Derleme
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Yıl 2020, Cilt: 15 Sayı: 1, 24 - 35, 31.01.2020

Öz

Kaynakça

  • [1] Yang, H. and Shu, Z., (2014). The Extraction of Collagen Protein From Pig Skin. Journal of Chemical and Pharmaceutical Research, 6(2):683-687.
  • [2] Alberts, B., Bray, D., Lewıs, J., Raff, M., Roberts, K., and Watson, J.D., (1995). Molekularbiologie der Zelle. CH-Verlagsgesellschaft, Weinheim, 3. Auflage, Kap. 4, 7, 12.5, 16.5.6, 16.5.7, 19.3.8-22.7.
  • [3] Ferraro, V., Martinie, B.G., Sayd, T., Chambon, C., Anton, M., and Lhoutellier, V.S., (2017). Collagen Type I from Bovine Bone. Effect of Animal Age, Bone Anatomy and Drying Methodology on Extraction Yield, Self-Assembly, Thermal Behaviour And Electrokinetic Potential. International Journal of Biological Macromolecules.97:55–66.
  • [4] Song, H. and Li, B., (2017). Beneficial Effects of Collagen Hydrolysate: A Review on Recent Developments. Biomedical Journal of Scientific and Technical Research, 1(2):1-4.
  • [5] Lafarga, T. and Hayes, M., (2014). Bioactive Peptides from Meat Muscle and By-Products: Generation, Functionality and Application As Functional İngredients. Meat Science, 98(2):227-239.
  • [6] Schmidt, M.M., Dornelles, R.C.P., Mello, R.O., Kubota, E.H., Mazutti, M.A., Kempka, A.P., and Demiate, I.M., (2016). Collagen Extraction Process. International Food Research Journal, 23(3):913-922.
  • [7] Damodaran S., Parkin, K., and Fennema, O.R., (2010). Química de al imentos de fennema. p. 726-730. 4ª ed. São Paulo: Artmed.
  • [8] Cheng, F.Y., Hsu, F.W., Chang, H.S., Lin, L.C., and Sakata, R., (2009). Effect of Different Acids on the Extraction of Pepsin-Solubilised Collagen Containing Melanin From Silky Fowl Feet. Food Chemistry. 113(2):563-567.
  • [9] Ehrlich, H., Wysokowski, M., Żółtowska-Aksamitowska, S., Petrenko, I., and Jesionowski, T., (2018). Collagens of Poriferan Origin. Marine drugs.
  • [10] Li, P. and Wu, G., (2018). Roles of Dietary Glycine, Proline, and Hydroxyproline in Collagen Synthesis and Animal Growth. Amino Acids, 50(1):29-38.
  • [11] Szpak, P., (2011). Fish Bone Chemistry and Ultrastructure: Implications for Taphonomy and Stable İsotope Analysis. Journal of Archaeological Science. 38(12):3358–3372.
  • [12] Temel, B., (2006). Doğal ve Sentetik Biomateryallerde, Osteogenic (rhBMP-7) ve Angiogenic (bFGF) Büyüme Faktörleri İle İnsan Osteoblast Hücrelerinin Gelişiminin İncelenmesi. Yüksek Lisans Tezi. Çukurova Üniversitesi. s.54.
  • [13] Miller, A., (1984). Philosophical Transactions of the Royal Society. 11, 304. 4% -477.
  • [14] Khan, R., Khan, M.H., and Bey, A., (2011). Use of collagen as an Implantable Material in The Reconstructive Procedures, an overview. Biol Med. 3:25-32.
  • [15] Poole, A.R., Kobayashi, M., Yasuda, T., Laverty, S., Mwale, F., Kojima, T., Sakai, T., Wahl, C., El Maadawy, S., Webb, G., and Tchetina, E., (2002). Type II Collagen Degradation and Its Regulation in Articular Cartilage in Osteoarthritis. Annals of the rheumatic diseases, 61(suppl 2), 78-81.
  • [16] Gupta, R., Canerdy, T., Skaggs, P., Stocker, A., Zyrkowski, G., Burke, R., Wegford, K., Goad, J.T., Rohde, K., Barnett, D., DeWees, W., Bagchi, M., and Bagchi, D., (2009). Therapeutic Efficacy of Undenatured Type-II Collagen (UC-II) in Comparison to Glucosamine and Chondroitin in Arthritic Horses. Vet Pharmacol Ther. 32:577-584.
  • [17] Howkins, A., (2015). Elucidation of Porcine Corneal Ultrastructure to Inform Development of Corneal Xenografts or Biomimetic Replacements.
  • [18] Birmingham, J., Vilim, V., and Kraus, V., (2007). Collagen Biomarkers for Arthritis Application. Biomarkers insights. 1:61-76. PMCID: PMC2716783.
  • [19] Banu, N., Hotoshi, H., Shinukuro, K., and Genshi, E., (1994). A Novel Method for Concentrating Urinary Type IV collagen based on participation with polyethylene glycol: application to its measurement by enzyme immunoassay. Ann Clin Biochem.31:485-491.
  • [20] Lamandé, S.R. and Bateman, J.F.,(2018). Collagen VI Disorders: Insights on form and Function in the Extracellular Matrix and Beyond. Matrix Biology, 71, 348-367.
  • [21] Woodley, D., Keene, D., Atha, T., Huang, Y., Lipman, K., Li, W., Chen, M.,(2004). Injection of Recombinant Human Type VII Collagen Restores Collagen Function on Dystrophic Epidermolysis Bullosa. Nat Med.10:693-695.
  • [22] Gelse, K., Poschl, E., and Aigner, T., (2003). Collagens-Structure, Function, And Biosynthesis. Adv Drug Deliv Rev. 55:1531-1546.
  • [23] Wotton, S., Duance, V., and Fryer, P., (1988). Type IX Collagen: a Possible Function in Articular Cartilage. FEBS Lett. 234:79-82.
  • [24] Ricard-Blum, S., (2010). The Collagen Family. Cold Spring Harbor Perspectives in Biology. 3:a004978.
  • [25] Karsdal, M., (2016). Biochemistry of Collagens Structure, Function and Biomarkers. London, United Kingdom: Academic Press.
  • [26] Brinckmann, J.C.B.C., Notbohm, H., Muller, P.K., and Bachinger, H.P., (2005). Collagen: Primer in Structure, Processing and Assembly. Berlin, Germany: Springer:56.
  • [27] Royce, P.M. and Steinmann, B., (2003). Connective Tissue and Its Heritable Disorders: Molecular, Genetic, and Medical Aspects. New York: Wiley.
  • [28] Fratzl, P., (2008). Collagen: Structure and Mechanics. New York: Springer. p 1-496.
  • [29] Buehler, M.J., (2006). Nature Designs Tough Collagen: Explaining the Nanostructure of Collagen Fibrils. PNAS. 103(33):12285-2290.
  • [30] Morimura, S., Nagata, H., Uemura, Y., Fahmi, A., Shigematsu, T., and Kida, K., (2002). Development of an Effective Process for Utilization of Collagen from Livestock And Fish Waste. Process Biochemistry, 37, 1403–1412.
  • [31] Yapar, E.A. and Tanrıverdi, S.T., (2016). Yaşlanma Karşıtı Kozmetik Yaklaşımlar ve Ürün Bileşenleri. Balıkesir Sağlık Bilimleri Dergisi, 5(2):99-109.
  • [32] Kim, S., (2012). Marine cosmeceuticals Trends and Prospects. Taylor and Francis Group, New York, 397s.
  • [33] Kim, S.K. and Mendis, E., (2006). Bioactive Compounds from Marine Processing Byproducts–A Review. Food Research International, 39(4):383-393.
  • [34] Leitinger, B. and Hohenester, E., (2007). Mammalian Collagen Receptors. Matrix Biology. 26:146-155.
  • [35] Oliveira, S., Ringshia, R., Legeros, R., Clark, E., Terracio, L., Teixeira, C., and Yost, M., (2009). An Improved Collagen Scaffold for Skeletal Regeneration. Journal of Biomedical Materials, 94(2):371-379.
  • [36] Parenteau-Bareil, R., Gauvin, R., and Berthod, F., (2010). Collagen-Based Biomaterials for Tissue Engineering Applications. Materials, 3, 1863-1887.
  • [37] Badylak, S.F., (2004). Xenogeneic Extracellular Matrix as a Scaffold for Tissue Reconstruction. Transplant Immunology, 12, 367-377.
  • [38] Gingras, M, Beaulieu, M.M., Gagnon V., Durham H.D., and Berthod F., (2008). In Vitro Study of Axonal Migration and Myelination of Motor Neurons in a Three-Dimensional Tissue Engineered Model. Glia, 56: 354-364.
  • [39] Che, Z.M., Jung, T.H., Choi, J.H., Yoon-do, J., Jeong, H.J., Lee, E.J., and Kim, J., (2006). Collagen Based Co-culture for Invasive Study on Cancer Cells-Fibroblasts Interaction. Biochemical and Biophysical Research Communications. 346:268-275.
  • [40] Sanz-Herrera J.A. and Reina-Romo, E., (2011). Cell-Biomaterial Mechanical Interaction in the Framework of Tissue Engineering: Insights, Computational Modeling and Perspectives. International Journal of Molecular Sciences, 12, 8217-8244.
  • [41] Cunniffe, G.M. and Brien, F.J.O., (2011). Collagen Scaffolds for Orthopedic Regenerative Medicine. The Journalof the Minerals, Metals and Materials Society, 63(4):66-73. [42] Rose, F.R. and Oreffo, R.O., (2002). Bone Tissue Engineering: Hope VS Hype. Biochemical and Biophysical Research Communications 292:1-7.
  • [43] Gökalp, M., (2006). Doğu Akdeniz-Ege Süngerlerinden (Porifera) Seçilen Türlerin İncelenmesi, Bu Canlılardaki Kolajen Tip II, IV ve İntegrin β1 Proteinlerinin Varlığının İmmünohistokimyasal ve Moleküler Genetik Düzeyde Araştırılması. Ankara Üniversitesi. Yüksek Lisans Tezi. s. 90.
  • [44] Orgel, J., Sella, I., Madhurapantula, R.S., Antipova, O., Mandelberg, Y., Kashman, Y., and Benayahu, Y., (2017). Molecular and Ultrastructural Studies of a Fibrillar Collagen from Octocoral (Cnidaria). The Journal of Experimental Biology, 220(Pt 18), 3327–3335.
  • [45] Stabili, L., Schirosi, R., Parisi, M., Piraino, S., and Cammarata, M., (2015). The Mucus of Actinia Equina (Anthozoa, Cnidaria): An Unexplored Resource for Potential Applicative Purposes. Marine drugs, 13(8):5276-5296.
  • [46] Addad, S., Exposito, J., Faye, C., Ricard-Blum, S., and Lethias, C., (2011). Isolation, Characterization and Biological Evaluation of Jellyfish Collagen for Use in Biomedical Applications. Marine drugs.
  • [47] Kantarcıoğlu, İ., (2017). Denizanası Kolajeni/Misvak Hibrit Membranların Üretimi ve Periodontal Doku Grefti Olarak Kullanımının Araştırılması. Çanakkale Onsekiz Mart Üniversitesi. Yüksek Lisans Tezi. s. 58.
  • [48] Pallela, R., Bojja, S., and Janapala, V.R., (2011). Biochemical and Biophysical Characterization of Collagens of Marine Sponge, Ircinia fusca (Porifera: Demospongiae: Irciniidae). International journal of Biological Macromolecules, 49(1):85-92.
  • [49] Miura, S. and Kimura, S., (1985). Jellyfish Mesogloea Collagen. Characterization of Molecules as a1a2a3 heterotetramers. Journal of Biological Chemistry, 260, 15352-15356.
  • [50] Nagai, T., Ogawa, T., Nakamura, T., Ito, T., Nakagawa, H., Fujiki, K., Nakao, M., and Yano, T., (1999). Collagen of Edible Jellyfish Exumbrella. Journal of the Science of Food and Agriculture, 79, 855-858.
  • [51] Rerk-am, U., Chawananorasest, K., Kongsombat, B., Tanstirapakdee, S., Sematong, T., and Thubthimthed, S., (2016). Extraction and Characterization of Collagen from the White Jellyfish (Lobonema smithi Mayer.). European Chemistry Congress, Rome, Italy.
  • [52] Felician, F.F., Yu, R.H., Li, M.Z., Li, C.J., Chen, H.Q., Jiang, Y., Tang, T., Qi, W.Y., and Xu, H.M., (2019). The Wound Healing Potential of Collagen Peptides Derived from The Jellyfish Rhopilema Esculentum. Chinese Journal of Traumatology, 22(1):12-20.
  • [53] Cheng, X., Shao, Z., Li, C., Yu, L., Raja, M.A., and Liu, C., (2017). Isolation, Characterization and Evaluation of Collagen from Jellyfish Rhopilema Esculentum Kishinouye for Use in Hemostatic Applications. Plos one, 12(1):e0169731.
  • [54] Barzideh, Z., Latiff, A.A., Gan, C.Y., Benjakul, S., and Karim, A.A., (2014). Isolation and Characterisation of Collagen from the Ribbon Jellyfish (Chrysaora sp.). International Journal of Food Science and Technology, 49(6):1490-1499.
  • [55] Hsieh, Y.H.P., (2005). Use of Jellyfish Collagen (Type II) in the Treatment of Rheumatoid Arthritis. No. 6,894,029. US Patent.
  • [56] Rastian, Z., Pütz, S., Wang, Y., Kumar, S., Fleissner, F., Weidner, T., and Parekh, S.H., (2018). Type I Collagen from Jellyfish Catostylus Mosaicus for Biomaterial Applications. ACS Biomaterials Science & Engineering, 4(6):2115-2125.
  • [57] Zhang, J., Duan, R., Huang, L., Song, Y., and Regenstein, J.M., (2014). Characterisation of Acid Soluble and Pepsin-solubilised Collagen from Jellyfish (Cyanea nozakii Kishinouye). Food Chemistry, 150:22–26.
  • [58] Kramer, J.M., (1994). Structures and Functions of Collagens in Caenorhabditis Elegans. The FASEB Journal, 8(3):329-336.
  • [59] Jridi, M., Bardaa, S., Moalla, D., Rebaii, T., Souissi, N., Sahnoun, Z., Nasri, M.,(2015). Microstructure, Rheological and Wound Healing Properties of Collagen-based gel from Cuttlefish Skin. International journal of biological macromolecules, 77, 369-374.
  • [60] Schmut, O., Roll, P., Reich, M.E., and Palm, W., (1980). Biochemical and Electronmicroscopic Investigations on Helix pomatia Collagen. Zeitschrift für Naturforschung C, 35:376-379.
  • [61] Wu, J., Guo, X., Liu, H., and Chen, L., (2019). Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata). Foods.
  • [62] Dyachuk, V., (2018). Extracellular Matrix Components in Bivalvia: Shell and ECM Components in Developmental and Adult Tissues. Fisheries and Aquaculture Journal. 9(2), 1a-1a.
  • [63] Kimura, S., Takema, Y., and Kubota, M., (1981). Octopus Skin Collagen. Isolation and Characterization of Collagen Comprising Two Distinct Alpha Chains. Journal of Biological Chemistry. 25;256(24):13230-13234.
  • [64] Shanmugam, V., Ramasamy, P., Subhapradha, N., Sudharsan, S., Seedevi, P., Moovendhan, M., Krishnamoorthy, J., Shanmugam, A., and Srinivasan, A., (2012).
  • Extraction, Structural and Physical Characterization of Type I Collagen from the Outer Skin of Sepiella Inermis. African Journal of Biotechnology, 11(78):14326-14337.
  • [65] Shanmugam, A., Ramasamy, P., Bharti, M.K., Saravanan, R., Subhapradha, N., Vairamani, S., and Jayalakshmi, K., (2011). Isolation and Characterization of Collagen from the skin of Sepia pharaonis (Ehrenberg, 1831). International Journal of Current Research. 33(6):107-111.
  • [66] Bairati, A. and Gioria, M., (2004). Collagen Fibrils of an Invertebrate (Sepia officinalis) are Heterotypic: Immunocytochemical Demonstration. Journal of structural biology, 147(2):159-165.
  • [67] Balti, R., Jridi, M., Sila, A., Souissi, N., Nedjar-Arroume, N., Guillochon, D., and Nasri, M., (2011). Extraction and Functional Properties of Gelatin from the skin of Cuttlefish (Sepia officinalis) Using Smooth Hound Crude Acid Protease-Aided Process. Food Hydrocolloids, 25(5):943-950.
  • [68] Jose, H.M.P.M., Murugesan, P., Arumugam, M., and Kumar, K.M., (2014). Isolation and Characterization of Acid and Pepsin-solubilised Collagen from the Muscle of Mantis Shrimp (Oratosquilla nepa). International Journal of Pharmacy and Pharmaceutical Sciences, 6(1), 14.
  • [69] Mizuta, S., Yoshinaka, R., Sato, M., and Sakaguchi, M., (1994). Characterization of Collagen in Muscle of Several Crustacean Species. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 107(2):365-370.
  • [70] Sivakumar, P., Suguna, L., and Chandrakasan, G., (2000). Molecular Species of Collagen in the Intramuscular Connective Tissues of the Marine Crab, Scylla Serrata. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 125(4):555-562.
  • [71] Yoshinaka, R., Mizuta, S., Itoh, Y., and Sato, M., (1990). Two Genetically Distinct Types of Collagen in Kuruma Prawn Penaeus Japonicus. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 96(3):451-456.
  • [72] Golob, R., Chetsanga, C.J., and Doty, P., (1974). The Onset of Collagen Synthesis in Sea Urchin Embryos. Biochimica et Biophysica Acta (BBA)-Nucleic Acids and Protein Synthesis, 349(1):135-141.
  • [73] Wijanarko, A., Januardi, Ginting, M., Sahlan, M., Krisanta Endah Savitri, I., Florensia, Y., Regina-Sudiarta, M., and Hermansyah, H., (2017). Saponin Isolation as Main Ingredients of Insecticide and Collagen Type I from Crown of Thorn-Starfish (Acanthaster planci). IOP Conference Series: Earth and Environmental Science, 89(1).
  • [74] Kimura, S., Omura, Y., Ishida, M., and Shirai, H., (1993). Molecular Characterization of Fibrillar Collagen from the Body Wall of Starfish Asterias Amurensis. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 104(4):663-668.
  • [75] Siddiqui, Y.D., Arief, E.M., Yusoff, A., and Suzina, A.H., (2013). Isolation of Pepsın-Solubilized Collagen (Psc) from Crude Collagen Extracted from Body Wall of Sea Cucumber (Bohadschıa spp.)
  • [76] El-Rashidy, A.A., Gad, A., Abu-Hussein, A.E.G., and Habib, S.I., (2015). Chemical and Biological Evaluation of Egyptian Nile Tilapia (Oreochromis niloticas) Fish Scale Collagen. International Journal of Biological Macromolecules. 79:618–626.

Denizel Omurgasız Canlılardan Elde Edilen Kolajenler ve Kullanım Alanları

Yıl 2020, Cilt: 15 Sayı: 1, 24 - 35, 31.01.2020

Öz

Kolajen tüm canlılarda mevcut olan
bir protein molekülüdür. Kolajen kaynakları arasında su ürünlerinden elde
edilen kolajen, yüksek ürün eldesi, biyo-uyumluluk, yüksek işlenebilirlik ve herhangi
bir hastalık riski taşımaması gibi sahip olduğu avantajlı özelliklerinden
dolayı karasal kökenli kolajenlerin en iyi alternatifidir. Sadece balık ve
balık ürünlerinden ibaret olmayan denizel canlılardan omurgasızlar da iyi birer
kolajen kaynağıdırlar. Denizel omurgasızların medikal, tıp, biyomedikal,
farmakoloji, doku mühendisliği ve malzeme mühendisliği gibi birçok alanda ham
madde olarak kullanılması mümkündür.
Bu derleme çalışmasında,
kolajen, kolajenin özellikleri, kolajenin yapısı ve tipleri ile ilgili
bilgilerin yanı sıra, denizel omurgasız canlılardan elde edilen kolajenler ve
bu kolajenlerin kullanım alanları hakkında son yıllarda yapılmış olan
çalışmalar derlenmiştir. 

Kaynakça

  • [1] Yang, H. and Shu, Z., (2014). The Extraction of Collagen Protein From Pig Skin. Journal of Chemical and Pharmaceutical Research, 6(2):683-687.
  • [2] Alberts, B., Bray, D., Lewıs, J., Raff, M., Roberts, K., and Watson, J.D., (1995). Molekularbiologie der Zelle. CH-Verlagsgesellschaft, Weinheim, 3. Auflage, Kap. 4, 7, 12.5, 16.5.6, 16.5.7, 19.3.8-22.7.
  • [3] Ferraro, V., Martinie, B.G., Sayd, T., Chambon, C., Anton, M., and Lhoutellier, V.S., (2017). Collagen Type I from Bovine Bone. Effect of Animal Age, Bone Anatomy and Drying Methodology on Extraction Yield, Self-Assembly, Thermal Behaviour And Electrokinetic Potential. International Journal of Biological Macromolecules.97:55–66.
  • [4] Song, H. and Li, B., (2017). Beneficial Effects of Collagen Hydrolysate: A Review on Recent Developments. Biomedical Journal of Scientific and Technical Research, 1(2):1-4.
  • [5] Lafarga, T. and Hayes, M., (2014). Bioactive Peptides from Meat Muscle and By-Products: Generation, Functionality and Application As Functional İngredients. Meat Science, 98(2):227-239.
  • [6] Schmidt, M.M., Dornelles, R.C.P., Mello, R.O., Kubota, E.H., Mazutti, M.A., Kempka, A.P., and Demiate, I.M., (2016). Collagen Extraction Process. International Food Research Journal, 23(3):913-922.
  • [7] Damodaran S., Parkin, K., and Fennema, O.R., (2010). Química de al imentos de fennema. p. 726-730. 4ª ed. São Paulo: Artmed.
  • [8] Cheng, F.Y., Hsu, F.W., Chang, H.S., Lin, L.C., and Sakata, R., (2009). Effect of Different Acids on the Extraction of Pepsin-Solubilised Collagen Containing Melanin From Silky Fowl Feet. Food Chemistry. 113(2):563-567.
  • [9] Ehrlich, H., Wysokowski, M., Żółtowska-Aksamitowska, S., Petrenko, I., and Jesionowski, T., (2018). Collagens of Poriferan Origin. Marine drugs.
  • [10] Li, P. and Wu, G., (2018). Roles of Dietary Glycine, Proline, and Hydroxyproline in Collagen Synthesis and Animal Growth. Amino Acids, 50(1):29-38.
  • [11] Szpak, P., (2011). Fish Bone Chemistry and Ultrastructure: Implications for Taphonomy and Stable İsotope Analysis. Journal of Archaeological Science. 38(12):3358–3372.
  • [12] Temel, B., (2006). Doğal ve Sentetik Biomateryallerde, Osteogenic (rhBMP-7) ve Angiogenic (bFGF) Büyüme Faktörleri İle İnsan Osteoblast Hücrelerinin Gelişiminin İncelenmesi. Yüksek Lisans Tezi. Çukurova Üniversitesi. s.54.
  • [13] Miller, A., (1984). Philosophical Transactions of the Royal Society. 11, 304. 4% -477.
  • [14] Khan, R., Khan, M.H., and Bey, A., (2011). Use of collagen as an Implantable Material in The Reconstructive Procedures, an overview. Biol Med. 3:25-32.
  • [15] Poole, A.R., Kobayashi, M., Yasuda, T., Laverty, S., Mwale, F., Kojima, T., Sakai, T., Wahl, C., El Maadawy, S., Webb, G., and Tchetina, E., (2002). Type II Collagen Degradation and Its Regulation in Articular Cartilage in Osteoarthritis. Annals of the rheumatic diseases, 61(suppl 2), 78-81.
  • [16] Gupta, R., Canerdy, T., Skaggs, P., Stocker, A., Zyrkowski, G., Burke, R., Wegford, K., Goad, J.T., Rohde, K., Barnett, D., DeWees, W., Bagchi, M., and Bagchi, D., (2009). Therapeutic Efficacy of Undenatured Type-II Collagen (UC-II) in Comparison to Glucosamine and Chondroitin in Arthritic Horses. Vet Pharmacol Ther. 32:577-584.
  • [17] Howkins, A., (2015). Elucidation of Porcine Corneal Ultrastructure to Inform Development of Corneal Xenografts or Biomimetic Replacements.
  • [18] Birmingham, J., Vilim, V., and Kraus, V., (2007). Collagen Biomarkers for Arthritis Application. Biomarkers insights. 1:61-76. PMCID: PMC2716783.
  • [19] Banu, N., Hotoshi, H., Shinukuro, K., and Genshi, E., (1994). A Novel Method for Concentrating Urinary Type IV collagen based on participation with polyethylene glycol: application to its measurement by enzyme immunoassay. Ann Clin Biochem.31:485-491.
  • [20] Lamandé, S.R. and Bateman, J.F.,(2018). Collagen VI Disorders: Insights on form and Function in the Extracellular Matrix and Beyond. Matrix Biology, 71, 348-367.
  • [21] Woodley, D., Keene, D., Atha, T., Huang, Y., Lipman, K., Li, W., Chen, M.,(2004). Injection of Recombinant Human Type VII Collagen Restores Collagen Function on Dystrophic Epidermolysis Bullosa. Nat Med.10:693-695.
  • [22] Gelse, K., Poschl, E., and Aigner, T., (2003). Collagens-Structure, Function, And Biosynthesis. Adv Drug Deliv Rev. 55:1531-1546.
  • [23] Wotton, S., Duance, V., and Fryer, P., (1988). Type IX Collagen: a Possible Function in Articular Cartilage. FEBS Lett. 234:79-82.
  • [24] Ricard-Blum, S., (2010). The Collagen Family. Cold Spring Harbor Perspectives in Biology. 3:a004978.
  • [25] Karsdal, M., (2016). Biochemistry of Collagens Structure, Function and Biomarkers. London, United Kingdom: Academic Press.
  • [26] Brinckmann, J.C.B.C., Notbohm, H., Muller, P.K., and Bachinger, H.P., (2005). Collagen: Primer in Structure, Processing and Assembly. Berlin, Germany: Springer:56.
  • [27] Royce, P.M. and Steinmann, B., (2003). Connective Tissue and Its Heritable Disorders: Molecular, Genetic, and Medical Aspects. New York: Wiley.
  • [28] Fratzl, P., (2008). Collagen: Structure and Mechanics. New York: Springer. p 1-496.
  • [29] Buehler, M.J., (2006). Nature Designs Tough Collagen: Explaining the Nanostructure of Collagen Fibrils. PNAS. 103(33):12285-2290.
  • [30] Morimura, S., Nagata, H., Uemura, Y., Fahmi, A., Shigematsu, T., and Kida, K., (2002). Development of an Effective Process for Utilization of Collagen from Livestock And Fish Waste. Process Biochemistry, 37, 1403–1412.
  • [31] Yapar, E.A. and Tanrıverdi, S.T., (2016). Yaşlanma Karşıtı Kozmetik Yaklaşımlar ve Ürün Bileşenleri. Balıkesir Sağlık Bilimleri Dergisi, 5(2):99-109.
  • [32] Kim, S., (2012). Marine cosmeceuticals Trends and Prospects. Taylor and Francis Group, New York, 397s.
  • [33] Kim, S.K. and Mendis, E., (2006). Bioactive Compounds from Marine Processing Byproducts–A Review. Food Research International, 39(4):383-393.
  • [34] Leitinger, B. and Hohenester, E., (2007). Mammalian Collagen Receptors. Matrix Biology. 26:146-155.
  • [35] Oliveira, S., Ringshia, R., Legeros, R., Clark, E., Terracio, L., Teixeira, C., and Yost, M., (2009). An Improved Collagen Scaffold for Skeletal Regeneration. Journal of Biomedical Materials, 94(2):371-379.
  • [36] Parenteau-Bareil, R., Gauvin, R., and Berthod, F., (2010). Collagen-Based Biomaterials for Tissue Engineering Applications. Materials, 3, 1863-1887.
  • [37] Badylak, S.F., (2004). Xenogeneic Extracellular Matrix as a Scaffold for Tissue Reconstruction. Transplant Immunology, 12, 367-377.
  • [38] Gingras, M, Beaulieu, M.M., Gagnon V., Durham H.D., and Berthod F., (2008). In Vitro Study of Axonal Migration and Myelination of Motor Neurons in a Three-Dimensional Tissue Engineered Model. Glia, 56: 354-364.
  • [39] Che, Z.M., Jung, T.H., Choi, J.H., Yoon-do, J., Jeong, H.J., Lee, E.J., and Kim, J., (2006). Collagen Based Co-culture for Invasive Study on Cancer Cells-Fibroblasts Interaction. Biochemical and Biophysical Research Communications. 346:268-275.
  • [40] Sanz-Herrera J.A. and Reina-Romo, E., (2011). Cell-Biomaterial Mechanical Interaction in the Framework of Tissue Engineering: Insights, Computational Modeling and Perspectives. International Journal of Molecular Sciences, 12, 8217-8244.
  • [41] Cunniffe, G.M. and Brien, F.J.O., (2011). Collagen Scaffolds for Orthopedic Regenerative Medicine. The Journalof the Minerals, Metals and Materials Society, 63(4):66-73. [42] Rose, F.R. and Oreffo, R.O., (2002). Bone Tissue Engineering: Hope VS Hype. Biochemical and Biophysical Research Communications 292:1-7.
  • [43] Gökalp, M., (2006). Doğu Akdeniz-Ege Süngerlerinden (Porifera) Seçilen Türlerin İncelenmesi, Bu Canlılardaki Kolajen Tip II, IV ve İntegrin β1 Proteinlerinin Varlığının İmmünohistokimyasal ve Moleküler Genetik Düzeyde Araştırılması. Ankara Üniversitesi. Yüksek Lisans Tezi. s. 90.
  • [44] Orgel, J., Sella, I., Madhurapantula, R.S., Antipova, O., Mandelberg, Y., Kashman, Y., and Benayahu, Y., (2017). Molecular and Ultrastructural Studies of a Fibrillar Collagen from Octocoral (Cnidaria). The Journal of Experimental Biology, 220(Pt 18), 3327–3335.
  • [45] Stabili, L., Schirosi, R., Parisi, M., Piraino, S., and Cammarata, M., (2015). The Mucus of Actinia Equina (Anthozoa, Cnidaria): An Unexplored Resource for Potential Applicative Purposes. Marine drugs, 13(8):5276-5296.
  • [46] Addad, S., Exposito, J., Faye, C., Ricard-Blum, S., and Lethias, C., (2011). Isolation, Characterization and Biological Evaluation of Jellyfish Collagen for Use in Biomedical Applications. Marine drugs.
  • [47] Kantarcıoğlu, İ., (2017). Denizanası Kolajeni/Misvak Hibrit Membranların Üretimi ve Periodontal Doku Grefti Olarak Kullanımının Araştırılması. Çanakkale Onsekiz Mart Üniversitesi. Yüksek Lisans Tezi. s. 58.
  • [48] Pallela, R., Bojja, S., and Janapala, V.R., (2011). Biochemical and Biophysical Characterization of Collagens of Marine Sponge, Ircinia fusca (Porifera: Demospongiae: Irciniidae). International journal of Biological Macromolecules, 49(1):85-92.
  • [49] Miura, S. and Kimura, S., (1985). Jellyfish Mesogloea Collagen. Characterization of Molecules as a1a2a3 heterotetramers. Journal of Biological Chemistry, 260, 15352-15356.
  • [50] Nagai, T., Ogawa, T., Nakamura, T., Ito, T., Nakagawa, H., Fujiki, K., Nakao, M., and Yano, T., (1999). Collagen of Edible Jellyfish Exumbrella. Journal of the Science of Food and Agriculture, 79, 855-858.
  • [51] Rerk-am, U., Chawananorasest, K., Kongsombat, B., Tanstirapakdee, S., Sematong, T., and Thubthimthed, S., (2016). Extraction and Characterization of Collagen from the White Jellyfish (Lobonema smithi Mayer.). European Chemistry Congress, Rome, Italy.
  • [52] Felician, F.F., Yu, R.H., Li, M.Z., Li, C.J., Chen, H.Q., Jiang, Y., Tang, T., Qi, W.Y., and Xu, H.M., (2019). The Wound Healing Potential of Collagen Peptides Derived from The Jellyfish Rhopilema Esculentum. Chinese Journal of Traumatology, 22(1):12-20.
  • [53] Cheng, X., Shao, Z., Li, C., Yu, L., Raja, M.A., and Liu, C., (2017). Isolation, Characterization and Evaluation of Collagen from Jellyfish Rhopilema Esculentum Kishinouye for Use in Hemostatic Applications. Plos one, 12(1):e0169731.
  • [54] Barzideh, Z., Latiff, A.A., Gan, C.Y., Benjakul, S., and Karim, A.A., (2014). Isolation and Characterisation of Collagen from the Ribbon Jellyfish (Chrysaora sp.). International Journal of Food Science and Technology, 49(6):1490-1499.
  • [55] Hsieh, Y.H.P., (2005). Use of Jellyfish Collagen (Type II) in the Treatment of Rheumatoid Arthritis. No. 6,894,029. US Patent.
  • [56] Rastian, Z., Pütz, S., Wang, Y., Kumar, S., Fleissner, F., Weidner, T., and Parekh, S.H., (2018). Type I Collagen from Jellyfish Catostylus Mosaicus for Biomaterial Applications. ACS Biomaterials Science & Engineering, 4(6):2115-2125.
  • [57] Zhang, J., Duan, R., Huang, L., Song, Y., and Regenstein, J.M., (2014). Characterisation of Acid Soluble and Pepsin-solubilised Collagen from Jellyfish (Cyanea nozakii Kishinouye). Food Chemistry, 150:22–26.
  • [58] Kramer, J.M., (1994). Structures and Functions of Collagens in Caenorhabditis Elegans. The FASEB Journal, 8(3):329-336.
  • [59] Jridi, M., Bardaa, S., Moalla, D., Rebaii, T., Souissi, N., Sahnoun, Z., Nasri, M.,(2015). Microstructure, Rheological and Wound Healing Properties of Collagen-based gel from Cuttlefish Skin. International journal of biological macromolecules, 77, 369-374.
  • [60] Schmut, O., Roll, P., Reich, M.E., and Palm, W., (1980). Biochemical and Electronmicroscopic Investigations on Helix pomatia Collagen. Zeitschrift für Naturforschung C, 35:376-379.
  • [61] Wu, J., Guo, X., Liu, H., and Chen, L., (2019). Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata). Foods.
  • [62] Dyachuk, V., (2018). Extracellular Matrix Components in Bivalvia: Shell and ECM Components in Developmental and Adult Tissues. Fisheries and Aquaculture Journal. 9(2), 1a-1a.
  • [63] Kimura, S., Takema, Y., and Kubota, M., (1981). Octopus Skin Collagen. Isolation and Characterization of Collagen Comprising Two Distinct Alpha Chains. Journal of Biological Chemistry. 25;256(24):13230-13234.
  • [64] Shanmugam, V., Ramasamy, P., Subhapradha, N., Sudharsan, S., Seedevi, P., Moovendhan, M., Krishnamoorthy, J., Shanmugam, A., and Srinivasan, A., (2012).
  • Extraction, Structural and Physical Characterization of Type I Collagen from the Outer Skin of Sepiella Inermis. African Journal of Biotechnology, 11(78):14326-14337.
  • [65] Shanmugam, A., Ramasamy, P., Bharti, M.K., Saravanan, R., Subhapradha, N., Vairamani, S., and Jayalakshmi, K., (2011). Isolation and Characterization of Collagen from the skin of Sepia pharaonis (Ehrenberg, 1831). International Journal of Current Research. 33(6):107-111.
  • [66] Bairati, A. and Gioria, M., (2004). Collagen Fibrils of an Invertebrate (Sepia officinalis) are Heterotypic: Immunocytochemical Demonstration. Journal of structural biology, 147(2):159-165.
  • [67] Balti, R., Jridi, M., Sila, A., Souissi, N., Nedjar-Arroume, N., Guillochon, D., and Nasri, M., (2011). Extraction and Functional Properties of Gelatin from the skin of Cuttlefish (Sepia officinalis) Using Smooth Hound Crude Acid Protease-Aided Process. Food Hydrocolloids, 25(5):943-950.
  • [68] Jose, H.M.P.M., Murugesan, P., Arumugam, M., and Kumar, K.M., (2014). Isolation and Characterization of Acid and Pepsin-solubilised Collagen from the Muscle of Mantis Shrimp (Oratosquilla nepa). International Journal of Pharmacy and Pharmaceutical Sciences, 6(1), 14.
  • [69] Mizuta, S., Yoshinaka, R., Sato, M., and Sakaguchi, M., (1994). Characterization of Collagen in Muscle of Several Crustacean Species. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 107(2):365-370.
  • [70] Sivakumar, P., Suguna, L., and Chandrakasan, G., (2000). Molecular Species of Collagen in the Intramuscular Connective Tissues of the Marine Crab, Scylla Serrata. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 125(4):555-562.
  • [71] Yoshinaka, R., Mizuta, S., Itoh, Y., and Sato, M., (1990). Two Genetically Distinct Types of Collagen in Kuruma Prawn Penaeus Japonicus. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 96(3):451-456.
  • [72] Golob, R., Chetsanga, C.J., and Doty, P., (1974). The Onset of Collagen Synthesis in Sea Urchin Embryos. Biochimica et Biophysica Acta (BBA)-Nucleic Acids and Protein Synthesis, 349(1):135-141.
  • [73] Wijanarko, A., Januardi, Ginting, M., Sahlan, M., Krisanta Endah Savitri, I., Florensia, Y., Regina-Sudiarta, M., and Hermansyah, H., (2017). Saponin Isolation as Main Ingredients of Insecticide and Collagen Type I from Crown of Thorn-Starfish (Acanthaster planci). IOP Conference Series: Earth and Environmental Science, 89(1).
  • [74] Kimura, S., Omura, Y., Ishida, M., and Shirai, H., (1993). Molecular Characterization of Fibrillar Collagen from the Body Wall of Starfish Asterias Amurensis. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 104(4):663-668.
  • [75] Siddiqui, Y.D., Arief, E.M., Yusoff, A., and Suzina, A.H., (2013). Isolation of Pepsın-Solubilized Collagen (Psc) from Crude Collagen Extracted from Body Wall of Sea Cucumber (Bohadschıa spp.)
  • [76] El-Rashidy, A.A., Gad, A., Abu-Hussein, A.E.G., and Habib, S.I., (2015). Chemical and Biological Evaluation of Egyptian Nile Tilapia (Oreochromis niloticas) Fish Scale Collagen. International Journal of Biological Macromolecules. 79:618–626.
Toplam 76 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Bölüm Makaleler
Yazarlar

Erkan Uğurlu 0000-0001-8940-8421

Önder Duysak 0000-0002-7484-3102

Eyüp İlker Saygılı 0000-0002-0102-4237

Sinem Uğur 0000-0003-4309-7415

Selin Sayın 0000-0002-7497-388X

Yayımlanma Tarihi 31 Ocak 2020
Yayımlandığı Sayı Yıl 2020 Cilt: 15 Sayı: 1

Kaynak Göster

APA Uğurlu, E., Duysak, Ö., Saygılı, E. İ., Uğur, S., vd. (2020). Denizel Omurgasız Canlılardan Elde Edilen Kolajenler ve Kullanım Alanları. Ecological Life Sciences, 15(1), 24-35.
AMA Uğurlu E, Duysak Ö, Saygılı Eİ, Uğur S, Sayın S. Denizel Omurgasız Canlılardan Elde Edilen Kolajenler ve Kullanım Alanları. NWSA. Ocak 2020;15(1):24-35.
Chicago Uğurlu, Erkan, Önder Duysak, Eyüp İlker Saygılı, Sinem Uğur, ve Selin Sayın. “Denizel Omurgasız Canlılardan Elde Edilen Kolajenler Ve Kullanım Alanları”. Ecological Life Sciences 15, sy. 1 (Ocak 2020): 24-35.
EndNote Uğurlu E, Duysak Ö, Saygılı Eİ, Uğur S, Sayın S (01 Ocak 2020) Denizel Omurgasız Canlılardan Elde Edilen Kolajenler ve Kullanım Alanları. Ecological Life Sciences 15 1 24–35.
IEEE E. Uğurlu, Ö. Duysak, E. İ. Saygılı, S. Uğur, ve S. Sayın, “Denizel Omurgasız Canlılardan Elde Edilen Kolajenler ve Kullanım Alanları”, NWSA, c. 15, sy. 1, ss. 24–35, 2020.
ISNAD Uğurlu, Erkan vd. “Denizel Omurgasız Canlılardan Elde Edilen Kolajenler Ve Kullanım Alanları”. Ecological Life Sciences 15/1 (Ocak 2020), 24-35.
JAMA Uğurlu E, Duysak Ö, Saygılı Eİ, Uğur S, Sayın S. Denizel Omurgasız Canlılardan Elde Edilen Kolajenler ve Kullanım Alanları. NWSA. 2020;15:24–35.
MLA Uğurlu, Erkan vd. “Denizel Omurgasız Canlılardan Elde Edilen Kolajenler Ve Kullanım Alanları”. Ecological Life Sciences, c. 15, sy. 1, 2020, ss. 24-35.
Vancouver Uğurlu E, Duysak Ö, Saygılı Eİ, Uğur S, Sayın S. Denizel Omurgasız Canlılardan Elde Edilen Kolajenler ve Kullanım Alanları. NWSA. 2020;15(1):24-35.