Elastin is a highly elastic protein found in the connective tissue of the skin, lungs, arteries (1), and several other elastic tissues in the body (2). It allows many tissues in the body to resume their shape after stretching or contracting. Its primary function is to allow tissues to "snap back" to their original shape, providing skin with elasticity and the ability to return to its original position when poked or pinched.

Origin and Synthesis

Elastin is synthesized from its precursor, tropoelastin. Fibroblast cells in the dermis produce this precursor, which then assembles into elastin fibers. This assembly happens alongside another protein called fibrillin, which forms the scaffold for elastin deposition. The cross-linking of elastin fibers gives them their unique, rubbery properties.

Elastin in Aging

Over time, and due to various factors like UV radiation exposure, environmental pollutants, and natural aging, the amount of elastin and its functionality decreases in the skin. This reduction leads to the loss of skin elasticity and the formation of wrinkles.

Clinical and Cosmetic Relevance

Many skincare products claim to boost elastin production, but the ability of topical treatments to meaningfully increase elastin in the skin remains a topic of research and debate. Nevertheless, ingredients like retinoids are believed to promote the synthesis of elastin and other essential skin matrix components.Some procedures, such as laser treatments, radiofrequency, and ultrasound, might stimulate the production of elastin to some extent, leading to skin tightening and wrinkle reduction.

Elastin in Medicine

Beyond its role in cosmetics, elastin's unique properties make it an area of interest in regenerative medicine and tissue engineering (3). Scientists are researching ways to utilize elastin in developing artificial organs and other medical applications (4).

Dietary Sources and Supplements

While the body produces elastin, certain foods rich in amino acids, like lysine and proline, can support its production. These amino acids are found in protein-rich foods like lean meats, cheese, nuts, legumes, and soy. However, direct dietary sources of elastin (like eating elastin-rich foods) may not directly boost skin elastin but might provide the necessary building blocks for its synthesis.

Allergies and Sensitivities

Elastin is a natural component of the body, and allergic reactions are rare. However, when used in cosmetic procedures or products, there's always a small risk of sensitivity or allergic reactions. As always, it's recommended to patch-test products and discuss any concerns with a dermatologist.

In summary, elastin plays a crucial role in maintaining skin's elasticity and overall youthful appearance. However, its synthesis and functionality decrease over time, leading to the common signs of aging like wrinkles and sagging skin.

It appears in the form of a white powder. 

Cosmetics

• Skin conditioning agent. It is the mainstay of topical skin treatment as it has the function of restoring, increasing or improving skin tolerance to external factors, including melanocyte tolerance. The most important function of the conditioning agent is to prevent skin dehydration, but the subject is rather complex and involves emollients and humectants that can be added in the formulation.
• Soothing. Ingredient with the task of restoring moisture to the skin, helping in the healing process of irritation, inflammation and skin disorders.

CAS   9007-58-3

EC number   232-701-4

Commercial Applications

Cosmetic and Skin Care Products. Elastin amino acids are often used in serums, lotions, and creams to promote skin elasticity and combat signs of aging.

Hair Products. Used in conditioners and hair treatments to enhance hair's elasticity and resilience.

Dietary Supplements. Some products promote skin and joint health.

Medical Applications

Dermatological Treatments. They may be used in treatments to enhance skin elasticity, reduce wrinkles, and address elastosis injuries.

Biomedical Research. Elastin amino acids are being studied for their potential applications in tissue regeneration and regenerative medicine.

References_____________________________________________________________________

(1) Lin CJ, Cocciolone AJ, Wagenseil JE. Elastin, arterial mechanics, and stenosis. Am J Physiol Cell Physiol. 2022 May 1;322(5):C875-C886. doi: 10.1152/ajpcell.00448.2021. 

Abstract. Elastin is a long-lived extracellular matrix protein that is organized into elastic fibers that provide elasticity to the arterial wall, allowing stretch and recoil with each cardiac cycle. By forming lamellar units with smooth muscle cells, elastic fibers transduce tissue-level mechanics to cell-level changes through mechanobiological signaling. Altered amounts or assembly of elastic fibers leads to changes in arterial structure and mechanical behavior that compromise cardiovascular function. In particular, genetic mutations in the elastin gene (ELN) that reduce elastin protein levels are associated with focal arterial stenosis, or narrowing of the arterial lumen, such as that seen in supravalvular aortic stenosis and Williams-Beuren syndrome. Global reduction of Eln levels in mice allows investigation of the tissue- and cell-level arterial mechanical changes and associated alterations in smooth muscle cell phenotype that may contribute to stenosis formation. A loxP-floxed Eln allele in mice highlights cell type- and developmental origin-specific mechanobiological effects of reduced elastin amounts. Eln production is required in distinct cell types for elastic layer formation in different parts of the mouse vasculature. Eln deletion in smooth muscle cells from different developmental origins in the ascending aorta leads to characteristic patterns of vascular stenosis and neointima. Dissecting the mechanobiological signaling associated with local Eln depletion and subsequent smooth muscle cell response may help develop new therapeutic interventions for elastin-related diseases.

(2) Daamen WF, Veerkamp JH, van Hest JC, van Kuppevelt TH. Elastin as a biomaterial for tissue engineering. Biomaterials. 2007 Oct;28(30):4378-98. doi: 10.1016/j.biomaterials.2007.06.025.

Abstract. Biomaterials based upon elastin and elastin-derived molecules are increasingly investigated for their application in tissue engineering. This interest is fuelled by the remarkable properties of this structural protein, such as elasticity, self-assembly, long-term stability, and biological activity. Elastin can be applied in biomaterials in various forms, including insoluble elastin fibres, hydrolysed soluble elastin, recombinant tropoelastin (fragments), repeats of synthetic peptide sequences and as block copolymers of elastin, possibly in combination with other (bio)polymers. In this review, the properties of various elastin-based materials will be discussed, and their current and future applications evaluated.

(3) Saitow CB, Wise SG, Weiss AS, Castellot JJ, Kaplan DL. Elastin biology and tissue engineering with adult cells. Biomol Concepts. 2013 Apr;4(2):173-85. doi: 10.1515/bmc-2012-0040. 

Abstract. The inability of adult cells to produce well-organized, robust elastic fibers has long been a barrier to the successful engineering of certain tissues. In this review, we focus primarily on elastin with respect to tissue-engineered vascular substitutes. To understand elastin regulation during normal development, we describe the role of various elastic fiber accessory proteins. Biochemical pathways regulating expression of the elastin gene are addressed, with particular focus on tissue-engineering research using adult-derived cells.

(4) Rodríguez-Cabello JC, Prieto S, Reguera J, Arias FJ, Ribeiro A. Biofunctional design of elastin-like polymers for advanced applications in nanobiotechnology. J Biomater Sci Polym Ed. 2007;18(3):269-86. doi: 10.1163/156856207779996904. 

Abstract. Elastin-like recombinant protein polymers are a new family of polymers which are captivating the attention of a broad audience ranging from nanotechnologists to biomaterials and more basic scientists. This is due to the extraordinary confluence of different properties shown by this kind of material that are not found together in other polymer systems. Elastin-like polymers are extraordinarily biocompatible, acutely smart and show uncommon self-assembling capabilities. Additionally, they are highly versatile, since these properties can be tuned and expanded in many different ways by substituting the amino acids of the dominating repeating peptide or by inserting, in the polymer architecture, (bio)functional domains extracted from other natural proteins or de novo designs. Recently, the potential shown by elastin-like polymers has, in addition, been boosted and amplified by the use of recombinant DNA technologies. By this means, complex molecular designs and extreme control over the amino-acid sequence can be attained. Nowadays, the degree of complexity and control shown by the elastin-like protein polymers is well beyond the reach of even the most advanced polymer chemistry technologies. This will open new possibilities in obtaining synthetic advanced bio- and nanomaterials. This review explores the present development of elastin-like protein polymers, with a particular emphasis for biomedical uses, along with some future directions that this field will likely explore in the near future.