elastina

Otros Nombres

Beta-elastinElastin (Bonito)Elastin (Cowhide)Elastin from bovine neck ligamentElastin from pigElastin hydrolysateElastin hydrolyzateElastin partial hydrolyzateElastin peptidesElastin polypentapeptideElastin, bovineElastin, bovine neck ligament, alkaline extractedElastin, soluble, from human lungElastin-like peptidesElastineElastinsElastins, hydrolyzatesELPHydrolysed elastinHydrolyzed elastinHydrolyzed marine elastin peptidesMarine elastinMarine elastin peptidesProelastinSoluble elastinTropoelastinWater-soluble elastin

Sinopsis

Elastin: A Comprehensive Encyclopedic Reference

1. Identity: Names, Sources, and Preparations

Chemical and Biological Identity

Elastin is one of the most abundant proteins in the body, functioning as a stretchy protein that resembles a rubber band — it can stretch out (extend) and shrink back (recoil). Elastin is an extracellular matrix protein that lends elasticity and resilience to tissues such as the arteries, lungs, tendons, skin, and ligaments. Elastic fibers have two components, one of which is encoded by the ELN gene. This protein has a high proportion of hydrophobic amino acids like glycine and proline, forming mobile hydrophobic domains.

The ELN gene is located on chromosome 7 of the human genome. Alternative splicing of the ELN gene results in the formation of at least 11 tropoelastin isoforms in humans. In its mature, insoluble form, the protein is referred to as elastin. Its soluble monomeric precursor is known as tropoelastin. Tropoelastin is a soluble precursor of elastin; it is a peptide with a molecular weight in the range of 70–75 kDa.

Elastin is a highly polymerized insoluble protein in the extracellular matrix, and elastic laminae are major structures of the blood vessels that confer elasticity to the extracellular matrix. The CAS registry number for elastin (from bovine neck ligament) is 9007-58-3.

Natural Sources

Elastin is a major component of tissues in the body that require stretchiness, like the lungs, bladder, large blood vessels, and some ligaments. Smaller amounts exist in skin and ear cartilage.

For supplementation and cosmetic use, elastin is sourced from several animal tissues:

Bovine neck ligament (ligamentum nuchae): The ligament extraction is comprised of taking dissected ligamentum nuchae ligaments and removing as much fat and excess connective tissue as possible. Bovine neck ligament was historically used as the raw material for cosmetics.
Marine (fish) sources: Marine-derived elastin protein is the main source of elastin supplements. Fish are rich in elastin, which is processed and hydrolyzed to yield concentrated, biologically active peptides.
Porcine and avian sources: Rat, sheep, and porcine aorta can be used as a source of elastin. Water-soluble elastin can also be extracted from broiler skin using sodium chloride, sodium hydroxide, and oxalic acid treatment before freeze-drying.

With the discovery of BSE and poultry infectious diseases, the safety of bovine-sourced material has been questioned. As a result, people have explored methods for producing elastin peptides using bovine ligament, bovine cardiac tube, bonito arterial ball, and porcine cardiac large artery as raw materials, achieving the purpose of beauty by oral administration and skin care.

Common Forms and Preparations

Mature elastin is nearly insoluble, making direct supplementation impractical without processing. The soluble tropoelastin molecules secreted into the extracellular space synthesize to form elastin filaments and sheets via crosslinking of the tropoelastin molecules primarily by crosslinking of lysine amino acid residues to form desmosine and isodesmosine. Mature elastin is amorphous and contains many crosslinks which makes it nearly impossible to solubilize.

The primary processing method to render elastin supplementable is hydrolysis:

Hydrolyzed elastin / elastin peptides: Enzymatic or acid hydrolysis breaks the intact protein into smaller peptide fragments. Elastin is considered an excellent resource for obtaining antioxidant peptides due to unique amino acid composition. However, it is hardly soluble in water or in dilute acid or alkali. Enzymes capable of hydrolyzing elastin into soluble peptides are therefore preferred from typical commercial protease preparations.
Low molecular weight elastin peptides: After digestion, products can be filtered through a 10,000 Da molecular weight cut-off ultrafiltration membrane. The resulting supernatant is an elastin-derived composition comprised of peptides having a molecular weight of less than about 10,000 Da. Commercial marine elastin peptides such as VGPG Elastin® have been characterized with an average molecular weight of 582 Da, derived from Bonito fish (Katsuwonus pelamis).
Topical preparations: Hydrolyzed elastin is used in creams, serums, and masks. Products containing hydrolyzed elastin may help skin look younger. However, the elastin in these products usually comes from animal products, so vegetarians may not want to use these products.
Oral capsules and tablets: Elastin peptides are formulated as capsules or tablets for dietary supplementation. The test product in at least one clinical trial was administered daily in capsule form with a small volume of water every morning.

2. Traditional and Historical Use

Unlike botanicals with millennia-long documented use, elastin as an isolated ingredient is a product of modern biochemistry. However, the concept of consuming connective tissues rich in elastin has deep roots in traditional food cultures worldwide.

Elastin was used for cosmetic purposes long ago, and a bovine neck ligament was used as the raw material for cosmetics. The use of whole-animal foods — broths, gelatins, and organ meats made from ligaments, skin, tendons, and cartilage — has been a longstanding practice across many cultures. Bonito fish processing has been central to East Asian cuisine (particularly Japanese), and the connective tissues of fish were consumed both for nutrition and their perceived benefits to skin and vitality, long before the protein elastin was identified scientifically.

The formal isolation of elastin as a distinct protein occurred in the mid-twentieth century, and its use as a defined cosmetic and nutraceutical ingredient dates to the late twentieth century. Methods for producing elastin peptides using bovine ligament, bovine cardiac tube, bonito arterial ball, and porcine cardiac large artery as raw materials have been developed for achieving the purpose of beauty by oral administration and skin care. The transition from whole-tissue consumption to refined elastin peptide supplementation occurred primarily in Japan and East Asian markets during the 1990s and 2000s, driven by the nutricosmetic industry.

There are no documented traditional uses of elastin as a specifically extracted herbal or dietary medicine in classical Ayurvedic, Traditional Chinese Medicine, Greek, or European phytotherapeutic literature, as it is an animal-derived protein rather than a botanical ingredient. Its history as a supplement is therefore recent and predominantly commercial and scientific rather than traditional in the herbal sense.

3. Chemical Constituents and Mechanisms of Action

Amino Acid Composition

The main amino acids that make up elastin are proline, glycine, desmosine, and isodesmosine. They are grouped in short, repeated sequences of three to nine amino acids which create strong, flexible structures.

Like collagen protein, elastin contains about 30% glycine amino acid residues and is rich in proline. Elastin differs from collagen in that it contains very little hydroxyproline and no hydroxylysine. Elastin has a very high content of alanine and also contains two unique amino acids, isodesmosine and desmosine.

The amorphous component of elastic fibers consists of elastin, which is characterized by having 95% nonpolar amino acid residues and two unique lysine-derived amino acid residues, desmosine and isodesmosine.

Chemical analysis of extracted elastin shows a high amount of proline and glycine, low amount of hydroxyproline, methionine, and histidine.

Desmosine and Isodesmosine: Unique Crosslinking Amino Acids

Desmosine is an amino acid found uniquely in elastin, a protein found in connective tissue such as skin, lungs, and elastic arteries. Desmosine is a component of elastin and crosslinks with its isomer, isodesmosine, giving elasticity to the tissue.

Desmosine and its isomer isodesmosine are both composed of four lysine residues, allowing for bonding to multiple peptide chains. The four lysine groups combine to form a pyridinium nucleus, which can be reduced to neutralize positive charge associated, and increase the hydrophobicity.

These amino acids are believed to be responsible for elastin's ability to return to its original shape after stretching. More precisely, these unique amino acids, formed after amalgamation of three or four lysines, are responsible for crosslinking of adjacent tropoelastin molecules into the resilient elastin polymer, giving it the ability to return to its original shape after stretching.

Detection of desmosine in urine, plasma, or sputum samples can be a marker for elastin breakdown due to high elastase activity related to certain diseases.

Biosynthesis: From Tropoelastin to Mature Elastin

Elastin is synthesized from the precursor molecule tropoelastin. Many molecules of tropoelastin are linked together to form the larger elastin complex. Each molecule of tropoelastin has 36 domains arranged in a random coil. It has alternating hydrophobic and hydrophilic domains encoded by separate regions of the gene. The hydrophilic domains contain lysine residues that are important for crosslinking the tropoelastin molecules during the formation of the elastin fiber.

The polymer precursor, tropoelastin, is a 72-kDa hydrophobic protein that is soluble in salt solutions. Tropoelastin proteins bind to each other via covalent crosslinking beginning with the oxidative deamination of lysine residues by lysyl oxidase.

All crosslinks in elastin form spontaneously after oxidative deamination of specific lysine residues of tropoelastin by lysyl oxidase in the extracellular space. Allysine, a formed reactive aldehyde, reacts with lysine and/or another allysine to form polyfunctional crosslinks such as desmosine (DES) or isodesmosine (IDE).

In the arterial tissues, tropoelastin is produced and secreted into the extracellular space by smooth muscle cells; in other tissues it is produced in cells like fibroblast cells, and is also secreted into the extracellular space. In these cells, tropoelastin is synthesized by ribosomes in the rough endoplasmic reticulum and processed by the Golgi apparatus.

Elastin-Derived Peptides (Elastokines) and the Elastin Receptor Complex

When elastin degrades, it releases elastin-derived peptides (EDP) called elastokines. These peptides have effects on other cells, including endothelial cells, monocytes, and smooth muscle cells, through interactions with the elastin receptor complex. It is believed that EDPs play an important role in age-related vascular disease.

The best-characterized elastin-derived bioactive peptide is VGVAPG. Unlike insoluble fibrous elastin, elastin peptides promote cell proliferation, cell chemotaxis, angiogenesis, and protease release in a wide variety of normal cells. The effects promoted by VGVAPG, a sequence repeated six times in human tropoelastin, are the most documented. As a consequence, this peptide is regarded as the archetypal elastin peptide.

The elastin peptide VGVAPG is known to stimulate the proliferation of both fibroblasts and cancerous cells by binding to the elastin-binding receptor and activating the MEK/ERK signal transduction pathway.

The protein motif VGVAPG has been previously shown to stimulate proliferation and migration of monocytes, dermal fibroblasts, and smooth muscle cells through its interaction with the cell-surface elastin receptor. More recently, it has been shown that elastin peptides, liberated through proteolytic digestion of bovine ligamentum nuchae and containing elastin receptor ligand sequences (GXXPG), also induce elastogenesis in dermal fibroblasts through interaction with the elastin receptor.

In cell culture studies, elastin-derived peptides stimulated the growth of human skin fibroblasts at concentrations in the nanomolar range, across strains from different donors.

Mechanical Properties

Unlike other fibrous tissues like collagen, elastin is unique in that it may be stretched to over 150% of its original length, and can rapidly return to its original size and shape. This property of elastin provides tissues that incorporate it the ability to resume their original form after stretching due to, for example, blood flow, breathing, or bending.

The resiliency of skin is maintained by elastic fibers in the extracellular matrix (ECM). These ECM components are organized into a network of rope-like structures composed of two major components: an amorphous core, consisting of extensively crosslinked elastin which makes up the bulk (>90%) of the fiber; and the 10–12-nm microfibrils made up of several distinct glycoproteins.

4. Age-Related Decline and Pathophysiology

In aging skin, the marked decline of elastin and the degradation of elastic fibers results in a loss of elasticity and subsequently compromises the structural integrity of the skin.

Skin aging is characterized by different features including wrinkling, atrophy of the dermis, and loss of elasticity associated with damage to the extracellular matrix protein elastin. The aging process of skin elastin is influenced by both intrinsic (chronological aging) and extrinsic factors (sun exposure).

The body's elastin production slows down and eventually stops in adulthood and affects the functionality and properties of tissues and organs.

Aging tissues are associated with extracellular matrix (ECM) dysregulation, including loss of elastin. The extracellular matrix components, specifically the mix of elastin and collagen in the vessel wall, determine the passive mechanical properties of the large arteries. The elastic fibers last the lifetime of the organism, but are subject to proteolytic degradation and chemical alterations that change their mechanical properties.

Vascular disease in both the systemic and pulmonary circulation is frequently associated with altered biomechanical properties of blood vessels, attributable to changes in the ratio of collagen fibers to elastin fibers. Even though elastin is one of the most stable ECM proteins, it can be proteolytically degraded by serine and cysteine proteases (such as neutrophil and pancreatic elastases and cathepsins) and members of the matrix metalloprotease (MMP) family.

5. Scientific Evidence by Area of Use

5.1 Skin Aging, Elasticity, and Wrinkles

Overview: Elastin peptide shows promise as a therapeutic agent similar to collagen peptides. However, only a few clinical trials have evaluated the efficacy of oral elastin peptide supplementation.

Key Human Clinical Trials

VGPG Elastin® RCT (2024, PMC10938029): A randomized, double-blinded, placebo-controlled study was conducted to clinically evaluate the effect of elastin peptide intake on human skin. Healthy adult participants (N = 100) were randomly assigned to receive a test product containing 100 mg of Bonito elastin peptide (VGPG Elastin®) or placebo. All participants were Asian from Korea. The parameters of skin wrinkles, hydration, and brightening (melanin index) were measured at baseline and 4, 8, and 12 weeks after intervention. Oral consumption of Bonito elastin peptide reduced fine wrinkles, enhanced skin moisture, and decreased melanin index without significant adverse effects. No adverse effects were observed in any of the participants throughout the study period.

Fish elastin hydrolysate double-blind, placebo-controlled study: A double-blind, placebo-controlled study demonstrated that skin elasticity, wrinkles, blood flow, and subjective evaluation of skin conditions were improved by elastin hydrolysate ingestion. Compared with the start of trial, skin elasticity and most parameters of subjective evaluation of skin conditions significantly improved after ingestion of elastin hydrolysate. In the placebo group, blood flow significantly decreased 4 weeks after the start of trial. The dose of approximately 400 mg elastin hydrolysate per day administered for 13 months did not result in clinically important problems in a prior supporting study.

Elastin-inducing composition (amino acids, copper, hyaluronic acid) — MDPI Cosmetics, 2022: A small open single-center study involved four treatments performed on five subjects at 1-week intervals with Elastic Lab®. As a result, eye wrinkles, skin moisture, inner elasticity, thickness, and density were improved 1 week after the last treatment in all subjects compared to the baseline. Among all evaluation items, skin elasticity, thickness, and density showed significant increases. This study is limited by the very small sample size (n=5) and lack of a control group; results should be considered preliminary.

Elastin-derived trifunctional peptide (TFP) topical study (PMC10408523): Twenty-two volunteers applied a TFP-based cream on one hemi-face and a placebo-based cream on the other hemi-face, twice a day during 28 days. Each patient was her own control, which greatly strengthens the statistical results. Using a cutometer device, an improvement of skin firmness and viscoelasticity was demonstrated after TFP treatment after 28 days, as compared to placebo treatment. This study's split-face design is methodologically appropriate but the sample size is modest.

In vitro mechanistic evidence: Elastin peptides enhance elastin synthesis and fibroblast proliferation, reduce epidermal thickness in photodamaged skin, and attenuate UV-induced cellular damage. Multiple in vitro and in vivo studies have suggested that elastin peptides improve the skin's biophysical properties, enhancing the proliferation of fibroblasts and elastin synthesis, resulting in anti-aging properties.

Evidence strength assessment: Supplements may help the body generate more elastin, but there isn't enough scientific research to draw definite conclusions. There isn't enough research to conclude that herbal supplements increase the amount of elastin in the skin. The available human RCT evidence is preliminary but promising, and restricted primarily to East Asian populations in a small number of trials.

5.2 Vascular Health and Arterial Stiffness

Data from animal models show that elastin amounts are inversely proportional to arterial stiffness and blood pressure. Large artery stiffness, as measured by pulse wave velocity (PWV), is correlated with high blood pressure and may be a causative factor in essential hypertension. The extracellular matrix components, specifically the mix of elastin and collagen in the vessel wall, determine the passive mechanical properties of the large arteries.

Increased stiffness of pulmonary arteries from patients with left heart disease correlates with impaired pulmonary hemodynamics. Extracellular matrix remodeling in the pulmonary arterial wall, manifested by dysregulated genes implicated in elastin degradation, precedes the onset of pulmonary hypertension. The resulting degradation of elastic fibers is paralleled by an accumulation of fibrillar collagens.

Hydrolyzed fish elastin has been recognized as a promising food ingredient for improving skin and blood vessel conditions. A high-quality elastin supplement made with marine elastin peptides can support skin elasticity and beauty, and also promotes vascular health. However, this claim is largely based on in vitro and animal-model data. Direct evidence from RCTs in humans specifically for vascular outcomes using oral elastin supplementation is limited as of the available literature.

The line of evidence for elastin supplementation and vascular benefit is somewhat tenuous, since key studies were carried out in animal models of a genetic condition in which elastin levels are abnormally low, and with a focus on young patients rather than older individuals.

Evidence strength assessment: The vascular role of elastin as a structural protein is well-established by basic science. The evidence that oral supplementation with elastin peptides meaningfully improves arterial mechanics in healthy adults is currently preclinical and preliminary. Human RCT data for vascular endpoints are lacking.

5.3 Antioxidant Activity

Elastin is considered an excellent resource for obtaining antioxidant peptides due to its unique amino acid composition. The amino acid content related to antioxidant activity has reached 68 mg/100 mg in enzymatically processed bovine elastin peptides, so it has extremely high free radical clearance. This is primarily demonstrated in in vitro assays; clinical evidence for systemic antioxidant effects in humans from oral elastin supplementation has not been firmly established.

5.4 Wound Healing and Cellular Senescence

Tropoelastin, the soluble elastin precursor, is not only a marker of young mesenchymal stromal cells (MSCs) but also actively preserves cell fitness and delays senescence during replicative aging. MSCs briefly exposed to tropoelastin exhibit upregulation of proliferative genes and concurrent downregulation of senescence genes. The seno-protective benefits of tropoelastin persist during continuous, long-term MSC culture, and significantly extend the MSC replicative lifespan. These findings are from laboratory cell culture models, not human clinical trials.

5.5 Pulmonary / Respiratory Health

Elastin from bovine neck ligament has been used in studies of chronic obstructive pulmonary disease (COPD). It may be used to investigate why there is a lack of repair for these proteins in patients with COPD. Crosslinks in elastin may resist elastolysis, and contribute to the biomechanical properties of this macromolecule that are essential for normal arterial function and are often deranged in diseases such as hypertension, arteriosclerosis, atherosclerosis, certain arteritides, and aneurysm formation. Clinical intervention evidence for elastin supplementation in lung disease is absent in the current literature.

6. Body Systems and Health Areas Associated with Elastin

Integumentary system (skin, hair): Skin aging is characterized by different features including wrinkling, atrophy of the dermis, and loss of elasticity associated with damage to the extracellular matrix protein elastin.
Cardiovascular system (arteries, heart): Elastin is one of the major structural components of the extracellular matrix of the blood vessel wall. It is especially important in blood vessels, where it comprises about 50% of the dry tissue weight.
Pulmonary system (lungs): Elastic fibers, of which elastin is the core component, enable connective tissues such as those of the skin and lungs to function.
Musculoskeletal system (tendons, ligaments): Elastin lends elasticity and resilience to tissues including tendons and ligaments.
Urological system (bladder): Elastin is a major component of the bladder, which requires stretchiness.
Cellular aging: Aging tissues are associated with extracellular matrix dysregulation, including loss of elastin.

7. Dosage Forms and Dosages Reported in Studies

The following dosages are drawn exclusively from published scientific studies and should not be interpreted as recommended doses:

100 mg/day (oral capsule): A randomized, double-blinded, placebo-controlled study evaluated the effect of elastin peptide intake on human skin with 100 mg of Bonito elastin peptide (VGPG Elastin®) in N=100 healthy adult participants.
~400 mg/day (oral) for 13 months: A dose of approximately 400 mg elastin hydrolysate per day administered for 13 months did not result in clinically important problems in a prior study cited in the Shiratsuchi et al. (2015) fish elastin publication.
Dose range reported across products: Effective doses in studies range from 50 mg to 250 mg daily.
Molecular weight of supplemental peptides: Optimal elastin peptides for intestinal absorption should be low-molecular-weight (<5 kDa). The VGPG Elastin® product used in clinical trials had a total average molecular weight of 582 Da.
Topical (trifunctional peptide cream): In a clinical study, volunteers applied a TFP-based cream on one hemi-face and a placebo-based cream on the other hemi-face, twice a day during 28 days.

8. Safety Considerations

General Tolerability

No adverse effects were observed in any of the 100 participants throughout the study period in the Bonito elastin peptide RCT. Elastin is renowned for its high biocompatibility and excellent skin tolerance. Available clinical studies report no notable side effects, nor any irritation or photosensitization reactions.

Cytotoxicity

The non-toxic effect of water-soluble extracted elastin was observed at a concentration lower than 0.5 mg/mL in MTT cytotoxicity assays.

Allergen Considerations

The primary sources of supplemental elastin — bovine tissues and marine fish — carry relevant allergen implications:

Fish-derived elastin: Marine-sourced elastin has a lower risk of mammalian contaminants and is preferred by pescatarians, but carries possible seafood allergy interactions.
Bovine-derived elastin: Bovine-derived elastin is widely available and cost-effective, but is not suitable for vegetarians or those avoiding beef and may carry potential allergen concerns.
Porcine-derived elastin: Porcine-sourced elastin is structurally similar to human elastin and used in some medical-grade biomaterials, but may be restricted by religious dietary considerations such as halal or kosher requirements.

BSE / Disease Transmission Concerns (Bovine Source)

With the discovery of BSE (bovine spongiform encephalopathy) and poultry infectious diseases, the safety of bovine-sourced elastin material has been questioned, prompting the search for alternative raw materials.

Bioactive Peptide Safety Considerations

Elastin-derived peptides (EDPs) are believed to play an important role in age-related vascular disease. Accumulations of EDPs have been shown to promote hyperglycemia and insulin resistance in mice. This consideration relates primarily to endogenously generated EDPs from elastin degradation in disease states, not to supplemental doses, but underscores the biological activity of these peptides and the need for further study of their systemic effects at supplemental doses.

Limitations of Current Safety Data

No large-scale, long-term (>12 months) safety studies of oral elastin peptide supplementation have been published in the peer-reviewed literature available to this review. The longest duration noted in the clinical literature is approximately 13 months at ~400 mg/day without clinically important problems. Formal drug interaction data for elastin supplements are not established in the published literature.

References

Condiciones de Salud

Condiciones de salud que elastina puede ayudar a apoyar.

Ira (excesiva)Científico
Elastin is the elastic protein of connective tissue (skin, arteries, lungs, ligaments) responsible for tissue recoil after deformation. Elastin hydrolysate supplementation has been studied for skin connective tissue elasticity. Elastin synthesis depends on copper-dependent lysyl oxidase for cross-linking, and elastin-derived peptides have been shown to stimulate fibroblast activity.
Costra lácteaCientífico
Elastin is the structural protein providing skin its elasticity and resilience, degraded progressively with aging and UV exposure. Green tea polyphenols have been shown to raise dermal elastin content in clinical studies. Multiple anti-aging interventions list elastin preservation as a mechanistic endpoint, and elastin degradation is identified as a central mechanism of skin aging in systematic reviews.

Sistemas Corporales

Sistemas corporales que elastina puede ayudar a apoyar.

No hay sistemas corporales disponibles.