Tesamorelin, also known as TH9507, is  a synthetic growth hormone-releasing factor agonist that may stimulate the production and release of endogenous growth hormone. It is comprised of all 44 amino acids of GHRH with a trans3-hexenoic acid group. Additionally, it is speculated to be more robust and stable than GHRH and may be resistant to cleavage by the dipeptidyl aminopeptidase enzyme. Tesamorelin is believed to activate the GHRH receptor in the pituitary gland, causing the synthesis and release of growth hormone-releasing hormone. This hormone, in turn, is speculated to act on several cells, including hepatocytes, to stimulate the production of insulin-like growth factor 1 (IGF-1). IGF-1 is considered to mediate many of the effects of growth hormones, including liver growth, suppression of programmed cell death, impaired glucose tolerance, and lipolysis.

Ipamorelin is a synthetic pentapeptide with distinct and specific growth hormone (GH) release properties, potentially as impactful as researchers suggest GHRP-6 is. It is believed to stimulate GH release via GHRP-like receptors, and surprisingly, it may not release ACTH or cortisol at levels significantly different from those observed after GHRH stimulation. This action is speculated to make ipamorelin potentially the first GHRH agonist specific for GH release, similar to GHRH. Ipamorelin appears to work in a completely different way to stimulate the release of growth hormones. It is suggested to bind to ghrelin receptors in the pituitary gland without affecting other hormones in the body. Ghrelin, which it interacts with, is believed to have profound metabolic regulatory effects, including increased or decreased hunger, suppression of the breakdown of accumulated fat, and most importantly, the release of growth hormone from the pituitary gland.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

What is FOXO4-DRI?

FOXO4-DRI, also known as Proxofim is a synthetic peptide developed by Dutch research teams. It contains a specific peptide antagonist named FOXO4-DRI. It is a modified protein type designed to trigger the selective death of aged cells. The discovery of this peptide analog has accentuated the attempts for cell aging reversal. Data suggests promising results during its initial testing in mice. FOXO4-DRI peptide bears the potential to promote cell longevity, possibly reduce physiological impacts linked to the onset of dementia, and suppress tumor development.

How does it work?

Cellular biologists have suggested that cells exhaust after 70 divisions and can no longer produce new cells. There does not appear to be any way to induce the continual division of cells without decay. Eliminating aged cells may make space for younger cell development, in a process called autophagy. Damaged cells tend to spread the decay process as well. Aged, decayed cells are considered to be suitable for nothing as they produce no energy. In addition, they keep occupying space within and between cells, hindering the growth of surrounding cells.

FOXO4-DRI peptide appears to work by removing these senescent cells that have outlived their efficacy. Considered to be the most effective senolytic agent to date; the peptide may potentially cease the communication of cells with p53 genes and convey signals that the cell is damaged and needs to be cleared by autophagy. Stem cells are considered to produce new cells after the death and clearance of aged cells. An increase in new cells to replace the aged ones may culminate in better overall physiological functioning.

Research Implications from FOXO4-DRI

Anti-Aging Impacts on Cells

Mitochondria is known as the ‘powerhouse of the cell’ as it is considered to primarily produce energy. The energy currency of an organism is called Adenosine Triphosphate (ATP). The organisms produce it inside the mitochondria due to several complex reactions. Lysosomes are responsible for removing cellular debris, and work as a dustbin of cells to remove aged and dead cells. If any of these structures becomes compromised, physiological functions are considered to decline. Studies found that test mice became healthier as compared to the control group. Mice in the test group achieved better energy levels, biomarkers for physiological function such as replenishment of follicle development, improved kidney function, and cell cycling with this protein.

Diabetes Research

FOXO proteins are considered to regulate insulin signaling and insulin-like growth factors (IGF). FOXO proteins may control cell growth, metabolism, and differentiation by acting on IGF. Future research may explore the effects of FOXO proteins in insulin signaling. This action may have correlative impacts on diabetes and its related complications.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

Research and isolation of Follistatin, a protein that is naturally produced, has led researchers to develop a synthetic version called Follistatin-344. The primary speculation is that Follistatin-344 peptide antagonizes the function of TGF-β. The TGF-β family comprises Follicle Stimulating Hormone (FSH), Myostatin, and Activin. In addition to potentially inhibiting TGF-β, Follistatin-344 might act on the IGF-1/Insulin pathway.

Follistatin-344 Peptide Research

Follistatin-344 peptide has been employed in research studies with a variety of focuses, though it is primarily examined within the context of muscle cells.

1. Muscle Cell Growth: As mentioned, myostatin functions to reduce muscle mass, and is a member of the TGF-1 family that inhibits the growth and differentiation of muscle fibers. There are suggestions that Follistatin-344 peptide may exert potent anti-myostatin action. Speculative research on mice lacking myostatin indicates that the peptide may induce greater muscle mass development. Additionally, speculative studies on Follistatin-344 peptide have suggested a remarkable increase in muscle mass without the involvement of other muscle-building factors. Follistatin-344 has been suggested to increase muscle bulk through two main mechanisms: hypertrophy and hyperplasia. Hypertrophy leads to an increase in the size of individual muscle cells, while hyperplasia increases the number of muscle fibers.

2. Speculative Effects on Diabetes Mellitus Type 1 diabetes, considered to result from a reduced expression of insulin-secreting beta-pancreatic cells, leads to reduced insulin secretion and poor glucose metabolism. Follistatin-344 peptide, following studies in animal research models, appears to lead to an increase in beta-pancreatic cells. The exposure of Follistatin-344 peptide in animal models resulted in a remarkable rise in the life expectancy of mice and a reduction in diabetes-related micro- or macro-vascular complications.

3. Follistatin-344 peptide and Breast Cancer Speculative research on the effects and levels of Follistatin in female research models of breast cancer  involved Reverse Transcription Polymerase Chain Reaction (RT-PCR) to check natural peptide levels. Results taken from females with under-expressed Follistatin indicated that only a few had normal or higher levels of Follistatin. Higher levels of Follistatin could be associated with a lower incidence of disease metastasis and a better prognosis.

4. Speculative Effects on Esophageal and Liver Cancer Barrett’s esophagus, a premalignant condition, involves transforming cells in the lower esophagus. Bone Morphogenetic Protein (BMP) might be a primary factor behind the metaplasia of the esophagus. Speculative research suggests that Follistatin may counteract the action of BMP and potentially prevent the development of esophageal cancer. Additionally, liver fibrosis, a condition predisposing to hepatocellular carcinoma, might see a significant improvement in the lifespan of liver cells (hepatocytes) with Follistatin. The peptide was suggested to reduce the risk of liver fibrosis by 32%, potentially leading to a reduction in the risk of hepatocellular carcinoma.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

What is AHK-Cu Peptide?

AHK-Cu is a short peptide with three amino acids attached to a copper molecule (Ala-His-Lys-Cu).  AHK-Cu peptide, also known as copper peptide, has been isolated in blood samples. This peptide may be responsible, in part, for growth and development of cells in the blood vessels. It has also been researched in relation to the generation of new blood vessels (angiogenesis). These actions of the AHK-Cu peptide are posited to be due to its potential to stimulate the production of another peptide called the Vascular Endothelial Growth Factor (VEGF). Producing new blood cells may help supply blood to biological structures such as skin and hair follicles, and may stimulate their development.

Researchers have also studied AHK-Cu in relation to its potential impact on Growth Factor Beta-1. Through its potential impact on Growth Factor Beta-1 and VEGF, AHK-Cu peptide may activate the replication and development of fibroblast cells. Fibroblasts are cells abundantly found in biological structures, including skin, hair follicles, and blood vessels. Fibroblasts are considered to activate the production of proteins such as elastin and collagen, essential participants of the extracellular matrix in the skin.

Research on AHK-Cu Peptide

Follicle Growth and Maintenance

AHK-Cu peptide may potentiate immense growth on follicle development and maintenance. Researchers suggest it may supplement follicle density by preventing possible loss and by stimulating new growth. Follicles may be found in highly vascular structures, areas where extensive network of blood vessels are concentrated, to supply blood to developing follicles. The supply of blood is considered to be crucial because follicles undergo a rapid cell turnover and appear to depend on the supply of blood and nutrients in the process. Along those same lines, blood supply has been suggested to limit the production of, and stability of existing follicles. AHK-Cu peptide may potentially promote new blood vessel development by triggering the release of VEGF.

Another important phenomenon that may potentially damage follicle development is the excessive conversion of testosterone to dihydrotestosterone (DHT). Researchers consider it to be a potentially critical pathology in certain conditions characterized by immense hair loss. AHK-Cu peptide might be relevant in these contexts, as researchers suggest it may prevent the conversion of testosterone to DHT. Second, it may potentially down-regulate the action of DHT on hair follicle receptors.

The hair follicles appear to undergo three main phases of growth: anagen, catagen, and telogen phase. The anagen phase is the growth phase of follicles, and is a highly active phase. Research suggests that AHK-Cu peptide may ‘trap’ the follicles in the anagen phase of the growth cycle and maintain that phase for a considerable duration (certain research findings suggest upwards of a year).

Cell Aging and Skin Structure

A subset of skin cells, fibroblasts are deemed responsible for the secretion of skin proteins such as collagen and elastin. These proteins are considered to lend the skin structure flexibility, and suppleness. Cell aging in the skin may lead to rapid decline in the number of fibroblasts. As a result, the amount of collagen and elastin endogenously produced begins to decline as well, introducing irregularities and textural inconsistencies in the skin and developing creases along the skin surface.

AHK-Cu peptide may potentiate the reversal of cell aging by triggering the growth and development of new fibroblasts. Once there are enough fibroblasts in the extracellular matrix of the skin, natural elastin and collagen production may follow. Research suggests that AHK-Cu may potentially stimulate the production of Type 1 collagen by up to 300%.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

Growth Hormone-Releasing Peptides (GHRPs)

Growth hormone-releasing peptides GHRPs are classified as synthetic peptides capable of inducing stimulatory effects on the endogenous secretion of growth hormone (GH). Research studies conducted on animal models have led scientists to explore and classify several research peptides within this family of peptides. However, researchers note that they appear to have no structural resemblance with Growth Hormone-Releasing Hormones and may potentially mediate their action by binding with specific cognate receptors present at the pituitary or hypothalamic level.

Ipamorelin

Ipamorelin is considered to be one of the most versatile synthetic peptides classified as a GHRP. Composed of only five amino acids, it appears to be a growth hormone secretagogue receptor (GHS-R) agonist. Research studies have posited that it may be relevant in various branches of scientific research, and may be implicated in gastrointestinal functioning, growth hormone production, and neurological impacts. Ipamorelin is considered by researchers to be a ‘gentle peptide’ compared to other peptides like Sermorelin or GHRP-6, as they assert it appears to affect only the growth hormone axis.

The binding of Ipamorelin peptide has been suggested to occur upon the ghrelin (growth hormone secretagogue) receptor. The ghrelin receptor (a.k.a. GHS-R) in the brain, liver, heart, and muscular structures, may potentiate the regulation of energy homeostasis and certain metabolic processes. It appears to be highly exclusive for growth hormone release from the pituitary gland.

Both Ipamorelin and a similar agonist, GHRP-6, belong to the class of third-generation GHRP. They are among the first synthetic peptides studied extensively in animal models. Ipamorelin and GHRP-6 appear to be similar in their functions. Both peptides, for example, have been suggested to release growth hormone at similar rates. However, there appears to be a moderate difference in how the two peptides mediate their action. GHRP-6 may potentially cause a release and an increase in cortisol and prolactin levels, whereas Ipamorelin potentially only selectively releases growth hormone.

Growth Hormone-Releasing Peptide-6

Growth hormone-releasing peptide-6 is a first-line synthetic hexapeptide and a met-enkephalin derivative. It comprises a chain of 6 synthetic D amino acids with the sequence (His-D-Trp-Ala-Trp-D-Phe-Lys-NH2). Additionally, the peptide also contains two methyl groups as modifications. It happens to be the first hexapeptide studied in animal model studies, and researchers identified it more than a decade ago.

GHRP-6 has been suggested by researchers to recognize and bind to specific receptors present at the pituitary or hypothalamic glands. Studies have suggested that GHRP-6 receptors are abundant in different peripheral tissues such as the heart, adrenal, ovary, testis, lung, and skeletal muscle.
Studies in animal test models posit that GHRP-6 may stimulate ghrelin response. Ghrelin, in turn, may increase the production of growth hormone (GH) by acting at the level of the pituitary or hypothalamus through a specific receptor that is different from that of the endogenous Growth Hormone-Releasing Hormone (GHRH). The four essential organs of the test subjects that have been observed to be influenced under exposure to GHRP-6 include the pituitary gland, central nervous system, liver, and stomach.

Research studies in animal models have highlighted that GHRP-6 and Ipamorelin may potentially stimulate ghrelin, “the hunger hormone,” by associating with its ghrelin receptor. This association may trigger a cascade of events by inducing increased growth hormone production.

Іn comparison with GHRP-6, Iраmоrеlіn appears to induce a more selective activation of GHRH as it does not appear to have any effect on cortisol or prolactin. It may potentially metabolize slower than GHRP-6, and may possibly remain present in the bloodstream for a longer duration, adding to its stability.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

The speculation is that Thyrotropin might influence the synthesis of thyroglobulin and the growth of thyroid cells. Researchers suggest that the paraventricular cells of the hypothalamus might secrete a Thyrotropin-releasing hormone (TRH), which then may command the release of the thyrotropin hormone. This release might form a hypothalamic pituitary thyroid axis in which the regulation of the secretion of hormones could occur through a feedback mechanism. It is suggested that whenever there is excess thyroxine in the circulation, this might act on the specific receptors of the pituitary, potentially suppressing the level of thyrotropin and, ultimately, Thyrotropin-Releasing Hormone. If there is insufficient thyroxine in the circulation, researchers propose that the positive feedback from elevated thyrotropin levels may stimulate the release of further thyroxine.

Thyrotropin levels might naturally be elevated in primary hypothyroidism and suppressed in thyrotoxicosis.The circulating levels of thyrotropin may manifest circadian and pulsatile variation, with concentration exceptionally high during rapid growth and development and increased metabolic demand. Another hormone released by the hypothalamus, called Somatostatin, might antagonize the action of Thyrotropin.

Thyrotropin is considered a glycoprotein consisting of Alpha and Beta subunits. The alpha subunit appears to be similar to other glycoprotein hormones such as Luteinizing hormone (LH), Follicle Stimulating Hormone (FSH), and Chorionic Gonadotropin (HCG). Conversely, the beta chain might differ in these glycoproteins, imparting unique biological characteristics. Researchers suggest that these glycoproteins function through Cyclic Adenosine Monophosphate (cAMP), potentially signaling the second messenger system. The dual messenger system may convert Adenosine monophosphate into Cyclic adenosine monophosphate.

Thyrotropin might activate another signaling cascade, called the Inositol Triphosphate second messenger system (IP3). Researchers propose that Thyrotropin might activate specific G protein-coupled receptors on the surface of thyroid follicular cells, leading to the activation of both cAMP and IP3 /Ca+2 pathways. This activation might ultimately enhance iodine uptake in the follicular thyroid cells, and an array of further steps might lead to the formation of T4 and T3, considered to be responsible for all the downstream physiological effects of the thyroid hormone.

Research Implications of Thyrotropin

Thyrotropin has been hypothesized to impact various physiological processes via the production of Thyroxine T4 and Triiodothyronine T3.

Regulation of metabolism: Thyrotropin peptide might stimulate the thyroid gland’s secretion of Thyroxine T4 and Triiodothyronine T3. This hormone may activate various metabolic processes, including increased glucose absorption, gluconeogenesis, glycogenolysis, lipolysis, and synthesis/degradation of the protein.

• All of these phenomena could lead to a net state of catabolism.
• The speculation is that the thyroid hormone might regulate metabolic rate, and thereby weight.
• It may help maintain temperature homeostasis in animal models.
• It may regulate the rate of the regeneration process of various tissues.
• The thyroid hormone might affect gastric emptying.
• It may control muscle contraction.

Potential of Thyrotropin as a Screening Test: Speculatively, it might be the first-line screening test in diagnosing both a state of hypothyroidism and hyperthyroidism. Measuring the thyrotropin level may prove to be a better method than measuring direct T3 and T4. This consideration was formed for two reasons. First, the thyrotropin levels may be affected before the T3 and T4 groups appear to change in any pathological state. Secondly, it may be more reliable than T3 and T4 levels as these fluctuate and remain volatile.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.