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ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ

Yıl 2024, , 1180 - 1188, 10.09.2024
https://doi.org/10.33483/jfpau.1423707

Öz

Amaç: Bugüne kadar oral kolajen takviyeleri hakkında yapılan birçok çalışma kolajen takviyelerinin eklem ve cilt sağlığına üzerindeki etkileri üzerinedir. Kolajenlerin vücudun diğer fonksiyonları üzerine yararlı etkileri bilinmekte olup bunlar hakkında yapılan çalışmalar yetersiz kalmaktadır. Mevcut veriler birçok insan tarafından günlük diyetin önemli bir parçası haline gelen kolajen takviyelerinin herhangi bir toksik etkisi olmadığını, kullanımlarının güvenli olduğunu göstermektedir. Ancak yapılan çalışmalar sonucu birbirini destekleyen verilerin olmamasından dolayı kolajen takviyelerinin bu kadar sık kullanımlarına rağmen toksisiteleri üzerine ek çalışmalar yapılmasına ihtiyaç duyulmaktadır.
Sonuç ve Tartışma: Yapılan literatür taramalarının sonuçları incelendiğinde, olası advers etkilere ait çok az veriye rastlanmıştır. Spesifik kolajenin uzun süreli oral uygulanması vücutta zararlı hücresel hasarlara sebep olabilir, kilo kaybına sebep olabilir, organları hedef alarak işleyişini aksatabilir. Değişken kolajen kaynaklarının içerikleri hakkında bilgi sahibi olmak ve kullanım sürelerine, kullanım miktarlarına dikkat edilmesi gerekir.

Kaynakça

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  • 2. Martínez-Puig, D., Costa-Larrión, E., Rubio-Rodríguez, N., Gálvez-Martín, P. (2023). Collagen supplementation for joint health: The link between composition and scientific knowledge. Nutrients, 15(6), 1332. [CrossRef]
  • 3. Biswal, S., Agmon, N. (2023). Collagen structured hydration. Biomolecules, 13(12), 1744. [CrossRef]
  • 4. Neltner, T.J., Sahoo, P.K., Smith, R.W., Anders, J.P.V., Arnett, J.E., Schmidt, R.J., Johnson, G.O., Natarajan, S.K., Housh, T.J. (2024). Effects of 8 weeks of shilajit supplementation on serum pro-c1α1, a biomarker of type 1 collagen synthesis: A randomized control trial. Journal of Dietary Supplements, 21(1), 1-12. [CrossRef]
  • 5. Anaya Mancipe, J.M., Boldrini Pereira, L.C., de Miranda Borchio, P.G., Dias, M.L., da Silva Moreira Thiré, R.M. (2023). Novel polycaprolactone (PCL)-type I collagen core-shell electrospun nanofibers for wound healing applications. Journal of Biomedical Materials Research: Part B, Applied Biomaterials, 111(2), 366-381. [CrossRef]
  • 6. Huang, Y., Gao, P., Qin, T., Chu, B., Xu, T., Yi, J., Wang, Q., Yang, Z., Jiang, T., Fan, J., Zhao, S., Zhou, W., Chen, J., Yin, G. (2023). Delayed inhibition of collagen deposition by targeting bone morphogenetic protein 1 promotes recovery after spinal cord injury. Matrix Biology: Journal of the International Society for Matrix Biology, 118, 69-91. [CrossRef]
  • 7. Kuttappan, S., Mathew, D., Nair, M.B. (2016). Biomimetic composite scaffolds containing bioceramics and collagen/gelatin for bone tissue engineering- A mini review. International Journal of Biological Macromolecules, 93, 1390-1401. [CrossRef]
  • 8. Fan, L., Ren, Y., Emmert, S., Vučković, I., Stojanovic, S., Najman, S., Schnettler, R., Barbeck, M., Schenke-Layland, K., Xiong, X. (2023). The use of collagen-based materials in bone tissue engineering. International Journal of Molecular Science, 24(4), 3744. [CrossRef]
  • 9. Tang C., Zhou K., Zhu Y., Zhang W., Xie Y., Wang Z., Zhou H., Yang T., Zhang Q., Xu B. (2022). Collagen and its derivatives: From structure and properties to their applications in food industry. Food Hydrocolloids, 131, 107748. [CrossRef]
  • 10. Nurilmala, M., Suryamarevita, H., Husein Hizbullah, H., Jacoeb, A.M., Ochiai, Y. (2022). Fish skin as a biomaterial for halal collagen and gelatin. Saudi Journal of Biological Sciences, 29(2), 1100-1110. [CrossRef]
  • 11. Hu, J., Li, J., Jiang, J., Wang, L., Roth, J., McGuinness, K. N., Baum, J., Dai, W., Sun, Y., Nanda, V., Xu, F. (2022). Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed. Nature Communications, 13(1), 6761. [CrossRef]
  • 12. Gómez-Guillén M.C., Giménez B., López-Caballero M.E., Montero M.P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25(8), 1813-1827. [CrossRef]
  • 13. Xu R., Zheng L., Su G., Luo D., Lai C., Zhao M. (2021). Protein solubility, secondary structure and microstructure changes in two types of undenatured type II collagen under different gastrointestinal digestion conditions. Food Chemistry, 343, 128555. [CrossRef]
  • 14. Zhang X., Zhang H., Toriumi S., Ura K., Takagi Y. (2020). Feasibility of collagens obtained from Bester Sturgeon Huso Huso × Acipenser Ruthenus for industrial use. Aquaculture, 529, 735641. [CrossRef]
  • 15. Zhang, H., Qi, L., Shen, Q., Wang, R., Guo, Y., Zhang, C., Richel, A. (2022). Comparative analysis of the bioactive compounds in chicken cartilage: Protective effects of chondroitin sulfate and type II collagen peptides against osteoarthritis involve gut microbiota. Frontiers in Nutrition, 9, 843360. [CrossRef]
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  • 18. Jafari, H., Lista, A., Siekapen, M.M., Ghaffari-Bohlouli, P., Nie, L., Alimoradi, H., Shavandi, A. (2020). Fish collagen: Extraction, characterization, and applications for biomaterials engineering. Polymers, 12(10), 2230. [CrossRef]
  • 19. Oslan, S.N.H., Li, C.X., Shapawi, R., Mokhtar, R.A.M., Noordin, W.N.M., Huda, N. (2022). Extraction and characterization of bioactive fish by-product collagen as promising for potential wound healing agent in pharmaceutical applications: Current trend and future perspective. International Journal of Food Science, 2022, 9437878. [CrossRef]
  • 20. Rastian, Z., Putz, S., Wang, Y., Kumar, S., Fleissner F., Weidner T., Parekh, S.H. (2018). Type I collagen from jellyfish catostylus mosaicus for biomaterial applications. ACS Biomaterials Science & Engineering, 4(6), 2115-2125. [CrossRef]
  • 21. Ahmed, R., Haq, M., Chun, B.S. (2019). Characterization of marine derived collagen extracted from the by-products of bigeye tuna (Thunnus obesus). International Journal of Biological Macromolecules, 135, 668-676. [CrossRef]
  • 22. Sheng, Y., Wang, W.Y., Wu, M.F., Wang, Y.M., Zhu, W.Y., Chi, C.F., Wang, B. (2023). Eighteen novel bioactive peptides from monkfish (Lophius litulon) swim bladders: Production, identification, antioxidant activity, and stability. Marine. Drugs, 21(3), 169. [CrossRef]
  • 23. Cai, S.Y., Wang, Y.M., Zhao, Y.Q., Chi, C.F., Wang, B. (2019). Cytoprotective effect of antioxidant pentapeptides from the protein hydrolysate of swim bladders of miiuy croaker (Miichthys miiuy) against H(2)O(2)-mediated human umbilical vein endothelial cell (HUVEC) injury. International Journal of Molecular Sciences, 20(21), 5425. [CrossRef]
  • 24. Zheng, J., Tian, X., Xu, B., Yuan, F., Gong, J., Yang, Z. (2020). Collagen peptides from swim bladders of giant croaker (Nibea japonica) and their protective effects against H2O2-induced oxidative damage toward human umbilical vein endothelial cells. Marine Drugs, 18(8), 430. [CrossRef]
  • 25. Zhao, Y.Q., Zeng, L., Yang, Z.S., Huang, F.F., Ding, G.F., Wang, B. (2016). Anti-fatigue effect by peptide fraction from protein hydrolysate of croceine croaker (Pseudosciaena crocea) Swim bladder through inhibiting the oxidative reactions including DNA damage. Marine Drugs, 14(12), 221. [CrossRef]
  • 26. Singh, P., Benjakul, S., Maqsood, S., Kishimura, H. (2011). Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chemistry, 124(1), 97-105. [CrossRef]
  • 27. Zhu, J., Madhurapantula, R., Kalyanasundaram, A., Sabharwal, T., Antipova, O., Bishnoi, S., Orgel, J. (2020). Ultrastructural location and interactions of the immunoglobulin receptor binding sequence within fibrillar type I collagen. International Journal of Molecular Sciences, 21(11), 4166. [CrossRef]
  • 28. Hou, C., Li, N., Liu, M., Chen, J., Elango, J., Rahman, S.U., Bao, B., Wu, W. (2022). Therapeutic effect of nile tilapia type II collagen on rigidity in CD8+ cells by alleviating ınflammation and rheumatoid arthritis in rats by oral tolerance. Polymers, 14(7), 1284. [CrossRef]
  • 29. Xu, R., Zheng, L., Su, G., Luo, D., Lai, C., Zhao, M. (2021). Protein solubility, secondary structure and microstructure changes in two types of undenatured type II collagen under different gastrointestinal digestion conditions. Food Chemistry, 343, 128555. [CrossRef]
  • 30. Oliveira, V. de M., Assis, C.R.D., Costa, B. de A.M., Neri, R.C. de A., Monte, F.T.D., Freitas, H.M.S. da C.V., França, R.C.P., Santos, J.F., Bezerra, R. de S., Porto, A.L.F. (2021). Physical, biochemical, densitometric and spectroscopic techniques for characterization collagen from alternative sources: A review based on the sustainable valorization of aquatic by-products. Journal of Molecular Structure, 1224, 129023. [CrossRef]
  • 31. Bello, A.E., Oesser, S. (2006). Collagen hydrolysate for the treatment of osteoarthritis and other joint disorders: A review of the literature. Current Medical Research and Opinion, 22(11), 2221-2232. [CrossRef]
  • 32. Mukherjee, S., Sundarapandian, A., Ayyadurai, N., Shanmugam, G. (2023). Collagen mimicry with a short collagen model peptide. Macromolecular Rapid Communications, 45(4), 2300573. [CrossRef]
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ORAL COLLAGEN SUPPLEMENTS AND DETERMINATION OF THEIR POSSIBLE ADVERSE EFFECTS

Yıl 2024, , 1180 - 1188, 10.09.2024
https://doi.org/10.33483/jfpau.1423707

Öz

Objective: Many studies on oral collagen supplements to date are on the effects of collagen supplements on joint and skin health. The beneficial effects of collagen on other functions of the body are known, but studies are insufficient. Available data show that collagen supplements, which have become an important part of the daily diet by many people, do not show any toxic effects and are considered to be safe to use. However, due to the lack of supporting data, it is necessary to draw attention to the need for additional studies on the toxicity of collagen supplements despite their frequent use.
Result and Discussion: When the results of the literature reviews were examined, very little data on possible adverse effects were found. Long-term oral administration of specific collagen can cause harmful cellular damage in the body, weight loss, and disrupt the functions of target organs. It is necessary to have information about the contents of variable collagen sources and pay attention to their usage durations and amounts.

Kaynakça

  • 1. Ahmad, M. I., Li, Y., Pan, J., Liu, F., Dai, H., Fu, Y., Huang, T., Farooq, S., Zhang, H. (2024). Collagen and gelatin: Structure, properties, and applications in food industry. International Journal of Biological Macromolecules, 254(Pt 3), 128037. [CrossRef]
  • 2. Martínez-Puig, D., Costa-Larrión, E., Rubio-Rodríguez, N., Gálvez-Martín, P. (2023). Collagen supplementation for joint health: The link between composition and scientific knowledge. Nutrients, 15(6), 1332. [CrossRef]
  • 3. Biswal, S., Agmon, N. (2023). Collagen structured hydration. Biomolecules, 13(12), 1744. [CrossRef]
  • 4. Neltner, T.J., Sahoo, P.K., Smith, R.W., Anders, J.P.V., Arnett, J.E., Schmidt, R.J., Johnson, G.O., Natarajan, S.K., Housh, T.J. (2024). Effects of 8 weeks of shilajit supplementation on serum pro-c1α1, a biomarker of type 1 collagen synthesis: A randomized control trial. Journal of Dietary Supplements, 21(1), 1-12. [CrossRef]
  • 5. Anaya Mancipe, J.M., Boldrini Pereira, L.C., de Miranda Borchio, P.G., Dias, M.L., da Silva Moreira Thiré, R.M. (2023). Novel polycaprolactone (PCL)-type I collagen core-shell electrospun nanofibers for wound healing applications. Journal of Biomedical Materials Research: Part B, Applied Biomaterials, 111(2), 366-381. [CrossRef]
  • 6. Huang, Y., Gao, P., Qin, T., Chu, B., Xu, T., Yi, J., Wang, Q., Yang, Z., Jiang, T., Fan, J., Zhao, S., Zhou, W., Chen, J., Yin, G. (2023). Delayed inhibition of collagen deposition by targeting bone morphogenetic protein 1 promotes recovery after spinal cord injury. Matrix Biology: Journal of the International Society for Matrix Biology, 118, 69-91. [CrossRef]
  • 7. Kuttappan, S., Mathew, D., Nair, M.B. (2016). Biomimetic composite scaffolds containing bioceramics and collagen/gelatin for bone tissue engineering- A mini review. International Journal of Biological Macromolecules, 93, 1390-1401. [CrossRef]
  • 8. Fan, L., Ren, Y., Emmert, S., Vučković, I., Stojanovic, S., Najman, S., Schnettler, R., Barbeck, M., Schenke-Layland, K., Xiong, X. (2023). The use of collagen-based materials in bone tissue engineering. International Journal of Molecular Science, 24(4), 3744. [CrossRef]
  • 9. Tang C., Zhou K., Zhu Y., Zhang W., Xie Y., Wang Z., Zhou H., Yang T., Zhang Q., Xu B. (2022). Collagen and its derivatives: From structure and properties to their applications in food industry. Food Hydrocolloids, 131, 107748. [CrossRef]
  • 10. Nurilmala, M., Suryamarevita, H., Husein Hizbullah, H., Jacoeb, A.M., Ochiai, Y. (2022). Fish skin as a biomaterial for halal collagen and gelatin. Saudi Journal of Biological Sciences, 29(2), 1100-1110. [CrossRef]
  • 11. Hu, J., Li, J., Jiang, J., Wang, L., Roth, J., McGuinness, K. N., Baum, J., Dai, W., Sun, Y., Nanda, V., Xu, F. (2022). Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed. Nature Communications, 13(1), 6761. [CrossRef]
  • 12. Gómez-Guillén M.C., Giménez B., López-Caballero M.E., Montero M.P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25(8), 1813-1827. [CrossRef]
  • 13. Xu R., Zheng L., Su G., Luo D., Lai C., Zhao M. (2021). Protein solubility, secondary structure and microstructure changes in two types of undenatured type II collagen under different gastrointestinal digestion conditions. Food Chemistry, 343, 128555. [CrossRef]
  • 14. Zhang X., Zhang H., Toriumi S., Ura K., Takagi Y. (2020). Feasibility of collagens obtained from Bester Sturgeon Huso Huso × Acipenser Ruthenus for industrial use. Aquaculture, 529, 735641. [CrossRef]
  • 15. Zhang, H., Qi, L., Shen, Q., Wang, R., Guo, Y., Zhang, C., Richel, A. (2022). Comparative analysis of the bioactive compounds in chicken cartilage: Protective effects of chondroitin sulfate and type II collagen peptides against osteoarthritis involve gut microbiota. Frontiers in Nutrition, 9, 843360. [CrossRef]
  • 16. Arias J.L., Carrino D.A., Fernández M.S., Rodríguez J.P., Dennis J.E., Caplan A.I. (1992). Partial biochemical and immunochemical characterization of avian eggshell extracellular matrices. Archives of Biochemistry and Biophysics, 298(1), 293-302. [CrossRef]
  • 17. Oliveira, V. de M., Assis, C.R.D., Costa, B. de A.M., Neri, R.C. de A., Monte, F.T.D., Freitas, H.M.S. da C.V., França, R.C.P., Santos, J.F., Bezerra, R. de S., Porto, A.L.F. (2021). Physical, biochemical, densitometric and spectroscopic techniques for characterization collagen from alternative sources: A review based on the sustainable valorization of aquatic by-products. Journal of Molecular Structure, 1224, 129023. [CrossRef]
  • 18. Jafari, H., Lista, A., Siekapen, M.M., Ghaffari-Bohlouli, P., Nie, L., Alimoradi, H., Shavandi, A. (2020). Fish collagen: Extraction, characterization, and applications for biomaterials engineering. Polymers, 12(10), 2230. [CrossRef]
  • 19. Oslan, S.N.H., Li, C.X., Shapawi, R., Mokhtar, R.A.M., Noordin, W.N.M., Huda, N. (2022). Extraction and characterization of bioactive fish by-product collagen as promising for potential wound healing agent in pharmaceutical applications: Current trend and future perspective. International Journal of Food Science, 2022, 9437878. [CrossRef]
  • 20. Rastian, Z., Putz, S., Wang, Y., Kumar, S., Fleissner F., Weidner T., Parekh, S.H. (2018). Type I collagen from jellyfish catostylus mosaicus for biomaterial applications. ACS Biomaterials Science & Engineering, 4(6), 2115-2125. [CrossRef]
  • 21. Ahmed, R., Haq, M., Chun, B.S. (2019). Characterization of marine derived collagen extracted from the by-products of bigeye tuna (Thunnus obesus). International Journal of Biological Macromolecules, 135, 668-676. [CrossRef]
  • 22. Sheng, Y., Wang, W.Y., Wu, M.F., Wang, Y.M., Zhu, W.Y., Chi, C.F., Wang, B. (2023). Eighteen novel bioactive peptides from monkfish (Lophius litulon) swim bladders: Production, identification, antioxidant activity, and stability. Marine. Drugs, 21(3), 169. [CrossRef]
  • 23. Cai, S.Y., Wang, Y.M., Zhao, Y.Q., Chi, C.F., Wang, B. (2019). Cytoprotective effect of antioxidant pentapeptides from the protein hydrolysate of swim bladders of miiuy croaker (Miichthys miiuy) against H(2)O(2)-mediated human umbilical vein endothelial cell (HUVEC) injury. International Journal of Molecular Sciences, 20(21), 5425. [CrossRef]
  • 24. Zheng, J., Tian, X., Xu, B., Yuan, F., Gong, J., Yang, Z. (2020). Collagen peptides from swim bladders of giant croaker (Nibea japonica) and their protective effects against H2O2-induced oxidative damage toward human umbilical vein endothelial cells. Marine Drugs, 18(8), 430. [CrossRef]
  • 25. Zhao, Y.Q., Zeng, L., Yang, Z.S., Huang, F.F., Ding, G.F., Wang, B. (2016). Anti-fatigue effect by peptide fraction from protein hydrolysate of croceine croaker (Pseudosciaena crocea) Swim bladder through inhibiting the oxidative reactions including DNA damage. Marine Drugs, 14(12), 221. [CrossRef]
  • 26. Singh, P., Benjakul, S., Maqsood, S., Kishimura, H. (2011). Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chemistry, 124(1), 97-105. [CrossRef]
  • 27. Zhu, J., Madhurapantula, R., Kalyanasundaram, A., Sabharwal, T., Antipova, O., Bishnoi, S., Orgel, J. (2020). Ultrastructural location and interactions of the immunoglobulin receptor binding sequence within fibrillar type I collagen. International Journal of Molecular Sciences, 21(11), 4166. [CrossRef]
  • 28. Hou, C., Li, N., Liu, M., Chen, J., Elango, J., Rahman, S.U., Bao, B., Wu, W. (2022). Therapeutic effect of nile tilapia type II collagen on rigidity in CD8+ cells by alleviating ınflammation and rheumatoid arthritis in rats by oral tolerance. Polymers, 14(7), 1284. [CrossRef]
  • 29. Xu, R., Zheng, L., Su, G., Luo, D., Lai, C., Zhao, M. (2021). Protein solubility, secondary structure and microstructure changes in two types of undenatured type II collagen under different gastrointestinal digestion conditions. Food Chemistry, 343, 128555. [CrossRef]
  • 30. Oliveira, V. de M., Assis, C.R.D., Costa, B. de A.M., Neri, R.C. de A., Monte, F.T.D., Freitas, H.M.S. da C.V., França, R.C.P., Santos, J.F., Bezerra, R. de S., Porto, A.L.F. (2021). Physical, biochemical, densitometric and spectroscopic techniques for characterization collagen from alternative sources: A review based on the sustainable valorization of aquatic by-products. Journal of Molecular Structure, 1224, 129023. [CrossRef]
  • 31. Bello, A.E., Oesser, S. (2006). Collagen hydrolysate for the treatment of osteoarthritis and other joint disorders: A review of the literature. Current Medical Research and Opinion, 22(11), 2221-2232. [CrossRef]
  • 32. Mukherjee, S., Sundarapandian, A., Ayyadurai, N., Shanmugam, G. (2023). Collagen mimicry with a short collagen model peptide. Macromolecular Rapid Communications, 45(4), 2300573. [CrossRef]
  • 33. Fields, G.B., Prockop, D.J. (1996). Perspectives on the synthesis and application of triple-helical, collagen-model peptides. Biopolymers, 40(4), 345-357. [CrossRef]
  • 34. Takahashi, S., Zhao, M., Eng, C. (1991). Isolation and characterization of insoluble collagen of dog hearts. Protein Expression and Purification, 2(4), 304-312.[CrossRef]
  • 35. Park, K.S., Park, M.J., Cho, M.L., Kwok, S.K., Ju, J.H., Ko, H.J., Park, S.H., Kim, H.Y. (2009). Type II collagen oral tolerance; mechanism and role in collagen-induced arthritis and rheumatoid arthritis. Modern Rheumatology, 19(6), 581-589. [CrossRef]
  • 36. Valcarcel, J., Fraguas, J., Hermida-Merino, C., Hermida-Merino, D., Piñeiro, M.M., Vázquez, J.A. (2021). Production and physicochemical characterization of gelatin and collagen hydrolysates from turbot skin waste generated by aquaculture activities. Marine Drugs, 19(9), 491. [CrossRef]
  • 37. Nur Hanani, Z.A., Roos, Y.H., Kerry, J.P. (2014). Use and application of gelatin as potential biodegradable packaging materials for food products. International Journal of Biological Macromolecules, 71, 94-102. [CrossRef]
  • 38. Sibilla, S., Godfrey, M., Brewer, S., Budh-Raja, A., Genovese, L. (2015). An overview of the beneficial effects of hydrolysed collagen as a nutraceutical on skin properties: Scientific background and clinical studies. The Open Nutraceuticals Journal, 8(1), 29-42. [CrossRef]
  • 39. Khavkin, J., Ellis, D.A.F. (2011). Aging skin: Histology, physiology, and pathology. Facial Plastic Surgery Clinics of North America, 19(2), 229-234. [CrossRef]
  • 40. Sparavigna, A. (2020). Role of the extracellular matrix in skin aging and dedicated treatment-State of the art. Plastic and Aesthetic Research, 2020. [CrossRef]
  • 41. Krutmann, J., Bouloc, A., Sore, G., Bernard, B. A., Passeron, T. (2017). The skin aging exposome. Journal of Dermatological Science, 85(3), 152-161. [CrossRef]
  • 42. Campos, L.D., Santos Junior, V.A., Pimentel, J.D., Carregã, G.L.F., Cazarin, C.B.B. (2023). Collagen supplementation in skin and orthopedic diseases: A review of the literature. Heliyon, 9(4), e14961. [CrossRef]
  • 43. Harvard edu web site. (2021). Erişim adresi https://www.hsph.harvard.edu/nutritionsource/collagen/. Erişim tarihi: 20.05.2021.
  • 44. Lima, L., Quintal, T., Soares, T., Ribeiro, C., Silva, L., Lima, E., Vieira, L., Barbosa, A. (2022). Evidence on the biomodulatory potential of oral collagen peptide supplementation for skin aging: Composition, mechanism of action, bioavailability, eficacy and toxicity. Acta Farmacêutica Portuguesa, 82-96.
  • 45. Kudayer, A., Alwan, N., Sawad, A. (2020). A chronic toxicity study of oral administration of collagen-α ® supplement using pregnant rabbits. Indian Journal of Forensic Medicine and Toxicology. 14. 930-935.
  • 46. Yamamoto, K., Igawa, K., Sugimoto, K., Yoshizawa, Y., Yanagiguchi, K., Ikeda, T., Yamada, S., Hayashi, Y. (2014). Biological safety of fish (tilapia) collagen. BioMed Research International, 2014, 630757. [CrossRef]
  • 47. Jabbari, M., Barati, M., Khodaei, M., Babashahi, M., Kalhori, A., Tahmassian, A. H., Mosharkesh, E., Arzhang, P., Eini-Zinab, H. (2022). Is collagen supplementation friend or foe in rheumatoid arthritis and osteoarthritis? A comprehensive systematic review. International Journal of Rheumatic Diseases, 25(9), 973-981. [CrossRef]
  • 48. Kim, J., Lee, S.G., Lee, J., Choi, S., Suk, J., Lee, J.H., Yang, J.H., Yang, J.S., Kim, J. (2022). Oral supplementation of low-molecular-weight collagen peptides reduces skin wrinkles and improves biophysical properties of skin: A randomized, double-blinded, placebo-controlled study. Journal of Medicinal Food, 25(12), 1146-1154. [CrossRef]
  • 49. Nishikimi, A., Koyama, Y.I., Ishihara, S., Kobayashi, S., Tometsuka, C., Kusubata, M., Kuwaba, K., Hayashida, O., Hattori, S., Katagiri, K. (2018). Collagen-derived peptides modulate CD4+ T-cell differentiation and suppress allergic responses in mice. Immunity, Inflammation and Disease, 6(2), 245-255. [CrossRef]
  • 50. Kuzan, A., Smulczyńska-Demel, A., Chwiłkowska, A., Saczko, J., Frydrychowski, A., Dominiak, M. (2015). An estimation of the biological properties of fish collagen in an experimental in vitro study. Advances in Clinical and Experimental Medicine: Official Organ Wroclaw Medical University, 24(3), 385-392. [CrossRef]
  • 51. Seo, H.S., Kim, J.H., Kim, S.H., Park, M.K., Seong, N.W., Kang, G.H., Kim, J.S., Kim, S.H., Kim, J.C., Moon, C. (2023). Toxicity of a 90-day repeated oral dose of a collagen peptide derived from skate (Raja kenojei) skin: A rat model study. Toxicological Research, 39(3), 383-398. [CrossRef]
Toplam 51 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Konular Farmasotik Toksikoloji
Bölüm Derleme
Yazarlar

Senanur Özsoy 0009-0002-8165-6847

Özge Cemiloğlu Ülker 0000-0002-8549-2993

Aylin Üstündağ 0000-0002-8449-1358

Erken Görünüm Tarihi 24 Temmuz 2024
Yayımlanma Tarihi 10 Eylül 2024
Gönderilme Tarihi 22 Ocak 2024
Kabul Tarihi 14 Haziran 2024
Yayımlandığı Sayı Yıl 2024

Kaynak Göster

APA Özsoy, S., Cemiloğlu Ülker, Ö., & Üstündağ, A. (2024). ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ. Journal of Faculty of Pharmacy of Ankara University, 48(3), 1180-1188. https://doi.org/10.33483/jfpau.1423707
AMA Özsoy S, Cemiloğlu Ülker Ö, Üstündağ A. ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ. Ankara Ecz. Fak. Derg. Eylül 2024;48(3):1180-1188. doi:10.33483/jfpau.1423707
Chicago Özsoy, Senanur, Özge Cemiloğlu Ülker, ve Aylin Üstündağ. “ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ”. Journal of Faculty of Pharmacy of Ankara University 48, sy. 3 (Eylül 2024): 1180-88. https://doi.org/10.33483/jfpau.1423707.
EndNote Özsoy S, Cemiloğlu Ülker Ö, Üstündağ A (01 Eylül 2024) ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ. Journal of Faculty of Pharmacy of Ankara University 48 3 1180–1188.
IEEE S. Özsoy, Ö. Cemiloğlu Ülker, ve A. Üstündağ, “ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ”, Ankara Ecz. Fak. Derg., c. 48, sy. 3, ss. 1180–1188, 2024, doi: 10.33483/jfpau.1423707.
ISNAD Özsoy, Senanur vd. “ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ”. Journal of Faculty of Pharmacy of Ankara University 48/3 (Eylül 2024), 1180-1188. https://doi.org/10.33483/jfpau.1423707.
JAMA Özsoy S, Cemiloğlu Ülker Ö, Üstündağ A. ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ. Ankara Ecz. Fak. Derg. 2024;48:1180–1188.
MLA Özsoy, Senanur vd. “ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ”. Journal of Faculty of Pharmacy of Ankara University, c. 48, sy. 3, 2024, ss. 1180-8, doi:10.33483/jfpau.1423707.
Vancouver Özsoy S, Cemiloğlu Ülker Ö, Üstündağ A. ORAL KOLAJEN TAKVİYELERİ VE OLASI ADVERS ETKİLERİNİN DEĞERLENDİRİLMESİ. Ankara Ecz. Fak. Derg. 2024;48(3):1180-8.

Kapsam ve Amaç

Ankara Üniversitesi Eczacılık Fakültesi Dergisi, açık erişim, hakemli bir dergi olup Türkçe veya İngilizce olarak farmasötik bilimler alanındaki önemli gelişmeleri içeren orijinal araştırmalar, derlemeler ve kısa bildiriler için uluslararası bir yayım ortamıdır. Bilimsel toplantılarda sunulan bildiriler supleman özel sayısı olarak dergide yayımlanabilir. Ayrıca, tüm farmasötik alandaki gelecek ve önceki ulusal ve uluslararası bilimsel toplantılar ile sosyal aktiviteleri içerir.