Figure - available from: Plastic and Aesthetic Research
This content is subject to copyright. Terms and conditions apply.
The production of collagen fibres in the dermis. The fibroblast secretes the procollagen fibre into the extracellular matrix, where they form larger collagen bundles. Elastin is also secreted and assembled into the collagen-based macromolecular structure. (By permission of MINERVA Research Labs Ltd - London)
Source publication
Collagen-based supplements have become a keystone in the management of the ageing process, with proven ability to repair skin damage, bestowing a youthful and healthy appearance sought in the pursuit of beauty. Collagen is an essential scaffold protein that gives smoothness and elasticity to skin, but its production declines with age. Finding ways...
Citations
... However, with increasing age, the concentration of HA in the skin diminishes considerably. These changes, along with declining collagen levels from the mid-30s, lead to a reduced dermal volume, elasticity, firmness, and hydration and manifest externally as sagging, wrinkles, and a rough texture to the skin [33,34]. ...
Collagen dietary supplements are becoming increasingly popular as a means to reduce signs of skin ageing. The objective of this three-way, randomised, placebo-controlled, double-blind study was to examine and contrast the effects of dietary supplementation with a daily dose of 5 g hydrolysed collagen with 80 mg of vitamin C (CP product) and their combination with 30 mg of hyaluronic acid (CPHA product) over 16 weeks. Validated methods were utilised for the objective evaluation of skin parameters. In total, 87 subjects (women, 40–65 years) completed the entire trial, distributed across the groups as follows: placebo group (n = 29), CPHA group (n = 28), and CP group (n = 30). The results showed beneficial effects of both test products, with notable enhancements in dermis density, skin texture, and a reduction in the severity of wrinkles. In contrast, the administration of either of the products did not yield any significant impacts on skin elasticity or hydration. Observation of the investigated skin parameters did not show superior effects of the addition of hyaluronic acid (HA) to collagen. Therefore, the ability of supplementation with HA to improve the effects on investigated skin parameters beyond the supplementation of collagen alone cannot be confirmed.
... The skin is the largest organ of the human body, with a surface area of 1.5-2 m 2 [1]; it is composed of three layers: epidermis, dermis and hypodermis, each with well-defined roles [1][2][3]. Collagen is the main structural protein in the dermis (75% of total dry weight [4]) and is responsible for most of its mechanically supportive function [5,6]. Another critical component of the dermis is elastin, which provides resilience and elasticity to the skin [4,5,7]. ...
... Collagen is the main structural protein in the dermis (75% of total dry weight [4]) and is responsible for most of its mechanically supportive function [5,6]. Another critical component of the dermis is elastin, which provides resilience and elasticity to the skin [4,5,7]. ...
... Thus, the renewal cycle is around 20 days in young adults, while in older adults it is more than 30 days [2,20]. Over time, the body's ability to replenish collagen decreases by about 1.0%-1.5% per year, resulting in the appearance of fine lines and deeper wrinkles [5]. ...
With ageing, collagen production slows down, leading to wrinkle appearance and loss of elasticity. Replenishing key structural molecules through oral supplementation is a promising strategy that complements the topical delivery of cosmetic products and creates a holistic skincare regimen. The present study assessed the effectiveness of a food supplement with collagen peptides, vitamins and minerals in improving the quality of the skin and general wellbeing of healthy women.
This was an open-label study of 135 women aged between 45 and 65 years. A 3-month treatment phase followed a 4-week washout phase, with visits scheduled at baseline and after each month of treatment. Subjects received three tablets of Richelet Skin Renewal daily. The primary outcome was change from baseline to month 3 in global wrinkles score by expert grader analysis. Secondary outcomes included changes in skin elasticity and other skin attributes, product assessment via self-perception questionnaires and total antioxidant status.
A total of 116 subjects completed the study. The mean global wrinkles score indicated a statistically significant decrease from 5.9 at baseline to 5.0 at month 3 (p < 0.0001), with 83.6% of subjects showing an improvement; significant changes were reported at all intermediate visits. The increase in skin elasticity was also statistically significant (R2 score 0.74 at month 3; p < 0.0001). All subjects (100%) demonstrated significant improvements in skin texture, skin tone evenness, skin radiance and overall skin quality at the month 3 visit.
The study product achieved statistically significant, noticeable effects on global wrinkles, skin elasticity and a range of skin attributes after 3 months of use in healthy women. These results strengthen the evidence for supplementation of collagen peptides and other micronutrients as an effective component of anti-ageing skincare.
... More than 80% of the total protein in fish skin discarded as processing residue is composed of type I collagen (Kimura et al., 1999;David et al., 2020). Type I collagen fulfills the main supporting function not only in fish but also in all vertebrates as the major fibrillar component. ...
Dipeptidyl peptidase IV (DPP-IV) inhibitors are antidiabetic drugs that can lower blood sugar levels. There are still few reports on the DPP-IV inhibitory activity of peptides obtained from discarded fish skin. Therefore, we prepared various enzymatic hydrolysates using the skins of six fish species and investigated their DPP-IV inhibitory effects. As a result, it was found that the DPP-IV inhibitory activity of yellowtail hydrolysate by Alcalase was higher than that of other enzymes. In addition, the IC50 after ethanol fractionation was found to be lower in yellowtail and eel skin hydrolysate. Amino acid composition analysis showed that the hydrolysate obtained from the skin of the yellowtail contained the highest amount of Gly, followed by Pro, Hyp, and Ala, indicating that it was a peptide derived from type I collagen. Fractionation with ethanol showed that the DPP-IV inhibitory components were contained in the low molecular weight fraction. The artificial digestion test observed no DPP-IV inhibitory activity or average molecular weight change. The DPP-IV inhibitory peptide obtained from fish skin has the potential to be applied as a food material to various food products.
... The primary constituent of the ECM and a crucial marker of skin photoaging, collagen contributes to maintaining the skin's structural integrity and physiological function. Especially type I collagen, accounting for 70 % of the generous layer in the skin's dermis, is essential for maintaining skin elasticity, firmness, and resistance to aging, but its production declines with age (Shin et al., 2019;Reilly and Lozano, 2021). UVB exposure contributes to the formation of ROS, which in turn activates the MAPK pathway and induces the AP-1 transcription factor; this further induces MMP-1 synthesis. ...
Photoaging of skin tissue can result from exposure to ultraviolet B (UVB) radiation. This study developed two nanocarriers Centella asiatica (CA) transfersomes (TF) and Bergamot essential oil (BEO) nanoemulsions (NE) combined in a gel formulation as a drug delivery system, in order to study whether they could synergize to prevent UVB radiation and provide anti-photoaging effects. Nanoencapsulation of CA-TF and BEO-NE were examined for their quality by characterizing their physicochemical properties. An in vivo study evaluated topically applied CA-TF and BEO-NE combination gels biological effect on BALB/c mice before UVB radiation (840 mJ/cm 2) for two weeks. Particle size analysis of developed nanocarriers exhibited monodispersed pattern with an average particle size and zeta potential of around 9.64 ± 0.35 nm and − 39.86 ± 1.33 mV, respectively. In vivo experiments showed that topically applied CA-TF and BEO-NE combination gel significantly prevented UVB-induced wrinkle formation and skin erythema and inhibited histological damage, including epidermal hyper-plasia, collagen fibers, and the destruction of elastic fibers. Additionally, the CA-TF and BEO-NE combination gel reduced UVB-induced oxidative stress by increasing superoxide dismutase (SOD) activity and suppressed lipid peroxidation by decreasing malondialdehyde (MDA) expression as well as inhibiting the expression of UVB-induced pro-inflammatory cytokines include tumor necrosis factor α (TNF-α) and interleukin 6 (IL-6). Moreover , the CA-TF and BEO-NE combination gel increased the type I collagen expression, restoring UVB-induced collagen production and density. Therefore, nanoencapsulation CA-TF and BEO-NE combination gel could synergistically prevent UVB-induced oxidative stress and inflammatory responses.
... Further work should address whether similar changes in homeostasis continue after development ceases; however, the reduction in collagen levels and increase in MMP levels are well-established markers of ageing [8,32,58]. These data are, therefore, good evidence that while senescent cells may play a role in tissue ageing and ECM degradation, cells are also undergoing an ageing process that is independent of their replicative lifespan. ...
Skin ageing is defined, in part, by collagen depletion and fragmentation that leads to a loss of mechanical tension. This is currently believed to reflect, in part, the accumulation of senescent cells. We compared the expression of genes and proteins for components of the extracellular matrix (ECM) as well as their regulators and found that in vitro senescent cells produced more matrix metalloproteinases (MMPs) than proliferating cells from adult and neonatal donors. This was consistent with previous reports of senescent cells contributing to increased matrix degradation with age; however, cells from adult donors proved significantly less capable of producing new collagen than neonatal or senescent cells, and they showed significantly lower myofibroblast activation as determined by the marker α-SMA. Functionally, adult cells also showed slower migration than neonatal cells. We concluded that the increased collagen degradation of aged fibroblasts might reflect senescence, the reduced collagen production likely reflects senescence-independent processes.
... Twenty-nine types of this protein can be distinguished. Collagen, mainly type I, II, and III, is present in human organisms and can be found in skin (type I and type III), bone tissue, tendons, or blood vessels [5][6][7][8][9]. For industrial purposes, usually porcine or bovine collagen is used but a source of collagen rather free from disease transmission can be extracted from marine organisms [4]. ...
The aim of this research was the modification of fish collagen films with various amounts of dialdehyde starch (DAS). Film properties were examined before and after the cross-linking process by DAS. Prepared biopolymer materials were characterized by Fourier Transform Infrared Spectroscopy and Atomic Force Microscopy. Moreover, the mechanical, thermal and swelling properties of the films were evaluated and the contact angle was measured. Research has shown that dialdehyde starch applied as a cross-linking agent influences collagen film properties. Mechanical testing indicated a decrease in Young’s Modulus and an increase in breaking force, elongation at break, and tensile strength parameters. Results for contact angle were significantly higher for collagen films cross-linked with DAS; thus, the hydrophilicity of samples decreased. Modified samples presented a lower swelling degree in PBS than native collagen films. However, the highest values for the degree of swelling among the modified specimens were obtained from the 1% DAS samples, which were 717% and 702% for 1% and 2% collagen, respectively. Based on AFM images and roughness values, it was noticed that DAS influenced collagen film surface morphology. The lowest value of Rq was observed for 2%Coll_2%DAS and was approximately 10 nm. Analyzing thermograms for collagen samples, it was observed that pure collagen samples were less thermally stable than cross-linked ones. Dialdehyde starch is a promising cross-linking agent for collagen extracted from fish skin and may increase its applicability.
... Pro-collagen is a precursor of collagen (Freiberger et al. 1980). Collagen is known to provide preservation of skin stability and elasticity (Reilly and Lozano 2021). ...
... With age, solubility tends to decrease due to the greater crosslinking of collagen in older animals [20]. Aging processes lead to crosslinking of the protein structure and affect its mechanical properties [15,20,33]. Mature CLG has a highly crosslinked structure and is usually insoluble in water. ...
... CLG is found in various tissues of the body (Tables 1 and 2), and its structure varies depending on its location and function. Aging processes lead to crosslinking of the protein structure and affect its mechanical properties [15,20,33]. Mature CLG has a highly crosslinked structure and is usually insoluble in water. ...
... In the immune system, it prevents the entry of pathogenic microorganisms and toxic substances [30]. It ensures the continuity of cell renewal processes in the skin and maintains the appropriate level of hydration, which affects its elasticity, appearance, and condition [33,38,39]. It accelerates wound healing, creates scars, and promotes the reconstruction of connective tissue [40,41]. ...
Collagen (CLG) belongs to the family of fibrillar proteins and is composed of left-handed α polypeptide chains, which, twisting around themselves and their axis, form a right-handed superhelix. In the chemical structure, it contains mainly proline, hydroxyproline, glycine, and hydroxylysine. It occurs naturally in the dermis in the form of fibers that provide the skin with proper density and elasticity. The review aimed to present the types of collagen protein, factors affecting its structure and its unusual role in the functioning of the human body. Also, an overview of cosmetic products containing collagen or its derivatives, the characteristics of the formulas of these products, and the effects of their use were presented. Throughout the market, there are many cosmetic and cosmeceutical products containing CLG. They are in the form of fillers administered as injections, belonging to the group of the oldest tissue fillers; products administered orally and for topical use, such as creams, gels, serums, or cosmetic masks. Analyzed studies have shown that the use of products with collagen or its peptides improves the general condition of the skin and delays the aging process by reducing the depth of wrinkles, improving hydration (in the case of oral preparations), reducing transepithelial water loss (TEWL), as well as improving skin density and elasticity. In addition, oral application of bioactive CLG peptides has shown a positive effect on the nails, reducing the frequency of their breakage.
... Collagen, being a ubiquitous protein constituent across mammalian species, assumes a multifaceted role, being deposited within diverse organs and tissues, while simultaneously playing a pivotal role in both structural and functional aspects (Franchi et al., 2007;Devos et al., 2023). Consistently, it has been well-established that the process of collagen deposition is orchestrated through a complex interplay of gene regulatory networks (Reilly and Lozano, 2021). ...
... These genetic variations within these collagen-related genes may exert substantial influence on collagen expression, structure, and function, thereby modulating the pathogenesis and clinical manifestations of atopic dermatitis (Söderhäll et al., 2007). Consistently, it has been revealed that collagen alpha family genes play a key role in skin aging in human (Wang and Gu, 2021), and hair follicular stem cell development in goat (Reilly and Lozano, 2021) by regulating extracellular matrix and collagen organization respectively. ...
The primary focus of donkey hide gelatin processing lies in the dermal layer of donkey hide due to its abundant collagen content. However, the molecular mechanism involved in collagen organization and skin development in donkey skin tissue across various developmental stages remains incomplete. The current study aims to investigate the transcriptomic screening of lncRNAs and mRNA associated with skin development and collagen organization across different ages in Dezhou donkeys’ skin. In the pursuit of this objective, we used nine skin tissue samples obtained from Dezhou donkeys at various ages including 8-month fetal stage, followed by 2 and 8 years. RNA-seq analysis was performed for the transcriptomic profiling of differentially expressed genes (DEGs) and lncRNAs associated with skin development in different age groups. Our investigation revealed the presence of 6,582, 6,455, and 405 differentially expressed genes and 654, 789, and 29 differentially expressed LncRNAs within the skin tissues of Dezhou donkeys when comparing young donkeys (YD) vs. middle-aged donkeys (MD), YD vs. old donkeys (OD), and MD vs. OD, respectively. Furthermore, we identified Collagen Type I Alpha 1 Chain (COL1A1), Collagen Type III Alpha 1 Chain (COL3A1), and Collagen Type VI Alpha 5 Chain (COL6A5) as key genes involved in collagen synthesis, with COL1A1 being subject to cis-regulation by several differentially expressed LncRNAs, including ENSEAST00005041187, ENSEAST00005038497, and MSTRG.17248.1, among others. Interestingly, collagen organizational and skin development linked pathways including Protein digestion and absorption, metabolic pathways, Phosphatidylinositol 3-Kinase-Protein Kinase B signaling pathway (PI3K-Akt signaling pathway), Extracellular Matrix-Receptor Interaction (ECM-receptor interaction), and Relaxin signaling were also reported across different age groups in Dezhou donkey skin. These findings enhance our comprehension of the molecular mechanisms underlying Dezhou donkey skin development and collagen biosynthesis and organization, thus furnishing a solid theoretical foundation for future research endeavors in this domain.
... As PIP3 has shown its capacity to initiate mechanisms linked to collagen production, it holds potential for addressing conditions involving reduced collagen levels, such as aging-related changes or wrinkle formation [96][97][98]. ...
... After observing increased collagen production upon the introduction of PIP3 and its complexes, the next objective was to investigate whether the addition of PIP3 can also As PIP3 has shown its capacity to initiate mechanisms linked to collagen production, it holds potential for addressing conditions involving reduced collagen levels, such as aging-related changes or wrinkle formation [96][97][98]. ...
Given the role of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in modulating cellular processes such as proliferation, survival, and migration, we hypothesized its potential as a novel therapeutic agent for wound closure enhancement. In this study, PIP3 was examined in its free form or as a complex with cationic starch (Q-starch) as a carrier. The intracellular bioactivity and localization of free PIP3 and the Q-starch/PIP3 complexes were examined. Our results present the capability of Q-starch to form complexes with PIP3, facilitate its cellular membrane internalization, and activate intracellular paths leading to enhanced wound healing. Both free PIP3 and Q-starch/PIP3 complexes enhanced monolayer gap closure in scratch assays and induced amplified collagen production within HaCAT and BJ fibroblast cells. Western blot presented enhanced AKT activation by free or complexed PIP3 in BJ fibroblasts in which endogenous PIP3 production was pharmacologically inhibited. Furthermore, both free PIP3 and Q-starch/PIP3 complexes expedited wound closure in mice, after single or daily dermal injections into the wound margins. Free PIP3 and the Q-starch/PIP3 complexes inherently activated the AKT signaling pathway, which is responsible for crucial wound healing processes such as migration; this was also observed in wound assays in mice. PIP3 was identified as a promising molecule for enhancing wound healing, and its ability to circumvent PI3K inhibition suggests possible implications for chronic wound healing.
