THE EFFECT OF DECELLULARIZATION TECHNIQUE ON COLLAGEN TYPE II AND MATRICES POROSITY OF CARTILAGE BOVINE SCAFFOLD
Downloads
Background: Cartilage has limited capacity for self-repair in case of defect. Stem cell based tissue engineering has become an alternative therapy for the treatment of cartilage defect. The use of decellularized cartilage bovine can serve as scaffold to support proliferation dan differentiation of the stem cell.
Purpose: This research is to compare the effect of decellularization technique on collagen type II and matrices porosity of cartilage bovine scaffold.
Methods: This experimental laboratory research used cartilage bovine scaffold which was decellularized using physical, chemical and enzymatic techniques with different time and concentration variations, then collagen type II measurement was performed by immunohistochemical method and evaluation of porosity size with electron microscopy.
Results: In the preparations with the highest concentration and the longest immersion time of 5% SDS for 72 hours, the decellularization process occurs perfectly. The collagen type II content was found to have significantly higher concentrations than the controls and other preparations, and have interconnected porosities in large size.
Conclusion: High concentrations of collagen type II and large diameter of pores after decellularization process in cartilage bovine scaffold confirm that this scaffold still has optimum biochemical cues that can be a good mechanical framework and microenvironment stem cell in effort to repair the cartilage defects. This result was expected to become a standard for the decellularization making of cartilage bovine scaffold.Heriawan R. Perkembangan Indikator Utama Sosial Ekonomi Indonesia. Subdirektorat Layanan dan Promosi Statistik Badan Pusat Statistik Indonesia. Jakarta: ISSN. 2011; 2085.5664.
Claire V, Carine Bouffi, Christophe Merceron, Jan Gordeladze, Jean-Marc Brondello,Christian Jorgensen ,Pierre Weiss, Jérome Guicheux, Danièle Noí«l; Cartilage Tissue Engineering: Towards a Biomaterial-Assisted Mesenchymal Stem Cell Therapy; Current Stem Cell Research &Therapy. Hospital Lapeyronie, Montpellier, Bentham Science Publishers Ltd, France. 2009; 318-332.
Myron Spector; Biomaterials-Based Tissue Engineering And Regenerative Medicine Solutions To Musculoskeletal Problems Tissue Engineering, Boston Healthcare System, And Orthopaedic Research Laboratory, Harvard Medical School, Boston,USA,Swiss Med Wkly. 2006;136:293–301.
Dwikora, Sasetia DR, Taufik A, Rofi'i, Sadabaskara, Bembie R, Musbhida A and Adi G. Freeze dried bovine cartilage powder as an alternative scaffold for cartilage defect. International symposia of stem cell and Tissue bank. Surabaya. 2011.
Asheesh Bedi, Brian T. Feeley, Riley J. Williams, Management of Articular Cartilage Defects ofthe Knee; Journal of Bone and Joint Surgery, Am. 2010; 92:994-1009./JBJS.I.00895
M. Wessling D.Stamatialis, K. Boller, C.A.van Blitterswijk, D.W. Grijpma; Design Strategies for Tissue Engineering Scaffolds. Bernke Papenburg, Enschede, The Netherlands. 2009.
Ferdiansyah. Use of Freeze-Dried Irradiated Bones in Orthopaedic Surgery.In Radiation in Tissue Banking Basic Science and Clinical Applications of Radiated Tissue Allografts (edited by Nather A, Yusof N, Hilmy N). World Scientific, Singapore. 2007; 317-326.
Konakci KZ, Bohle B, Blumer R, Hoetzenecker W, Roth G, Moser B, et al. Alpha-Gal on bioprostheses: xenograft immune response in cardiac surgery. Eur J Clin Invest 2005;35:17–23.
Badylak SF, Taylor D, Uygun K. Whole-organ tissue engineering: decellularization and recellularization of three-dimensional matrix scaffolds. Annu Rev Biomed Eng 2011;13:27–53.
Salter MB. Textbook of Disorders and Injuries of the Musculoskleletal System. 2nd ed.1983 p.6-25
Scott J. Hollister ; Porous scaffold design for tissue engineering Is At The Scaffold Tissue Engineering Group, Departments Of Biomedical Engineering, Surgery and Mechnical Engineering,The University of Michigan, Ann Arbor, Michigan 41809, USA
Baltimore.Tissue Engeneering, Journal of Bone and Joint Surgery. 2005; 86 : 1541-1557.
Cook SD, Barrack RL, Skinner HB. Basic Science in Orthopaedic Surgery, In : Skinner HB, ed. Current Diagnosis and Treatment in Orthopaedics. 2nd ed. New York : Lange Medical Book. 2000; p. 8 – 11.
Akeson WH, Amiel D, Gershuni DH. Articular Cartilage Physiology and Metabolism. In: Resnick D, ed. Diagnosis of Bone and Joint Disorders. 3rd ed. Philadelphia: Saunders WB.1996; p.769 – 90.
Vunjak-Novakovic G. The fundamentals of tissue engineering: scaffolds and bioreactors. In: Tissue Engineering of Cartilage and Bone (Novartis Foundation Symposium). Editors: Bock G and Goode J. John Wiley & Sons Ltd, Chichester. 2003; 249, 34-51.
Erdag G,Morgan JR. Allogeneic versus xenogeneic immune reaction to bioengineered skin grafts.Cell Transplant.2004; 13:701–12.
Gock H, Murray-Segal L, Salvaris E, Cowan P, D'Apice AJ. Allogeneic sensitization is more effective than xenogeneic sensitization in eliciting Gal-mediated skin graft rejection. Transplantation. 2004; 77:751–53.
Ross JR, Kirk AD, Ibrahim SE, Howell DN, Baldwin WM 3rd, Sanfilippo FP. Characterization of human anti-porcine "natural antibodies” recovered from ex vivo perfused hearts”predominance of IgM and IgG2. Transplantation.1993. 55:1144–50.
BernardMP, ChuML, Myers JC, Ramirez F,Eikenberry EF, Prockop DJ. Nucleotide sequences of complementary deoxyribonucleic acids for the pro alpha 1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution. Biochemistry 22. 1983; :5213–23.
Bernard MP, Myers JC, Chu ML, Ramirez F, Eikenberry EF, Prockop DJ. Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies structurally conserved features of the protein and the gene. Biochemistry 22.1983;1139–45.
Constantinou CD, Jimenez SA. Structure of cDNAs encoding the triple-helical domain of murine alpha 2 (VI) collagen chain and comparison to human and chick homologues. Use of polymerase chain reaction and partially degenerate oligonucleotide for generation of novel cDNA clones. Matrix.1991;11:1–9.
Exposito JY, D'AlessioM, Solursh M, Ramirez F. Sea urchin collagen evolutionarily homologous to vertebrate pro-alpha 2(I) collagen. J. Biol. Chem.1992;267:15559–62.
McPherson TB, Liang H, Record RD, Badylak SF. Galalpha(1,3)Gal epitope in porcine small intestinal submucosa. Tissue Eng.2000;6:233–39.
Raeder RH, Badylak SF, Sheehan C, Kallakury B, Metzger DW. Natural anti-galactose alpha1,3 galactose antibodies delay, but do not prevent the acceptance of extracellular matrix xenografts. Transplant.Immunol.2002;10:15–24.
Daly K, Stewart-Akers A, Hara H, Ezzelarab M, Long C, et al. Effect of the alphaGal epitope on the response to small intestinal submucosa extracellular matrix in a nonhuman primate model. Tissue Eng. Part A 2009;15:3877–88.
- The author acknowledges that the copyright of the article is transferred to the Journal of Orthopaedi and Traumatology Surabaya (JOINTS), whilst the author retains the moral right to the publication.
- The legal formal aspect of journal publication accessibility refers to Creative Commons Attribution-Non Commercial-Share Alike 4.0 International License (CC BY-NC-SA).
- All published manuscripts, whether in print or electronic form, are open access for educational, research, library purposes, and non-commercial uses. In addition to the aims mentioned above, the editorial board is not liable for any potential violations of copyright laws.
- The form to submit the manuscript's authenticity and copyright statement can be downloaded here.
Journal of Orthopaedi and Traumatology Surabaya (JOINTS) is licensed under a Creative Commons Attribution-Non Commercial-Share Alike 4.0 International License.
Journal Orthopaedi and Traumatology Surabaya (JOINTS) (