Type 1 collagen supplement
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Benefits and Effects of Type 1 Collagen Supplementation
Introduction to Type 1 Collagen
Type 1 collagen is a crucial structural protein found abundantly in various tissues, including skin, bones, tendons, and ligaments. It plays a significant role in maintaining the structural integrity and function of these tissues3. Given its importance, type 1 collagen supplementation has garnered attention for its potential health benefits, particularly in skin health and anti-aging.
Skin Health and Anti-Aging Benefits
Improvement in Skin Parameters
Research indicates that oral supplementation of hydrolyzed type 1 collagen can lead to improvements in several skin health parameters. Studies have shown enhancements in skin elasticity, reduction in wrinkles, increased hydration, and improved skin thickness, particularly in individuals aged 35 and above, with a notable impact on the female demographic1. These benefits suggest that type 1 collagen supplementation could be a valuable tool in combating skin aging.
Divergence in Dosage and Duration
Despite the promising results, there is a lack of consensus on the optimal dosage and duration of type 1 collagen supplementation. The studies reviewed highlight a need for standardized protocols to determine the most effective dosage and supplementation period for achieving the best skin health outcomes1.
Collagen Synthesis and Biomarkers
Shilajit Supplementation and Collagen Synthesis
A study investigating the effects of Shilajit supplementation on type 1 collagen synthesis found significant increases in serum pro-c1α1, a biomarker of collagen synthesis, after 8 weeks of daily supplementation. Both low (500 mg/day) and high (1000 mg/day) doses of Shilajit resulted in increased collagen synthesis compared to a placebo, with the high dose showing a more pronounced effect2. This suggests that Shilajit could be an effective supplement for enhancing collagen production.
Sources and Extraction of Type 1 Collagen
Fish as a Source of Collagen
Fish skin, bones, and fins have been identified as viable sources of type 1 collagen. Studies have demonstrated that collagen extracted from these fish parts has acceptable yields and physicochemical properties, making them suitable for use in supplements and other applications5. The denaturation temperatures of fish-derived collagen are slightly lower than those of porcine collagen, but they still offer a valuable alternative, especially considering concerns over BSE transmission from land animals5.
Impact of Collagen-Rich Diets
Supplementing the diet of aquatic animals, such as Tilapia, with hydrolyzed collagen has been shown to enhance the yield of extracted collagen. This approach not only supports sustainable practices by utilizing fish waste materials but also potentially increases the body's collagen biosynthesis4.
Conclusion
Type 1 collagen supplementation offers promising benefits for skin health, particularly in improving elasticity, reducing wrinkles, and enhancing hydration. While there is evidence supporting the efficacy of collagen supplements, further research is needed to standardize dosages and supplementation periods. Additionally, fish-derived collagen presents a sustainable and effective source for these supplements, potentially enhancing collagen biosynthesis and supporting overall tissue health.
Sources and full results
Most relevant research papers on this topic
BENEFITS OF HYDROLYZED COLLAGEN TYPE 1 SUPPLEMENTATION ON SKIN HEALTH
Type 1 hydrolyzed collagen supplementation may improve skin elasticity, wrinkles, hydration, and thickness in individuals aged 35 and over, but more research is needed to standardize doses and duration.
Systematic ReviewEffects of 8 Weeks of Shilajit Supplementation on Serum Pro-c1α1, a Biomarker of Type 1 Collagen Synthesis: A Randomized Control Trial
8 weeks of Shilajit supplementation with 500 and 1000 mgd1 significantly increased type 1 collagen synthesis compared to placebo.
RCTCurrent Insights into Collagen Type I
Collagen type I (Col-I) is a biocompatible protein with potential applications in pharmaceutical, cosmeceutical, regenerative medicine, and clinical fields due to its high biocompatibility and acceptable physicochemical properties.
Highly CitedWAXS and SAXS Investigation of Collagen-Rich Diet Effect on Multiscale Arrangement of Type I Collagen in Tilapia Skin Fed in Aquaponics Plant
A collagen-rich diet in Tilapia enhances collagen biosynthesis and enhances collagen yield at the nanoscale, but has no effect on submolecular scale.
Isolation of collagen from fish waste material — skin, bone and fins
Fish waste materials, such as skin, bone, and fins, have potential as a source of collagen to supplement land vertebrates' skin.
Highly CitedCollagen supplementation for rheumatoid arthritis and osteoarthritis
Collagen supplementation may help reduce joint pain and inflammation in rheumatoid arthritis and osteoarthritis, but it's important to consider other factors like vitamin C, age, and collagen-related food intake.
Systematic ReviewMultilayered dense collagen–silk fibroin hybrid: a platform for mesenchymal stem cell differentiation towards chondrogenic and osteogenic lineages
Multilayered dense collagen-silk fibroin hybrids stabilize collagen-based hydrogels, promoting mesenchymal stem cell differentiation towards chondrogenic and osteogenic lineages.
In Vitro StudyEfficacy and tolerability of an undenatured type II collagen supplement in modulating knee osteoarthritis symptoms: a multicenter randomized, double-blind, placebo-controlled study
Undenatured type II collagen supplementation significantly improved knee osteoarthritis symptoms and was well-tolerated compared to placebo and glucosamine hydrochloride plus chondroitin sulfate.
RCT
Very Rigorous JournalHighly CitedIsolation and characterization of the rat alpha 1(I) collagen promoter. Regulation by 1,25-dihydroxyvitamin D.
The rat alpha 1(I) collagen promoter is regulated by 1,25-dihydroxyvitamin D in osteosarcoma cells, suggesting its potential role in type I collagen synthesis inhibition.
In Vitro StudyHighly CitedComparison of physical-chemical properties of type I collagen from different species
Type I collagen from bird feet and porcine skin show better biostability and thermal stability, while frog skin collagen has higher enzyme resistance.
Highly Cited