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The Benefits of Using hydrolyzed elastin factory

Jun. 24, 2024

Elastin: Understanding Its Structure, Function & Supplements

What is elastin?

Elastin is one of the most abundant proteins found in the human body. Similar to a rubber band, it possesses the remarkable ability to stretch and recoil. This protein plays a pivotal role in various tissues that require flexibility, such as the lungs, bladder, large blood vessels, and certain ligaments. Additionally, it exists in smaller quantities within the skin and ear cartilage.

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Is elastin a type of collagen?

No, elastin and collagen are not the same; they are separate proteins often mistaken for one another. Histologists, who examine tissue at a microscopic level, employ specific dyes to highlight these proteins within body tissues, revealing their distinct characteristics. Structures abundant in elastin are typically stained brown or purple.

Collagen mainly provides structural support, strength, and stability to the body, while elastin is fundamentally responsible for elasticity, exhibiting approximately 1,000 times more stretchiness than collagen.

How is elastin synthesized?

Elastin is formed when multiple molecules of a large, flexible structure known as tropoelastin combine together.

Significant effects of dietary supplements based on ...

Associated Data

Data Availability Statement

The datasets utilized and/or assessed during the ongoing study are obtainable from the corresponding author upon a reasonable request.

Abstract

Aging represents a complex, multifaceted process that includes a decline in collagen and elastin levels. Collagen is prominently found in the dermis layer, contributing to the skin's strength, hydration, and mechanical properties. As a widely available substance derived from various animal sources, collagen is extensively utilized in the cosmetic and pharmaceutical industries to treat signs of premature aging. Bioactive peptides, particularly hydrolyzed collagen, are among the most sought-after ingredients for creating nutraceuticals, which are food substances that possess specific physiological effects. Numerous studies have illustrated that peptides resulting from the ingestion of hydrolyzed collagen travel into the bloodstream and exhibit chemotactic properties for skin fibroblasts, thus assisting in the skin restoration process. This minireview aims to update the conversation surrounding the use of hydrolyzed collagen for skincare.

Keywords:

hydrolyzed collagen, wrinkles, skin, peptide, nutraceuticals

1. Introduction

Visible signs of aging generally start in the second decade of life, manifesting numerous significant changes over time. While initial signs may be subtle, more pronounced structural and functional transformations become apparent by the third decade. The skin serves as a protective barrier against environmental threats and fulfills multiple essential roles in sensory and defensive functions (1). Due to the skin's large exposure to external elements, it frequently endures alterations that can affect both appearance and overall health (3). As a response, the food, cosmetic, and pharmaceutical industries focus on developing innovative and effective products to prevent, delay, or minimize signs of aging while promoting skin health (4).

Nutraceuticals, a blend of nutrition and pharmaceuticals, encompass foods, food ingredients, or cosmetic products that boast defined physiological effects (5) without adverse effects, intending to enhance health (6). Given population growth and increasingly varied dietary preferences, the demand for nutraceuticals has surged. Plant-based nutraceuticals are rich in antioxidants, polyunsaturated fatty acids, as well as prebiotics and probiotics. Recently, addressing collagen deficiencies has involved utilizing bioactive peptides derived from the enzymatic hydrolysis of food proteins. Bioactive peptides, like collagen hydrolyzate, are critical in creating nutraceuticals. Given that collagen constitutes roughly 30% of the body's protein mass, it is vital in maintaining the structure of various tissue types, adding rigidity and vitality to bones and skin.

The extracellular matrix primarily comprises collagen proteoglycans. Skin hydration, resistance, and molecular filtration hinge on proteoglycans, which also affect cellular behavior or interactions between cells and their matrix. Collagen proteoglycans, being significant sources of cytokines and growth factors, may encounter changes in expression or structure, profoundly influencing tissue homeostasis (8).

As collagen and elastin reserves wane with age, compounded by sun exposure, the cosmetics industry is inspired to discover solutions for rejuvenating facial and neck skin appearances (9). Collagen serves as a vital component in food or pharmaceutical products, impacting connective tissues found in skin, tendons, ligaments, and teeth. Research has demonstrated the positive influence of collagen peptides on skin elasticity, effectively reducing wrinkles and increasing collagen deposition within the dermis across various clinical studies (10-15). To effectively penetrate the deeper skin layers, hydrolyzed collagen must first traverse the bloodstream while overcoming the intestinal barrier (16).

Table I

ProductType of productTherapeutic effectAuthors/Refs.VERISOL® (GELITA AG)Bioactive collagen peptides (BCP)-collagen peptides from porcine skin type I collagenDecrease in the degree of cellulite and reduced skin wavinessSchunck et al (10)VERISOL® (GELITA AG)Bioactive I collagenIncrease nail growthHexsel et al (11)NutraceuticalsMarine collagen peptides (MCPs) - fish skin MCPs combined with plant-derived skin-targeting antioxidants (AO) (coenzyme Q10 + grape-skin extract + luteolin + selenium)Improve skin elasticity, sebum production, and dermal ultrasonic markersDe Luca et al (12)Oral supplementContent (per tablet): marine protein (105 mg), vitamin C (27 mg), grape seed extract (13.75 mg), zinc (2 mg), and tomato extract (14.38 mg)Improve skin aging in menCosta et al (13)Marine collagenFish collagen hydrolysates (FCH)Anti-aging effectJe et al (14)BioCell Collagen® (BCC; BioCell Technology, LLC Newport Beach, CA, USA)Chicken sternal articular cartilage (hydrolyzed collagen type II and low molecular-weight hyaluronic acid and chondroitin sulfate)Reduce skin dryness and wrinklesSchwartz and Park (15)Open in a separate window

2. Skin aging - natural occurrence and external triggers

The epidermis, composed of proliferative basal cells, and the dermis, made up of keratinocytes, represent the skin's primary structures. Dermal fibroblasts are responsible for producing elastin and collagen types I and III, in addition to other extracellular matrix proteins (17). The dermis, supplied with vital nutrients through blood vessels, offers essential structural support to the epidermis; hence, maintaining dermal integrity is critical for optimal skin cell function. Skin aging can result from a combination of intrinsic (chronological) factors or extrinsic triggers related to environmental exposures (18-20). Changes to the dermal structure, extracellular matrix modifications, elevated inflammatory markers, and reduced blood circulation contribute to skin aging.

The aging process is intertwined with cumulative exposure to harmful stimuli, such as hemodynamic stress and oxidized lipids, associated with impaired angiogenesis and endothelial dysfunction (21). Naturally, fibroblasts in aged skin synthesize reduced amounts of collagen, while ultraviolet radiation generates reactive oxygen species that activate matrix metalloproteinases, affecting collagen production through neocolagenesis. This shift leads to an imbalance between collagen types I and III, resulting in the degradation of the extracellular matrix and photoaging (1). With a decrease in collagen levels and the occurrence of elastosis, which triggers disorganized elastin accumulation in the dermis, skin atrophy becomes evident, leading to an aged appearance (22). The elastosis phenomenon is especially prevalent in sun-exposed areas of the body. As a result of this process, fibroblast activity diminishes, and mechanical tension decreases, contributing to the breakdown of existing collagen fibers. Fine lines arise as a consequence of decreased collagen synthesis and increased collagen breakdown within the dermis (1).

The dermis is also adversely affected in individuals who smoke, while persistent stress disrupts the cortisol/corticosterone rhythm, altering collagen synthesis and degradation. Following prolonged sun exposure, aging skin tends to become drier, exhibit laxity, and develop wrinkles. During the aging process, deep wrinkles and increasing laxity become increasingly pronounced (16).

3. Sources of collagen peptides

The formation of gelatin occurs when collagen molecules denature irreversibly. To halt this denaturation process, either chemical or thermal treatment can be applied. Collagen denaturation via heat is implemented in various beauty treatments and medical techniques including orthopedics, plastic surgery, dental, or ophthalmological interventions, as well as in the pharmaceutical or food industries. Gelatin is widely utilized in the food industry due to the diverse bioactivities associated with collagen peptides, particularly their high biocompatibility and bioavailability (23).

Researchers continuously seek new collagen sources. Currently, the hydrolyzed collagen and gelatin in use are predominantly derived from porcine or bovine type I collagen. Contrary to gelatin, hydrolyzed collagen is easier to digest, as it dissolves in water or brine and presents excellent absorption qualities. Studies indicate that an animal's age impacts collagen solubility, with older animals yielding less soluble collagen compared to younger ones. Innovations in collagen extraction techniques have been developed while considering the source and solubility of collagen (24). Good quality gelatin is sourced primarily from bovine bone, whose peptides contribute positively to bone metabolism. However, concerns regarding bovine spongiform encephalopathy limit the use of this collagen source, urging the industry to investigate alternative collagen sources. Collagen can be obtained from both animal and vegan sources, including algae and marine organisms (3,25).

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In the pharmaceutical, cosmetic, and food sectors, marine collagen is increasingly favored (26). Collagen and other bioactive substances can be extracted from various marine organisms. Notable marine sources for collagen extraction include jellyfish, sponges, sea urchins, and octopus, as well as fish and marine mammals. Collagen derived from marine sources is particularly appealing due to its superior absorption, lower molecular weight, diminished inflammatory reactions, and reduced contamination potential when compared to animal collagen (27). Marine collagen maintains biocompatibility and amino acid profiles akin to those of porcine or bovine collagen. Regenerative medicine relies heavily on tissue engineering for replacing or restoring damaged tissues, with collagen serving as the ideal biomaterial by facilitating proper cell migration and extracellular matrix-cell interactions essential for tissue regeneration (26).

Within the cosmetics industry, marine collagen shows promise in treating wounds, burns, and ulcers, as well as providing antimicrobial benefits and preventing moisture loss from compromised tissues (26).

Given the plentiful marine collagen sources, the peptides obtained exhibit the unique ability to traverse the bloodstream intact following gastrointestinal digestion, coupled with their healing properties, making them a preferred choice for industry. However, it is important to remain cautious about potential heavy metal contamination (27-29).

4. Clinical evidence for the beneficial roles of collagen-based products for skin care

Hydrolyzed collagen has been a staple in dietary supplements and the pharmaceutical industry due to numerous clinical trials showcasing its benefits, which include bioavailability, rapid gastrointestinal absorption, and subsequent distribution in the bloodstream as small peptides. Importantly, these peptides accumulate in the skin within 96 hours post-consumption. Upon ingestion, proline and hydroxyproline have been detected in the bloodstream. With low molecular weights and rapid absorption rates, collagen peptides distribute to various tissues, including the skin, where they showcase their benefits (30,31).

Numerous in vitro studies investigated the antioxidant capacity of collagen peptides, revealing that peptides entering the bloodstream post-hydrolysis possess chemotactic effects that draw skin fibroblasts, promoting their migration and proliferation (30,31). Activated fibroblasts influence the production of collagen, hyaluronic acid, and elastin. After ingestion, collagen peptides can persist in the dermis for up to 14 days, safeguarding skin from UV damage and augmenting moisture retention while aiding in the restoration of endogenous elastin and collagen fibers. Following oral consumption of bovine hydrolyzed collagen, clinical improvements associated with aging skin, including elevated cutaneous collagen levels and shifts in collagen type ratios, have been reported (32). Currently, numerous commercial products exist in the field of food supplements and cosmetics that leverage collagen and its positive clinical findings.

The Pure Gold Collagen® Food Supplement (Minerva Research Labs Ltd.) is an example of a type I hydrolyzed collagen product derived from fish, incorporating low molecular weight hyaluronic acid and an assortment of vitamins and minerals. In a study conducted by Borumand and Sibilla, participants consuming 50 ml of Pure Gold Collagen daily for 60 days experienced reduced skin dryness, a decrease in the depth of wrinkles, and firmer skin with enhanced collagen density after 12 weeks (33).

Another product, BioCell Collagen® (BCC; BioCell Technology, LLC), consists of type II hydrolyzed collagen, low molecular weight hyaluronic acid, and chondroitin sulfate. A study by Schwartz and Park (15) surveyed 26 healthy women who were administered 1 g of BioCell Collagen® daily over 12 weeks, demonstrating significant improvements in skin dryness and wrinkle reduction. Laboratory analyses showed increased hemoglobin and dermal collagen content following six weeks of BioCell Collagen® consumption. Each BCC capsule features 300 mg of hydrolyzed collagen sourced from chicken cartilage, 100 mg of depolymerized chondroitin sulfate, and 50 mg of hyaluronic acid. Participants took two capsules daily for 12 weeks, with assessments revealing notable skin improvements in texture, tone, and pigmentation (15).

Research indicates that the administration of hydrolyzed collagen from animal sources (chicken, pig) led to an uptick in hydroxyproline levels in participant blood post 12 hours of fasting, peaking at two hours post-consumption and decreasing four hours afterward (15).

The VERISOL® product (GELITA AG), which is type I porcine hydrolyzed collagen, was evaluated in a study involving 69 healthy women who were given daily doses ranging from 2.5-5 g. After four weeks, older participants showed marked increases in skin elasticity, effects that persisted after discontinuation of the treatment, affirming the beneficial impact of hydrolyzed collagen regardless of dosage administered (2.5 or 5 g) (18).

Further investigation into nutritional products combining collagen peptides and antioxidants has revealed enhanced skin elasticity after 90 days of consumption. Bioactive peptides in the dermis exert dual actions: on one side, free amino acids promote collagen fiber formation, while concurrently, these peptides interact with fibroblast membrane receptors to stimulate the production of hyaluronic acid, collagen, and elastin (23).

Substantial scientific evidence supports the notion that supplementation with vitamins C or E contributes to improved skin appearance through mechanisms like attracting water molecules (enhancing hydration), scavenging free radicals, or diminishing inflammation. Vitamin C also plays a crucial co-factor role in collagen biosynthesis. One study assessed a hydrolyzed collagen product in a cohort of 18 menopausal women. This product, enriched with vitamin C and hyaluronic acid, led to pronounced improvements in skin appearance and significantly decreased wrinkle depth following nine weeks of administration. Additionally, increased hydration levels, reduced moisture loss, and enhancements in skin elasticity and dryness were documented. Daily oral supplementation with 1 g of this hydrolyzed collagen type led to marked reductions in wrinkles and improvements in skin elasticity and dryness over a 12-week period (33).

Campos et al. (34) conducted an investigation involving a synergistic combination of amino acids (hydrolyzed collagen peptides: glycine, proline, and hydroxyproline), accompanied by water-soluble vitamins (A, C) and liposoluble vitamins (E) along with zinc. Efficacy was evaluated through biophysical assessments and skin imaging techniques, enrolling 60 healthy women who each received a daily dose of 10 g of the trial product over three months. End-of-study evaluations showed visibly diminished wrinkles and enlarged pores, improved skin elasticity, and enhanced dermal structure. The findings indicated that a hydrolyzed collagen product fortified with vitamins and zinc significantly outperformed in addressing aging-related skin conditions. Eventually, by integrating three distinct amino acids with vitamins and zinc to exert antioxidant effects, the study concluded that protective mechanisms against reactive oxygen species – which trigger oxidative stress – were ensured, thereby influencing both the inflammatory response and collagen synthesis processes (35,36). Numerous studies outline the positive effects of hydrolyzed collagen on various skin conditions. While extensive documentation exists regarding its utility across a range of dermatological ailments, further research is warranted to explore its applications for other skin conditions (e.g., topical applications for hyperpigmented, velvety plaques in Acanthosis nigricans patients) (38).

5. Conclusions

Aging skin is closely interconnected with changes in molecular metabolism and modifications in the extracellular matrix within the dermis, resulting in altered structures and functionalities of collagen fibers, elastin, and hyaluronic acid. Clinical manifestations of this aging process comprise increased skin laxity, fragility, dryness, and wrinkle formation. Evidence substantiates the assertion that daily intake of hydrolyzed collagen, sourced from various mediums, can confer multifaceted benefits to human health, ranging from alleviating joint pain to bolstering skin vitality. Hydrolyzed collagen can be sourced from an array of sources including bovine, porcine, marine organisms, chicken skin, and fish cartilage, with compatibility for vitamin and nutrient supplements. In light of BSE outbreaks in cattle, collagen derived from marine sources continues to emerge as a highly valued alternative. The intake of supplements featuring hydrolyzed collagen can yield numerous benefits, including the effective deceleration of skin aging.

Acknowledgements

We extend our gratitude to Dr. Ana-Maria Enciu for her valuable assistance during the revision of this manuscript.

Funding

This investigation was financed through grant COP A 1.2.3., ID: P_40_197/ (Ctr. 52// component project 259) with the support of the Ministry of Research and Innovation in Romania under Program 1 - The Improvement of the National System of Research and Development, Subprogram 1.2 - Institutional Excellence - Projects of Excellence Funding in RDI, Contract No. 7PFE/16.10.

Availability of data and materials

The datasets employed and/or analyzed during the current study are available from the corresponding author upon reasonable request.

Authors' contributions

MAL, GGP, MCC, RA, CT: contributed equally to data collection, manuscript preparation, and critical manuscript revision for substantial intellectual content. All authors reviewed and approved the final manuscript.

Ethics approval and consent to participate

Not applicable.

Patient consent for publication

Not applicable.

Competing interests

The authors declare that there are no competing interests.

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