L-Ergothioneine is a natural and water-soluble compound which has been first isolated in rye ergot (Claviceps purpurea) in 1909 by the French pharmacist Charles Tanret .
To date, the only organisms known to be able to synthesize L-ergothioneine are bacteria, more specifically mycobacteria  and cyanobacteria , and fungi of the phyla Ascomycota, Zygomycota and Basidiomycota, which include lower fungi (molds) and higher edible fungi [4-9].
The biosynthesis of L-ergothioneine has been studied in Neurospora crassa [10-12] and mycobacteria . In the first stage, L-histidine is methylated threefold by one specific N-methyltransferase to yield the betaine derivative L-hercynine, with S-adenosyl-methionine as the methylating agent. Sulfur is then added to L-hercynine in an oxidation reaction catalyzed by an iron-containing enzyme. In N. crassa and mycobateria, the reaction uses cysteine or γ-glutamylcysteine, respectively, as the sulfur-donating substrate. Both pathways pass through the formation of hercynyl-cysteine sulfoxide, which is cleaved to yield L-ergothioneine and pyruvate by a β-lyase, in the presence of pyridoxal phosphate.
L-Ergothioneine is found throughout the living world from plants to man, including in particular the well-known horseshoe crab (Limulus polyphemus), one of the oldest living animal species on Earth . However, these organisms are unable to synthesize L-ergothioneine. Plants absorb L-ergothioneine via symbiotic associations between their roots and soil fungi [15,16]. Animals and humans only absorb L-ergothioneine via their respective food chains [3,5,17,18]. In animals, intestinal microbiota has been shown not to contribute to L-ergothioneine occurence in the body [19,20].
The determination of the L-ergothioneine content in common foods shows that edible mushrooms, black and red beans, oat bran, garlic and some meat products (liver and kidney) are the main dietary sources of this compound for man [21,22].
L-Ergothioneine has been identified or assayed in plant tissues [21,23,24] and animal tissues/fluids [14,25-46], including human ones [18,25,27,42,44,47-51].
For a given animal tissue or fluid, high variations are observed in L-ergothioneine concentration, which may of course reflect dietary variations but also the lack of specificity and sensitivity of earlier analysis methods. This highlights the need to verify older data using more recent analytical techniques such as liquid chromatography coupled to mass spectrometry .
L-Ergothioneine is distributed in most tissues, but unevenly, as shown in the mouse: liver > kidney ≃ heart > skin ≃ lung ≃ spleen ≃ small intestine ≃ blood (erythrocytes) > pancreas ≃ testis ≃ muscle ≃ large intestine ≃ brain . Cross-species analysis of its content in organs also reveals differences across species [5,44].
Most often found in the sub-millimolar range, L-ergothioneine may reach millimolar concentrations in some tissues or fluids, for example the lens in man , various ocular tissues in cows and pigs , and seminal plasma in boars .
At subcellular level, it has been shown that L-ergothioneine is mainly distributed in the cytoplasm [28,32]. Use of tritiated L-ergothioneine enabled demonstration that it is also distributed, to a lesser extent, in membranes, mitochondria, nuclei and microsomes .
About a century after the identification of L-ergothioneine, the discovery that it is the physiological substrate of the OCTN1 transporter  has boosted the knowledge of this unique natural compound. Earlier characterized in humans and described as a multispecific organic cation transporter [54,55], OCTN1 (also known as SLC22A4) was shown to have a high affinity for L-ergothioneine (Km=21μM) and to be specific for this compound, whose transport is also sodium dependent [53,56]. ETT, for ergothioneine transporter, was thus proposed as a new name for OCTN1 .
In humans, the expression of OCTN1/ETT has been shown in numerous organs, with the highest level in bone marrow, small intestine, trachea, fetal liver, kidney, cerebellum and spinal cord [53,56]. In hematopoietic tissues, OCTN1/ETT is strongly expressed in the erythroid lineage, from the CD71+ (transferrin receptor) progenitor cells until mature erythrocytes [53,57]. In peripheral blood mononuclear cells, OCTN1/ETT is predominantly expressed in CD14+ and is absent in lymphocytes [53,58]. Taken together, these results show that OCTN1/ETT is associated with myeloid cells.
The expression of OCTN1/ETT has been evidenced on the cytoplasmic membrane of various cell types, such as Sertoli cells , endothelial cells [60,61], dermal fibroblasts [62,63], epidermal keratinocytes , brain neurons , neural progenitor cells , and epithelial cells, mainly apically in the latter, as evidenced in renal , pulmonary [66,67], ocular , small intestinal  and nasal [66,70] epithelial cells. In basal epidermal keratinocytes  and most probably in glandular cells of seminal vesicles , the expression of OCTN1/ETT is basolateral.
OCTN1/ETT expression has also been evidenced at mitochondrial level , but this result has been questioned .
Metabolomic analysis in OCTN1/ETT gene knockout mice has shown an almost complete disappearance of L-ergothioneine in the tissues of these mice . This has also been shown in a more in-depth study of the various regions of the brain in the knockout mice  and in the OCTN1/ETT knockout zebra fish [73,74]. These studies confirm the key role of the OCTN1/ETT transporter in the tissue absorption of L-ergothioneine. Consistently, the tissue distribution of L-ergothioneine matches the OCTN1/ETT expression pattern and OCTN1/ETT mRNA expression is correlated to L-ergothioneine content [44,45].
OCTN1/ETT expression is up-regulated by pro-inflammatory cytokines (TNF-α, IL-1β) via activation of the transcription factor NF-κB [75,76], and is also under the control of the transcription factors Sp1 and RUNX1 .
OCTN1/ETT-gene variants have been associated with chronic inflammatory diseases in specific populations, e.g. the slc2F2 variant with rheumatoid arthritis [58,77] and the L503F variant with Crohn's disease [78,79], the latter being in particular associated with a slightly more efficient L-ergothioneine transport . The involvement of these variants as causal genes for these diseases has not been demonstrated and is even questioned for the L503F variant . Indeed, it has been suggested that the increase of L503F variant frequency is the result of genetic hitchhiking . Interestingly, the authors of this study suggest that it would also be an adaptation to low dietary levels of L-ergothioneine among early Neolithic farmers in the Fertile Crescent . Furthermore, a recently published study provides new insights supporting a beneficial effect of OCTN1/ETT on intestinal inflammation by mediating uptake of L-ergothioneine .
Finally, it is interesting to highlight that OCTN1/ETT knockdown studies support a role of this transporter and L-ergothioneine in cell proliferation and differentiation, as shown in erythroid cells  and neuronal cells [45,64].
The kinetics of incorporation and tissue elimination of L-ergothioneine were studied in rodents, following oral absorption of L-ergothioneine [42,84-86] or after intraperitoneal or intravenous injection . These studies show that L-ergothioneine has a slow turnover. It accumulates gradually and at different speeds in the organs and in blood, and it is also strongly retained in tissues.
A relatively early study in rats showed the effect of age and gender on the blood concentration of L-ergothioneine . In that study, the authors show that, in rats maintained on a normal diet, the blood concentration of L-ergothioneine doubles during the first 3 months of life for both sexes. But while this concentration is stabilized up to 18 months (end of study) in the female, it reaches a plateau at a value twice as high in male rats. These authors have also shown that testosterone may be the cause of this increased accumulation in the male. No other study of gender effect on tissue concentration of L-ergothioneine has been reported to date.
The effect of age on erythrocyte concentration of L-ergothioneine was also identified in a population of men with an increase in concentration between the age of 1 and 10 years, which peaks at about 18 and decreases until about 50, when it stabilizes .
In rats, L-ergothioneine has been shown to pass from the mother to the neonate or pup during weaning via maternal milk , which is consistent with the evidencing of the OCTN1/ETT expression in the mammary epithelium [88,89].
In the current state of knowledge, no metabolite of L-ergothioneine has been identified so far in man or animals.
The following intrinsic properties of L-ergothioneine have been shown in vitro:
- Sequestering, reducing or disactivating highly oxidizing chemical entities: hypochlorous acid , peroxynitrite anion , peroxyl radicals , ferrylmyoglobin , singlet oxygen [94,95], and photosensitizer in the excitated state .
- Chelating metal cations (copper, mercury, cadmium, zinc) [97-99] and, in particular, preventing the pro-oxidative effects of copper [100-102].
In a biological context, numerous studies have evidenced antioxidant activities and/or protective effects of L-ergothioneine under experimental conditions involving oxidative stress, i.e. following stimulation by pro-inflammatory or pro-oxidizing agents/conditions.
Such in vitro properties of L-ergothioneine are summarized below:
- Protection of bacteriophages T4 and P22 against inactivation induced by γ-irradiation .
- Protection of isolated rat heart from ischemia/reperfusion-induced injury .
- Protection against oxidative damage to macromolecule, including nuclear and mitochondrial DNA, proteins and lipids, induced by:
– reactive oxygen species in HeLa cells  and PC12 cells ,
– peroxynitrite anion in N-18-RE-105 cells ,
– UV  and UVA/visible light  in human epidermal keratinocytes,
– UVA in human dermal fibroblasts ,
– UVB in HaCaT cells ,
– β-amyloid peptide in PC12 cells .
- Inhibition of UVB-induced up-regulation of TNF-α expression , as well as of UVA-induced MMP-1  and peroxide  production in human dermal fibroblasts.
- Inhibition of UV-induced apoptosis, caspase-9 activity and PARP cleavage in human epidermal keratinocytes .
- Inhibition of β-amyloid peptide-induced apoptosis, caspase-3 activity and PARP cleavage in PC12 cells .
- Inhibition of hydrogen peroxide-induced apoptosis and p38 MAPK phosphorylation in PC12 cells .
- Prevention of cisplatin-induced inhibition of the growth of axon and dendrite in primary cortical neurons .
- Inhibition of hydrogen peroxide- and TNF-α-induced NF-κB activation and IL-8 release in epithelial cells .
- Protection against cell death induced by reactive oxygen species in human brain microvascular endothelial cells .
- Prevention of phosphorylation of NO synthase, and decrease of SOD and catalase activities induced by oxidized LDL in human umbilical vein endothelial cells (HUVECs) .
- Inhibition of oxidized LDL-induced apoptosis of HUVECs, in association with inhibiting Bax activation, Bcl-2 downregulation and caspase-3 activity elicited by oxidized LDL .
- Inhibition of oxidized LDL-induced p38 phosphorylation and NFκB activation in HUVECs, substantiated by the inhibition of the expression of cell adhesion molecules (VCAM-1, ICAM-1 and E-selectin), and subsequent monocyte binding . This inhibitory effect of L-ergothioneine on monocyte adhesion was also demonstrated in human artery endothelial cells following IL-1β stimulation .
- Inhibition of IL-6 production by C2C12 myoblasts  and 3T3-L1 adipocytes  following stimulation by palmitic acid and TNF-α, respectively.
- Inhibition of mushroom polyphenoloxidase activity .
Some protective effects of L-ergothioneine against oxidative stress-induced injury were not confirmed [21,119], owing to differing experimental conditions and/or concentrations used.
Furthermore, consistently with its in vitro antioxidant properties, L-ergothioneine has been shown to improve food preservation by preventing discoloration and lipid peroxidation of meat [118,120].
Interestingly, a recent study on neural progenitor cells has demonstrated that L-ergothioneine inhibits cell proliferation and promotes neuronal differentiation, in correlation with inhibiting the intracellular production of reactive oxygen species and up-regulating Math1 gene, respectively .
With respect to reproduction, the following effects of L-ergothioneine have been described:
- Decrease of the inhibitory effect of p-chloromercuribenzoic acid on spermatozoa respiration in the guinea pig .
- Increase in the acrosome reaction of guinea pig spermatozoa, and increase in the fertility of mouse spermatozoa, both in vitro and in vivo in the latter case .
- Increase in the oocyte maturation and embryonic development in the ewe .
- Increase in spermatozoa preservation in the guinea pig , stallion  and ram [125-127].
In vivo protective effects of L-ergothioneine are summarized below:
- Protection of N. crassa conidia against peroxide damage during germination, and improvement of their longevity [12,128].
- Decrease of nitrite-induced methemoglobin formation in rabbits  and rats .
- Prevention of the teratogenic effects of cadmium in mice .
- Protection against ethionine-induced liver injury in rats .
- Decrease of the rate of embryo malformation in diabetic rats .
- Protection against ischemia/reperfusion-induced injury in rat liver  and small intestine .
- Protection against oxidative damage induced by ferric-nitrilotriacetate in rat liver and kidney .
- Neuroprotection against NMDA excitotoxicity in rats .
- Neuroprotection against cisplatin , β-amyloid  and D-galactose  toxicity in mice.
- Protection against cytokine-induced lung inflammation and injury in rats .
- Prevention of streptozotocin-induced impairment of relaxation to acetylcholine in rat artery .
Through these in vivo studies, it was in particular shown that L-ergothioneine treatment, with respect to no treatment, resulted in decreasing lipid peroxidation, saving endogenous antioxidant defenses, such as vitamin E and glutathione, and protecting tissue against oxidative stress-induced injury.
No clinical data have been published to date regarding the effect of specifically administering pure L‑ergothioneine in humans. However, the following interesting observations, sometimes contradictory, have been reported in humans on the variation of L-ergothioneine concentration in various pathological conditions associated with an inflammatory process, compared to that of healthy control subjects:
- Decrease of L-ergothioneine concentration in erythrocyte of patients with chronic myeloid leukemia .
- Decrease of L-ergothioneine concentration in the lens eye of cataract patients, and all the more when the degree of cataract is high .
- Decrease  or increase  of L-ergothioneine concentration in erythrocyte of patients with rheumatoid arthritis.
- Increase of L-ergothioneine concentration in erythrocyte of women in pre-eclampsia condition .
- Decrease  and increase  of L-ergothioneine concentration in erythrocyte and intestinal mucosa, respectively, of patients with Crohn's disease.
- Decrease of the seric concentration of L-ergothioneine in patients with Parkinson's disease .
Future studies will be needed to better understand the origin of these variations and to assess their clinical interest.
While many studies continue to highlight protective effets of L-ergothioneine under experimental conditions involving oxidative stress, the exact role of L-ergothioneine remains unknown today. It has been suggested that L-ergothioneine may represent a new vitamin , but its essential role has not been discovered yet through deprivation or knockout in vivo studies, the resulting animals being phenotypically similar to control animals. Such an essential role might be only displayed after a longer period of observation and/or under stress conditions.
In this context, it is essential to emphasize the increase sensitivity to oxidative stress that has been reported in OCTN1/ETT-knockdown cells , OCTN1/ETT-knockout mice [42,76], and OCTN1/ETT-knockout zebrafish , as well as in microorganisms whose ability to produce L-ergothioneine was prevented by disruption of a biosynthetic gene .
Given its tissue absorption by a specific transporter, its in vivo protective effects, and the results of knockdown/knockout studies, L-ergothioneine can at least be considered as a physiological antioxidant endowed with anti-inflammatory properties.
However, naming L-ergothioneine an "antioxidant" might be confusing if this property is only related to its ability to scavenge reactive oxygen/nitrogen species. Indeed, chemically speaking, L-ergothioneine is a weak reducing agent at physiological pH, due to the fact that its thione tautomeric form predominates at these pH . This accounts in particular for its stability towards oxygen in aqueous solution, which distinguishes it from other biological thiols such as glutathione and dihydrolipoic acid.
In a biological context, another antioxidant mechanism may account for the protective effects of L-ergothioneine. It is related to the ability of L-ergothioneine to specifically interact with proteins. It is implicit when considering its transporter, and it has recently been described for the first time in the case of a bacterial enzyme for which L-ergothioneine is used as co-factor . This putative mechanism remains to be investigated in regard to redox alterations of protein cysteine residues, such as disulfide formation, nitrosylation and metal coordination. It is now well established that these reversible chemical modifications play a key role in the redox signaling of cellular events and cell fate. So in that case, defining L-ergothioneine as a modulator of redox homeostasis would be more appropriate to describe its antioxidant mechanism of action.
Tissue absorption of L-ergothioneine by a specific transporter implies a beneficial role of this unique micronutrient. Furthermore, L-ergothioneine has been shown to be not mutagenic, nor genotoxic [150,151], and without an adverse effect on a broad range of reproductive parameters . Its good tolerance was also exemplified in investigating various health indications [153-155]. A better understanding of its role requires more studies and deserves further attention with regard to human health, in particular as micronutrient deficiencies may increase the risk of developing age-related disorders and diseases [156-158]. Their development is correlated with a mild pro-inflammatory state in which oxidative stress, i.e. disruption of redox signaling and control , plays a major role.
This has led Tetrahedron to develop a novel industrial process (WO2011042480), using a biomimetic and sustainable approach , to make L-ergothioneine available and to supply it in bulk quantities. Tetrahedron supplies L-ergothioneine for Research and can propose a GMP quality product whose characterization and safety have been assessed according to regulatory requirements for its use as a nutritional ingredient in humans.
For more information on our product, please contact us.
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