Cartalax Peptide: Potential Implications for Cellular Aging, Renewal, and Resilience to Stress

Cartalax (AED or T-31 peptide) is a synthetic tripeptide that some investigators categorize among the so-called Khavinson peptides. These peptides are a set of short amino acid chains that may exert regulatory influences on biological functions and are consequently termed “bioregulators.” Researchers have been interested in the designation “bioregulator” in reference to Cartalax peptide because it indicates that it might modulate fundamental physiological mechanisms related to DNA and gene expression. According to some reports, this peptide may have been isolated from kidney tissue extracts containing polypeptides.

Researchers have noted the peptide’s sequence of Alanine, Glutamate, and Aspartate (AED) in the alpha-1 chain of type XI collagen. This structural protein might be involved in maintaining tissue integrity under specific conditions.  Based on its potential as a bioregulator, scientists have observed that Cartalax peptide may influence certain biological pathways related to cellular aging within experimental frameworks. However, there is ongoing debate regarding how it might achieve these actions.

 

Research

Cartalax Peptide and Cell Renewal

Cartalax peptide is sometimes described as a synthetic peptide that may influence several markers linked to cell proliferation and programmed cell death. For example, Khavinson et al. proposed that Cartalax peptide may diminish the expression of p53 (a tumor cell suppressor and pro-apoptotic transcription factor) in aging renal epithelial cell cultures.⁽¹⁾ This decrease in p53 might suggest a relative decrease in apoptosis, which may thereby create conditions that favor cell renewal. Cartalax peptide apparently did not raise Ki-67 levels (a widely tracked nuclear protein that is often relevant to research settings as a proliferation-associated marker) in these specific renal epithelial cell cultures. Yet, Lin’kova et al. reported a potentially significant Ki-67 increase in fibroblast cultures exposed to Cartalax peptide.⁽²⁾  Fibroblasts are considered to be specialized cells most commonly found in connective tissue. They play a critical role in synthesizing and maintaining the extracellular matrix—the intricate network of proteins and carbohydrates that provides structural and biochemical support to surrounding cells. Notably, these cells produce collagen (a primary protein in connective tissue) as well as other matrix components such as fibronectin and various proteoglycans. Because Ki-67 is frequently employed to gauge cell proliferative capacity, this observation might imply that Cartalax peptide has some ability to boost or maintain cell renewal in certain cell types.

Lin’kova et al. also noted that Cartalax peptide may be possibly upregulating CD98hc (a multifunctional cell membrane protein that is implicated in amino acid transport and integrin signaling) in fibroblasts. By increasing CD98hc expression, Cartalax peptide might support the fundamental activities that rely on nutrient uptake and cell adherence. Regarding programmed cell death, Cartalax peptide appears to reduce caspase-3 expression in both early- and advanced-passage fibroblasts, suggesting that it may help lessen apoptotic signaling. Caspase-3 is often viewed as a central “executioner” in the apoptosis cascade, so its apparent downregulation may point toward a protective mechanism for sustaining fibroblast viability. Indeed, Lin’kova et al. commented that the peptide “reduced the level of apoptosis in young and aged cultures.” Cartalax peptide was further noted in connection with matrix metalloproteinase-9 (MMP-9), a protease that is commonly linked to extracellular matrix (ECM) remodeling. In later-passage fibroblast cultures, Cartalax peptide may lead to diminished MMP-9 expression, hinting at a possible reduction in excessive ECM breakdown. In separate experiments, Chalisova et al. further confirmed that Cartalax peptide might both raise Ki-67 expression and lower p53 levels in kidney culture systems.⁽³⁾ These findings may reflect the potential of Cartalax peptide to modulate cell cycle progression and apoptotic signaling, possibly through adjustments in the genes that govern cell proliferation and survival markers, consequently upregulating cell renewal.

Cartalax Peptide and Cell Aging

In addition to potentially decreasing the expression of p53, further research by Khavinson et al. indicates that Cartalax peptide may also lower levels of p16 and p21.⁽⁴⁾ Specifically, p16 and p21 may function as cyclin-dependent kinase inhibitors that typically limit cell cycle progression. Because these three factors are commonly associated with cell aging, Cartalax peptide might influence several checkpoints involved in cellular senescence. Concurrently, Cartalax peptide may upregulate SIRT-6, an enzyme believed to participate in chromatin remodeling and metabolic regulation. Decreased SIRT-6 levels are sometimes correlated with cellular aging, so a Cartalax peptide-induced increase in SIRT-6 may reflect mechanisms that counteract age-related decline. In addition to its potential actions on protein levels, Cartalax peptide is hypothesized to form energetically favorable complexes with specific DNA motifs—particularly the sequence d(ATATATATAT)2—within the DNA minor groove. Such sequence-specific binding may impact local chromatin conformation and, in turn, influence the transcription of genes linked to cell aging. Although the precise structural aspects remain under investigation, these DNA interactions might underlie Cartalax peptide’s reported actions on senescence-associated markers.

Further research by Lin’kova et al. suggests that Cartalax peptide may also alter the expression of TNKS2 in replicative cellular aging models.⁽⁵⁾  TNKS2 encodes tankyrase 2, an enzyme that is often considered essential for telomere stability through regulation of telomeric repeat-binding factors. Telomeres are repetitive DNA sequences at chromosome ends that shorten with each cell division, and their progressive shortening is frequently associated with cellular aging. Tankyrase 2 is additionally believed to be involved in metabolic control, mitotic processes, and Wnt signaling pathways. In this context, “Wnt” refers to a group of proteins that govern cell proliferation, polarity, and fate decisions. By modulating TNKS2, Cartalax peptide might, therefore, affect telomere maintenance, glucose metabolism, cell cycle progression, and various developmental processes. In aging cell cultures, any increase in tankyrase 2 levels might help stabilize telomeres or modify metabolic pathways at a point when cell division becomes limited.

Cartalax Peptide and Cellular Stress Resistance

Ashapkin et al. are one of the first research groups to point out that Cartalax peptide may increase.

IGF-1 transcripts in various aging cell culture models.⁽⁶⁾ Specifically, they mentioned that “IGF1 gene expression levels were very similar in [different] cell culture aging models, being enhanced by 3.5-5.6 fold upon the addition of the peptides” such as Cartalax peptide. IGF-1 is frequently viewed as a mediator of anabolic or growth-associated processes, and its potential elevation in senescent cells might reflect an adaptive attempt to support synthetic or reparative pathways during stressful conditions. Researchers have noted that this apparent IGF-1 upregulation remains relatively consistent across different culture systems, which may imply that Cartalax peptide’s influence on IGF-1 does not rely heavily on a particular cell type. According to the same researchers, it also appears that Cartalax peptide might reduce the expression of TERT (Telomerase Reverse Transcriptase), the key enzymatic subunit involved in maintaining telomere length.

Suppose older cells elevate TERT as a form of stress response.  In that case, a decrease in TERT under Cartalax peptide exposure might suggest a possible transition toward a more stable or less reactive gene expression pattern. Another observation reported by multiple investigators is that Cartalax peptide may elevate NFκB (Nuclear Factor kappa B) transcript levels, although the exact consequences of this potential induction remain uncertain. NFκB, commonly considered a pivotal regulator of inflammation and stress responses, might be upregulated as part of a compensatory mechanism in aging cells. Cartalax peptide’s possible impact on NFκB might, therefore, represent only one aspect of a broader cellular network encompassing senescence, inflammatory pathways, and metabolic adaptation.

You can find Cartalax for sale with 99% purity, on our website (available for research use only).

NOTE: These products are intended for laboratory research use only. This peptide is not intended for personal use. Please review and adhere to our Terms and Conditions before ordering.

 

References:

1. Khavinson VKh, Lin’kova NS, Polyakova VO, Durnova AO, Nichik TE, Kvetnoi IM. Peptides regulate the expression of signaling molecules in kidney cell cultures during in vitro aging. Bull Exp Biol Med. 2014 Jun;157(2):261-4. doi: 10.1007/s10517-014-2540-y. Epub 2014 Jun 24. PMID: 24958378.
2. Lin’kova NS, Drobintseva AO, Orlova OA, Kuznetsova EP, Polyakova VO, Kvetnoy IM, Khavinson VKh. Peptide Regulation of Skin Fibroblast Functions during Their Aging In Vitro. Bull Exp Biol Med. 2016 May;161(1):175-8. doi: 10.1007/s10517-016-3370-x. Epub 2016 Jun 4. PMID: 27259496.
3. Chalisova NI, Lin’kova NS, Nichik TE, Ryzhak AP, Dudkov AV, Ryzhak GA. Peptide Regulation of Cells Renewal Processes in Kidney Tissue Cultures from Young and Old Animals. Bull Exp Biol Med. 2015 May;159(1):124-7. doi: 10.1007/s10517-015-2906-9. Epub 2015 Jun 2. PMID: 26033601.
4. Khavinson VKh, Tarnovskaia SI, Lin’kova NS, Poliakova VO, Durnova AO, Nichik TE, Kvetnoĭ IM, D’iakonov MM, Iakutseni PP. [Tripeptides slow down the aging process in renal cell culture]. Adv Gerontol. 2014;27(4):651-6. Russian. PMID: 25946838.
5. Linkova N, Khavinson V, Diatlova A, Myakisheva S, Ryzhak G. Peptide Regulation of Chondrogenic Stem Cell Differentiation. Int J Mol Sci. 2023 May 8;24(9):8415. doi: 10.3390/ijms24098415. PMID: 37176122; PMCID: PMC10179481.
6. Ashapkin V, Khavinson V, Shilovsky G, Linkova N, Vanuyshin B. Gene expression in human mesenchymal stem cell aging cultures: modulation by short peptides. Mol Biol Rep. 2020 Jun;47(6):4323-4329. doi: 10.1007/s11033-020-05506-3. Epub 2020 May 12. PMID: 32399807.