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Beneficial Effect of Collagen Peptide Supplement on Anti-aging Against Photodamage
Abstract
Recent research has revealed that hydrolyzed collagen peptides have beneficial effects in various diseases such as osteoarthritis and human rheumatoid arthritis and also play a protective role in skin by improving the activity of antioxidants. In this study, we investigated the effects of a novel mixture (AP-CPM01) containing collagen peptides and elastin peptides on photoaged hairless mice skin both in vivo and in vitro. To evaluate the effects of AP-CPM01 on UVBinduced skin wrinkle formation in vivo, the hairless mice were exposed to UVB irradiation and orally administered the AP-CPM01 at 333 mg/kg per day for 10 weeks. The effects on skin appearance and epidermal thickness were measured using bioengineering and histochemical methods. In addition, the influence of AP-CPM01 on collagen metabolism in human skin fibroblasts was also investigated. The skin of mice in the AP-CPM01 treated group had better appearance and less wrinkling than that of mice in the control group. In the human fibroblast cells, the amount of de novo procollagen synthesis was increased after AP-CPM01 treatment, reflecting that AP-CPM01 can induce de novo procollagen synthesis and reduce UVB-induced skin wrinkle formation. These results suggest that AP-CPM01 is a potent candidate for antiphotoaging functions.
... In our previous study, oral LMCP administration displayed health benefits in human skin by reducing wrinkles and increasing hydration and elasticity [16]. Through a mechanism study, we confirmed that LMCP stimulated skin fibroblasts to synthesize type I collagen and hyaluronic acid [17,18]. In addition, LMCP inhibits the decomposition of dermal collagen by downregulating the gene expression of collagenases (MMP-3 and MMP-13) and gelatinases (MMP-2 and MMP-9) [19]. ...
... In our previous study, LMCP exerted beneficial effects on skin health by stimulating skin fibroblasts and promoting the synthesis of ECM components such as type I collagen and hyaluronic acid [17,18]. Similar to our previous findings, LMCP contributed to OA inhibition by promoting the synthesis of type II collagen and aggrecan in chondrocytes. ...
This study aimed to determine the function of LINC00511 in NLRP3 inflammasome-mediated chondrocyte pyroptosis via the regulation of miR-9-5p and FUT 1. Chondrocyte inflammatory injury was induced by treating chondrocytes with LPS. Afterwards, the levels of IL-1β and IL-18, the expression of NLRP3, ASC, Caspase-1, and GSDMD, cell viability, and LDH activity in chondrocytes were assessed. LINC00511 expression in LPS-treated chondrocytes was detected, and LINC00511 was subsequently silenced to analyse its role in chondrocyte pyroptosis. The subcellular localization of LINC00511 was predicted and verified. Furthermore, the binding relationships between LINC00511 and miR-9-5p and between miR-9-5p and FUT1 were validated. LINC00511 regulated NLRP3 inflammasome-mediated chondrocyte pyroptosis through the miR-9-5p/FUT1 axis. LPStreated ATDC5 cells exhibited elevated levels of inflammatory injury; increased levels of NLRP3, ASC, Caspase-1, and GSDMD; reduced cell viability; increased LDH activity; and increased LINC00511 expression, while LINC00511 silencing inhibited the NLRP3 inflammasome to restrict LPS-induced chondrocyte pyroptosis. Next, LINC00511 sponged miR-9-5p, which targeted FUT1. Silencing LINC00511 suppressed FUT1 by upregulating miR-9-5p. Additionally, downregulation of miR-9-5p or overexpression of FUT1 neutralized the suppressive effect of LINC00511 knockdown on LPSinduced chondrocyte pyroptosis. Silencing LINC00511 inhibited the NLRP3 inflammasome to quench Caspase-1-dependent chondrocyte pyroptosis in OA by promoting miR-9-5p and downregulating FUT1.
... In our previous study, oral LMCP administration displayed health benefits in human skin by reducing wrinkles and increasing hydration and elasticity [16]. Through a mechanism study, we confirmed that LMCP stimulated skin fibroblasts to synthesize type I collagen and hyaluronic acid [17,18]. In addition, LMCP inhibits the decomposition of dermal collagen by downregulating the gene expression of collagenases (MMP-3 and MMP-13) and gelatinases (MMP-2 and MMP-9) [19]. ...
... In our previous study, LMCP exerted beneficial effects on skin health by stimulating skin fibroblasts and promoting the synthesis of ECM components such as type I collagen and hyaluronic acid [17,18]. Similar to our previous findings, LMCP contributed to OA inhibition by promoting the synthesis of type II collagen and aggrecan in chondrocytes. ...
This study reveals that low-molecular-weight collagen peptide (LMWCP) can stimulate the differentiation and the mineralization of MC3T3-E1 cells in vitro and attenuate the bone remodeling process in ovariectomized (OVX) Sprague-Dawley rats in vivo. Moreover, the assessed LMWCP increased the activity of alkaline phosphatase (ALP), synthesis of collagen, and mineralization in MC3T3-E1 cells. Additionally, mRNA levels of bone metabolism-related factors such as the collagen type I alpha 1 chain, osteocalcin (OCN), osterix, bone sialoprotein, and the Runt family-associated transcription factor 2 were increased in cells treated with 1,000 μg/ml of LMWCP. Furthermore, we demonstrated that critical bone morphometric parameters exhibited significant differences between the LMWCP (400 mg/kg)-receiving and vehicle-treated rat groups. Moreover, the expression of type I collagen and the activity of ALP were found to be higher in both the femur and lumbar vertebrae of OVX rats treated with LMWCP. Finally, the administration of LMWCP managed to alleviate osteogenic parameters such as the ALP activity and the levels of the bone alkaline phosphatase, the OCN, and the procollagen type 1 N-terminal propeptide in OVX rats. Thus, our findings suggest that LMWCP is a promising candidate for the development of food-based prevention strategies against osteoporosis.
Background
Photoaging is a process of the architecture of normal skin damaged by ultraviolet radiation. Topical cosmeceuticals have been used to treat this condition. The authors aimed to understand the mechanism and level of evidence of different commonly used cosmeceuticals used to treat photodamaged skin.
Objective
A range of commonly used topical cosmeceuticals (botanicals, peptides, and hydroquinone) has been used in cosmetic medicine for many years to treat photodamaged skin. This review article compares their efficacy and level of evidence.
Material and methods
This study was a systematic review to evaluate the efficacy of different topical cosmeceuticals. Keywords including “Photoaging,” “Azelaic acid,” “Soy,” “Green Tea,” “Chamomile,” “Ginkgo,” “Tea Tree Oil,” “Resveratrol,” “Cucumber,” “Ginseng,” “Centella asiatica,” “Licorice Root,” “Aloe Vera,” “Peptides,” “Argireline,” “Hydroquinone,” were typed on OVID, PUBMED, MEDLINE for relevant studies published on photoaging treatment.
Results
Most of the evidence behind cosmeceuticals is of high‐quality ranging from Level I to Level II. In particular, the evidence base behind peptides is the strongest with most studies achieving Level Ib status in the evidence hierarchy.
Conclusion
Topical cosmeceuticals like botanicals, peptides and hydroquinone can effectively treat photodamaged skin
The objective of this study was to determine the optimal cooking time by considering the cooking loss, shear force, and off-odor reduction of pork large intestines. Commercial pork large intestines were purchased, quartered perpendicularly, and cooked in boiling water for 40, 120, 180, and 240 min. Cooking loss of the samples increased after 240 min of cooking (10.92, p<0.05) while shear force value was lower at 240 min (4.45) compared to that at other cooking times (p<0.001). The amount of major volatile organic compounds showed a decreasing trend with increasing cooking time. In particular, the amount of methyl pentanoate (17,528.71) and methyl isobutyrate (812.51), compounds with a relatively low odor threshold, decreased significantly after 120 min of cooking and no change was observed thereafter (p<0.05). In addition, the amount of 2-pentanol (3,785.65) and 1-propanol (622.26), possibly produced by lipid oxidation, significantly decreased at the same cooking time (p<0.001). In the principal component analysis, only the 40 min cooking time was significantly different from other cooking time by high amounts of 1-propanol, 2-pentanol, and methyl isobutyrate. In conclusion, in the present study, the optimal cooking time for pork large intestines was 120 min in terms of off-odor reduction, cooking loss, and shear force.
This study examined whether the oral administration of low-molecular-weight collagen peptide (LMCP) containing 3% Gly-Pro-Hyp with >15% tripeptide (Gly-X-Y) content could ameliorate osteoarthritis (OA) progression using a rabbit anterior cruciate ligament transection (ACLT) model of induced OA and chondrocytes isolated from a patient with OA. Oral LMCP administration (100 or 200 mg/kg/day) for 12 weeks ameliorated cartilage damage and reduced the loss of proteoglycan compared to the findings in the ACLT control group, resulting in dose-dependent (P < 0.05) improvements of the OARSI score in hematoxylin & eosin and Safranin O staining. In micro-computed tomography analysis, LMCP also significantly (P < 0.05) suppressed the deterioration of the microstructure in tibial subchondral bone during OA progression. The elevation of IL-1β and IL-6 concentrations in synovial fluid following OA induction were dose-dependently (P < 0.05) reduced by LMCP treatment. Furthermore, immunohistochemistry illustrated that LMCP significantly (P < 0.05) upregulated type II collagen and downregulated matrix metalloproteinase-13 in cartilage tissue. Consistent with the in vivo results, LMCP significantly (P < 0.05) increased the mRNA expression of COL2A1 and ACAN in chondrocytes isolated from a patient with OA regardless of the conditions for IL-1β induction. These findings suggest that LMCP has potential as a therapeutic treatment for OA that stimulates cartilage regeneration.
Social and social–ecological network analysis (S(E)NA) have recently emerged as new methods in the environmental governance (EG) literature. By investigating networks of connections between actors, S(E)NA advances the understanding of who is involved in EG and how. We provide an overview of the EG literature applying S(E)NA and map (1) the citation network emerging from cross-references and (2) the similarity network emerging from word similarities between publications.
We show that S(E)NA application in EG is in the process of developing into a field of research where publications frequently cite each other. We identify 20 publications which occupy positions as sources, storers, or bridges of knowledge in the citation network. While we see S(E)NA applied in diverse resource contexts, these are mainly discussed on the local spatial level, with a focus on “policy” or “collaboration.” We discover that “power structures” and “the production of knowledge” are themes influencing the whole field.
Keywords: bibliometric network analysis, environmental management, Latent Dirichlet Allocation, social network analysis, topic detection.
Hydroxyproline and Pro-Hyp dipeptide are the digestive products of collagen hydrolysate called collagen peptide. Some suggested that collagen peptides could improve aged or damaged skins, however, the effects of collagen peptides on the skin have not been known. In this study, we investigated the effects of digestive products of collagen peptides, hydroxyproline and Pro-Hyp dipeptide on skin quality using the UV-damaged dorsal skin of hairless mouse as a model system. Female SKH hairless mice were pre-irradiated with UV for 7 weeks, and then hydroxyproline, Pro-Hyp dipeptide were orally administered for 7 weeks with UV irradiation. Wrinkle formation (by replica image), skin elasticity, barrier status (by TEWL, transepidermal water loss), epidermis thickness, and biophysical changes in the stratum comeum (by hematoxylin & eosin staining) were examined. With the oral peptide treatment, effects such as skin barrier maintenance, anti-skin thickening, and recovery of the stratum corneum were observed. These results indicate that oral intake of collagen peptides may have beneficial effects on damaged skin cells.
Hepatic stellate cells become activated into myofibroblast-like cells during the early stages of hepatic injury associated
with fibrogenesis. The subsequent dysregulation of hepatic stellate cell collagen gene expression is a central pathogenetic
step during the development of cirrhosis. The cytoplasmic Raf and mitogen-activated protein (MAPK) kinases were found to differentially regulate αI(I) collagen gene expression in activated stellate cells. This suggests an unappreciated branch point exists between
Raf and MAPK. A MAPK-stimulatory signal was mapped to the most proximal NF-1 and Sp-1 binding domains of the 5′-untranslated
region of the collagen gene. A Raf-inhibitory signal was mapped to a further upstream binding domain involving a novel 60-kDa
DNA-binding protein (p60). The cell-specific expression and induction of p60 in stellate cells during the early stages of
hepatic fibrogenesis in vivo suggest a central role for this pathway during liver injury and stellate cell activation.
This study aimed to investigate the alterations in plasma antioxidant activity after the consumption of a single oral dose of curcumin, vitamin C, and E administered individually or in combination to (i) assess possible synergies or antagonism between the antioxidants and (ii) determine the optimal composition of the antioxidant mixture such that the duration of action is prolonged to beyond that of individual antioxidants. Each antioxidant was administered to male Sprague-Dawley rats, and blood samples were drawn at different time points up to 180 min to measure the plasma total antioxidant capacity (TAC). Five antioxidant compositions (M1-M5) were evaluated to assess the possible synergies or antagonisms among them and to determine the optimal composition of the antioxidant mixture. Blood samples were collected up to 360 min post-consumption. A single oral dose of individual antioxidants significantly increased the TAC values; however, the time to reach the peak TAC value varied. Among the 5 antioxidant compositions, M2 exhibited the highest and most prolonged antioxidant effect in plasma; this was greater than the proportional sum of the effects of the individual antioxidants in the composition. This result indicates a synergistic interaction among antioxidants in the optimal composition M2.
UV irradiation induces a variety of cutaneous responses, including disruption of epidermal permeability barrier function, the basis for which is not known. Herein, we investigated the separate roles of hyperproliferation and inflammation in the pathogenesis of UVB-induced barrier disruption. Adult hairless mice were exposed to increasing doses of UVB (1.5–7.5 MED), and transepidermal water loss (TEWL) was monitored daily for up to 7 d. The extent of TEWL increase was dependent on the UVB dose, but with all doses, the increase began after 48 h and peaked at 96 h, decreasing by 120 h. Epidermal [³H]thymidine incorporation increased at 24 h and peaked at 48 h (570%), preceding the maximal increase in TEWL. Cyclosporin A, methotrexate, 5-fluorouracil, or arabinosylcytosine significantly diminished the UVB-induced TEWL increase. Athymic nude mice also displayed a markedly diminished response to UVB, and DNA synthesis did not increased at 48 h. Transplantation of athymic mice with T-cell- enriched mixed immune cells significantly restored sensitivity to both the UVB-induced hyperproliferation and the barrier defect. Finally, although UVB exposure increased PGE2 levels in whole skin samples (2- to 3-fold within 1–3 h; p < 0.005), this increase was completely blocked by topical indomethacin, and neither topical indomethacin nor topical glucocorticoids blocked development of the barrier abnormality. These results show that (i) UVB produces delayed alteration in barrier function and (ii) both an epidermal proliferative response and thymocyte-mediated events (but not PGE2 production and nonspecific inflammation) appear to contribute to UVB-induced abrogation of the permeability barrier.Keywords: epidermal permeability barrier, DNA synthesis, T cells, athymic
Chronic ultraviolet (UV) exposure is the major cause of photoaging that causes skin wrinkling, roughness, dry-ness, laxity, and pigmentation. Recently, increasing efforts are being made to understand the relationship between foods and skin health. Ginsenosides are present in ginseng (Ginseng Radix Rubra) extract, and are known to have biomedical properties, such as, anti-oxidant and anti-inflammatory effects. In this study, we investigated whether KTNG0345 prepared from red ginseng extracts delivered orally reduces skin wrinkling and ultraviolet B (UVB)-induced wrinkle formation in hairless mouse skin. KTNG0345 was administrated orally to the mice (5 times a week) during the period of UVB-irra-diation (3 times a week) for 8 weeks at three different doses of 300 mg/kg, 500 mg/kg and 1000 mg/kg (w/v). UV doses were increased weekly by 1 MED (1MED = 75 mJ/cm 2) up to 4 MED and then maintained at this level. After the 8-week administration period, it was found that orally administered KTNG0345 significantly inhibited UVB-induced wrinkle for-mation in a dose-dependent manner. Increases in skin thickness caused by UVB were prevented by KTNG0345. More-over, it also significantly inhibited matrix metalloproteinases (MMP) -13 and MMP-9 expressional inductions by UVB. In addition, KTNG0345 was observed to prevent UVB-induced water loss of epidermis in hairless mouse skin. Our results demonstrate that orally administered KTNG0345 has anti-wrinkling effects in hairless mouse skin, and suggest that dietary red ginseng and herbal mixture may be considered a functional beauty food for preventing UVB-induced skin wrinkles.
The expression of collagen type I, II, and III was investigated to evaluate phenotypic change in chondrocytes in loose bodies
related to osteoarthritis. We assessed collagen type I, II, and III production in loose bodies from knee joints of ten osteoarthritic
patients, using an immunohistochemical method with monoclonal antibodies. Collagen type III expression was identified in all
ten loose bodies and was mainly located in cartilage, including chondrocytes and matrices, as well as in a layer of fibroid
tissue on the surface. No positive signal for collagen type III was observed in necrotic osteocytes. There was weakly positive
staining for collagen type I in chondrocytes. No positive staining for collagen type II could be seen in the cartilage of
loose bodies. Cartilage from the non-osteoarthritic knee joints of four people was negative for the expression of collagen
type I and III, and positive for the expression of collagen type II. Collagen type I and III expression suggested the dedifferentiation
status of chondrocytes in loose bodies.
We examined the effect of prolyl-hydroxyproline (Pro-Hyp), which occurs in human peripheral blood after ingestion of collagen peptide, on the migration and growth of mouse skin fibroblasts. Mouse skin discs were cultured on a 24-well plastic plate in a fetal bovine serum (FBS)-free medium. Addition of Pro-Hyp (200 nmol/mL) significantly increased the number of fibroblasts migrating from the skin to the plate after incubation for 72 h. This effect of Pro-Hyp was abolished by the addition of mitomycin C. The fibroblasts that had migrated from the mouse skin were collected and cultured on collagen gel. The growth of fibroblasts on the collagen gel was suppressed even in the presence of FBS, while rapid fibroblast growth was observed on the plastic plate. Addition of Pro-Hyp (0-1000 nmol/mL) to the medium containing 10% FBS enhanced the growth of fibroblasts on the collagen gel in a dose-dependent manner. These results suggest that Pro-Hyp might stimulate the growth of fibroblasts in the skin and consequently increase the number of fibroblasts migrating from the skin.
Dietary supplements (vitamins, polyphenols, micronutrients and proteins) have demonstrated beneficial effects on skin health. The classical route of administration of active compounds is by topical application and manufactures have substantial experience of formulating ingredients in this field. However, the use of functional foods or nutraceuticals for improving skin condition is increasing. The preclinical efficacy assays and bioavailability trials provide a basis from which to establish appropriate collagen hydrolysate (CH) intakes that might impact skin health outcomes. This commentary deals essentially with the general aspects of CH, bioavailability and findings of preclinical studies concerning the effects of CH intake on skin. To comprehensively study the different benefits of CH on skin, controlled clinical trials are needed in addition to the previous pre-clinical and bioavailability assays. Gaps in knowledge are identified and suggestions are made for future research.
Calcitonin has an important role in the treatment of post-menopausal osteoporosis. The authors investigated the effect of calcitonin administration or calcitonin administration supplement with a diet rich in collagen proteins on markers of bone metabolism.
A group of 108 patients with postmenopausal osteoporosis (BMD lower than 80% of the BMD in premenopausal women) was treated with Calsynar (Rhoune Poulenc-Rorer), 100 u., i.m. twice a week for 24 weeks. Forty-nine of these women took an oral collagen hydrolysate, 10 g per day, for the same period of time. Before and after termination of treatment clinical and laboratory tests were made, X-ray examination of the LS spine and the right forearm, single-photon osteometry of the right forearm and urinary excretion of pyridinoline (UPD), deoxypyridinoline (UDPD) and hydroxyproline (Uhyp) was assessed. As a result of treatment the BMD values increased only insignificantly (by 1.8%) the UPD values declined (to 62.51%) and those of UDPD (to 70.4%), as compared with basal values. The statistical significance is at the 1% level. When collagen proteins were administered concurrently, the decline was more marked (to 56.22% and 56.1% resp.), and as compared with the calcitonin treated group (to 67.73% and 82.30% resp.); the difference is significant at the 5% level. The decline of UPD and UDPD values persisted also three months after discontinued treatment; in patients on the diet with collagen hydrolysate practically no rise of these indicators occurred (54.02% and 56.66% resp.).
a) administration of 100 u. calcitonin twice a week for 24 weeks led to a decline of excretion indicators of bone collagen breakdown products, b) the effect of treatment must be monitored using these indicators, c) oral administration of collagen proteins enhanced and prolonged the effect of calcitonin.