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      Collagen-Based Biomaterials for Tissue Engineering Applications

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          Abstract

          Collagen is the most widely distributed class of proteins in the human body. The use of collagen-based biomaterials in the field of tissue engineering applications has been intensively growing over the past decades. Multiple cross-linking methods were investigated and different combinations with other biopolymers were explored in order to improve tissue function. Collagen possesses a major advantage in being biodegradable, biocompatible, easily available and highly versatile. However, since collagen is a protein, it remains difficult to sterilize without alterations to its structure. This review presents a comprehensive overview of the various applications of collagen-based biomaterials developed for tissue engineering, aimed at providing a functional material for use in regenerative medicine from the laboratory bench to the patient bedside.

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          Decellularization of tissues and organs.

          Thomas Gilbert, Tiffany Sellaro, Stephen Badylak (2006)
          Decellularized tissues and organs have been successfully used in a variety of tissue engineering/regenerative medicine applications, and the decellularization methods used vary as widely as the tissues and organs of interest. The efficiency of cell removal from a tissue is dependent on the origin of the tissue and the specific physical, chemical, and enzymatic methods that are used. Each of these treatments affect the biochemical composition, tissue ultrastructure, and mechanical behavior of the remaining extracellular matrix (ECM) scaffold, which in turn, affect the host response to the material. Herein, the most commonly used decellularization methods are described, and consideration give to the effects of these methods upon the biologic scaffold material.
          Article 0 comments Cited 450 times – based on 0 reviews     Review now
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            Collagen/chitosan porous scaffolds with improved biostability for skin tissue engineering.

            L. Ma (2003)
            Porous scaffolds for skin tissue engineering were fabricated by freeze-drying the mixture of collagen and chitosan solutions. Glutaraldehyde (GA) was used to treat the scaffolds to improve their biostability. Confocal laser scanning microscopy observation confirmed the even distribution of these two constituent materials in the scaffold. The GA concentrations have a slight effect on the cross-section morphology and the swelling ratios of the cross-linked scaffolds. The collagenase digestion test proved that the presence of chitosan can obviously improve the biostability of the collagen/chitosan scaffold under the GA treatment, where chitosan might function as a cross-linking bridge. A detail investigation found that a steady increase of the biostability of the collagen/chitosan scaffold was achieved when GA concentration was lower than 0.1%, then was less influenced at a still higher GA concentration up to 0.25%. In vitro culture of human dermal fibroblasts proved that the GA-treated scaffold could retain the original good cytocompatibility of collagen to effectively accelerate cell infiltration and proliferation. In vivo animal tests further revealed that the scaffold could sufficiently support and accelerate the fibroblasts infiltration from the surrounding tissue. Immunohistochemistry analysis of the scaffold embedded for 28 days indicated that the biodegradation of the 0.25% GA-treated scaffold is a long-term process. All these results suggest that collagen/chitosan scaffold cross-linked by GA is a potential candidate for dermal equivalent with enhanced biostability and good biocompatibility.
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              Collagens: molecular biology, diseases, and potentials for therapy.

              D J Prockop, K Kivirikko (1995)
              The collagen superfamily of proteins now contains at least 19 proteins formally defined as collagens and an additional ten proteins that have collagen-like domains. The most abundant collagens form extracellular fibrils or network-like structures, but the others fulfill a variety of biological functions. Some of the eight highly specific post-translational enzymes involved in collagen biosynthesis have recently been cloned. Over 400 mutations in 6 different collagens cause a variety of human diseases that include osteogenesis imperfecta, chondrodysplasias, some forms of osteoporosis, some forms of osteoarthritis, and the renal disease known as the Alport syndrome. Many of the disease phenotypes have been produced in transgenic mice with mutated collagen genes. There has been increasing interest in the possibility that the unique post-translational enzymes involved in collagen biosynthesis offer attractive targets for specifically inhibiting excessive fibrotic reactions in a number of diseases. A number of experiments suggest it may be possible to inhibit collagen synthesis with oligo-nucleotides or antisense genes.
              Article 0 comments Cited 203 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Materials (Basel)
                Journal ID (iso-abbrev): Materials (Basel)
                Journal ID (publisher-id): materials
                Title: Materials
                Publisher: Molecular Diversity Preservation International
                ISSN (Electronic): 1996-1944
                Publication date (Electronic): 16 March 2010
                Publication date Collection: March 2010
                Volume: 3
                Issue: 3
                Pages: 1863-1887
                Affiliations
                [1 ]Laboratoire d’Organogénèse Expérimentale (LOEX), Centre de recherche FRSQ du CHA universitaire de Québec, Hôpital du Saint-Sacrement, Québec, QC, G1S 4L8 Canada; E-Mails: remi.parenteau.1@ 123456ulaval.ca (R.P.B.); robert.gauvin.1@ 123456ulaval.ca (R.G.)
                [2 ]Département de chirurgie, Faculté de médecine, Université Laval, Québec, QC, G1V 0A6 Canada
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: francois.berthod@ 123456chg.ulaval.ca ; Tel.: +1-418-682-7565; Fax: +1-418-682-8000.
                Article
                Publisher ID: materials-03-01863
                DOI: 10.3390/ma3031863
                PMC ID: 5445871
                SO-VID: 93684c5e-dad1-4e42-ad14-12f504489766
                Copyright © © 2010 by the authors;
                License:

                licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 02 February 2010
                Date revision received : 09 March 2010
                Date accepted : 11 March 2010
                Categories
                Subject: Review

                Keywords: collagen,biomaterial,soft tissue
                Data availability:
                Keywords: collagen, biomaterial, soft tissue

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