- today
Epithalon (epitalon) is a four-amino-acid-long peptide derived from a naturally occurring pineal gland protein. It has been shown, through extensive animal research, to be a potent regulator of cell metabolism, including growth and cell division. In particular, epithalon is able to extend cell survival in vitro. At least part of the reason that epithalon can extend cell survival comes down to its action on telomeres.
Telomeres
Telomeres, the repetitive nucleotide sequences at the end of linear chromosomes, protect DNA from degradation and deterioration. A telomere sequence starts out at about 11,000 DNA units (bases) long, but decreases in length to about 4,000 bases in old age. Interestingly, the rate of telomere degradation is faster in men than in women.
Telomeres are like self-sacrificing guards against actual DNA damage. Because they don’t code for anything, telomeres can be sacrificed when DNA is replicated (copied) without actually damaging any genes. This is necessary because DNA replication is an imperfect process. Of course, telomeres eventually get too short to serve their protective role. Cells have mechanisms to detect when this happens. When a telomere becomes too short, the cell either becomes inactive or dies. This is essentially the process of aging at a molecular level.
Epithalon and Telomerase
There is an enzyme, called telomerase reverse transcriptase (telomerase for short), that rebuilds telomeres and thus slows the molecular ageing of cells. Unfortunately, telomerase is not 100% effective and thus ageing occurs even with this enzyme around.
Research in 1998 demonstrated that artificially boosting telomerase activity could not only extend the lifespan of human somatic (skin) cells in culture but could actually make them immortal. Since that time, researchers have sought to boost telomerase activity through the use of gene therapy, metabolic suppression, and torpor/hibernation. Each of these approaches has significant drawbacks and none has, as of yet, been demonstrated to have much effect on human ageing.
In 2003, the first evidence that epithalon could impact telomerase activity was demonstrated in human somatic cells in vitro. The study found that epithalon could be added to fibroblast cultures that had no detectable telomerase activity to stimulate the production of telomerase. All of the cells demonstrated telomere lengthening [1].
Epithalon: Beyond Telomerase
The idea lost traction for a short period, but was revived again in 2016 when research, again using cultured fibroblasts, found that epithalon’s effects extend beyond activation of telomerase. It turns out that epithalon also inhibits the accumulation of senescent proteins like MMP-9. Senescent proteins are those that arise as a result of aging and signal that cells should stop dividing [2].
In addition to inhibiting the production of MMP-9, epithalon has been shown to suppress caspase-dependent apoptosis, [2]. This is one of the main processes by which cells that have short telomeres or other signs of aging are killed.
All of these activities of epithalon are, in some way, connected to its effects on telomere length. That said, it isn’t clear if the above effects are the indirect result of epithalon protecting telomeres or might be a direct result of an as-of-yet-unidentified action of epithalon.
More than Just Anti-Aging
Beyond the fact that epithalon can impact the aging process, its effects on caspase are of interest in several medical conditions. Excessive caspase activity has been identified in neurodegenerative disorders, like Alzheimer’s disease, as well as in numerous autoimmune conditions [3,4]. A peptide capable of controlling caspase activity may not just slow the aging process, it may prevent or slow the progression of serious neurological and autoimmune diseases.
Resources
1. Khavinson, V. K., Bondarev, I. E. & Butyugov, A. A. Epithalon peptide induces telomerase activity and telomere elongation in human somatic cells. Bull. Exp. Biol. Med. 135, 590 – 592 (2003).
2. Lin’kova, N. S. et al. Peptide Regulation of Skin Fibroblast Functions during Their Aging In Vitro. Bull. Exp. Biol. Med. 161, 175 – 178 (2016).
3. Goodsell, D. S. The molecular perspective: caspases. The Oncologist 5, 435 – 436 (2000).
4. McIlwain, D. R., Berger, T. & Mak, T. W. Caspase functions in cell death and disease. Cold Spring Harb. Perspect. Biol. 5, a008656 (2013).
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