fragment 176-191 solutions is ongoing. This will assist in determining the appropriate chemical solution to better match the natural form of this amino acid which would be present in an organic setting, allowing synthetic versions to behave much like these natural chemicals when introduced into an organic environment.

Sources

http://ajpgi.physiology.org/content/234/5/G521.short

http://diabetes.diabetesjournals.org/content/29/10/782.short

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Fragment 176-191 refers to the PGP9.5 synthetic peptide which corresponds to the amino acids of peptide 175-191 PGP9.5. It may also be known under the names neuron cytoplasmic protein 9.5 or gracile axonal dystrophy.

This particular concentration is suggested to be used as an antibody or antigen binder in animals. When used with antibodies, fragment 176-191 should be pre-incubated with a peptide before it is introduced to a given tissue. The chemical has not been tested outside of this application so further dilutions or concentrations of this chemical are determined within the confines of a given study.

Functionality

The use of fragment 176-191 is largely focused on the cytoplasm and endoplasmic reticulum membrane, a majority of which associated with membranes of the brain.

In a natural setting, the chemical stimulates the ubiquitin-protein hydrolase that is involved in processing ubiquitinated proteins and ubiquitin precursors.

This enzyme will recognize the peptide bond at the glycine C-terminal of ubiquitin.

The chemical may also bind to a free monobiquitin in order to prevent degradation of lysosomes. The chemical might have ATP-independent ubiquitin ligase activity.

In a natural setting fragment 176-191 is found in the neocortex within the neuronal cell bodies of animals. It is expressed through the cells and neurons as a means of diffusing the neuroendocrine system and tumors created therein. Fragment 176-191 may weakly appear in the ovaries of such subjects.

 

Sources

http://www.abcam.com/PGP9-5-peptide-175-191-ab38203.html?productWallTab=Questions

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Hexarelin refers to the peptide GH secretagogue which is quite similar in structure to GHRP-6. Because hexarelin is synthetic, its effects are not as potent as the naturalized chemicals.

Using hexarelin to stimulate some hormones will cause an insulin-like growth factor or IGF-1 which is the natural substance used to encourage muscle growth in animals. Unlike similar chemicals, hexarelin does not have any impact on appetite or increase of ghrelin levels.

Effects on Subjects of Varying Ages

Hexarelin has been established as an effective chemical in inducing hormone secretions in small mammals, but the effects and stability of this chemical compared to other common options are largely unknown.

• To better understand the effects of hexarelin and how they compared to those of common GH stimulators such as GHRP6, GHRP1 or GHRP2, secretions were studied in rats of varying ages and results were compared to the known stable chemical 2-methyl-trp.

• In 10 day old rats Trp was substituted with 2-methyl-trp and a hexapeptide hexarelin to achieve GH secretion. The chemicals were successful in achieving this stimulation.

In trials, hexarelin appeared to be more effective than GHRP6 in eliciting the desired response. This indicates that hexarelin could be used as an effective releasing agent that could act as a tool for both diagnostic and therapeutic work in clinical practice in the future.

Cardio-protective Effects of Hexarelin

As selected GH deficiency has been established as a risk for cardiac dysfuntion, hexarelin was administered to determine its potential use in addressing this risk.

• Non-GH mediated effects of the heart were examined in hypo-physectomized rats. Throughout the study, rats were administered hexarelin for a week.

• Throughout the study, the hexarelin injections prevented the increases of diastolic or left ventricular pressure and also helped to reduce reactivity of the coronary vasculature to angiotensin II and coronary perfusion pressure.

• In addition to these findings, hexaralin was determined to prevent prostacyclin release levels falling while recovering contractility. Administering natural GH allowed for similar results. However, the administration of EP 51389, was not effective in relieving symptoms.

These conclusions indicate that hexarelin can help to reduce the damage to the cardiovascular system that occurs following ischemia-reperfusion which is not mediated by GH but the activating of certain cardiac receptors. Additional study may reveal a solution of hexarelin that may be administered as a form of preventative care for these circumstances.

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Ongoing study continues to reveal potential uses of hexarelin in mammalian test subjects. This research hopes to address safety issues including proper levels of administration and likely side effects of interaction with this chemical.

Sources:

http://www.sciencedirect.com/science/article/pii/0024320594005109

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