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PubMed1975

Characterisation of the major CNBr-Derived peptides of porcine type II collagen.

As part of a general study on the matrix macromolecules of pig cartilage, the CNBr-derived peptides of porcine type II collagen have been isolated from laryngeal cartilage and characterized. Type II was the only molecular type of collagen detected in laryngeal cartilage from 6-9 month old pigs. The major CNBr-peptides of this collagen were prepared by ion exchange and molecular sieve chromatography and characterized by SDS-polyacrylamide disc electrophoresis and amino acid analysis. Six peptides were recovered in high yield and were shown to be closely homologous to similar peptides previously recovered from bovine and human type II collagens. The largest peptide alpha1(II)CB10 appeared by SDS-disc electrophoresis to be slightly larger than previously reported. The amino acid composition of alpha1(II)CB10 supported this finding of a higher molecular weight.

Animals↗
PubMed1988

Enzymatic alteration of C1q, the collagen-like subcomponent of the first component of complement, leads to cross-reactivity with type II collagen.

Native serum C1q, the collagenous-like subcomponent of the first component of complement, is not recognized by polyclonal anti-collagen type II antibodies. However, when purified C1q was subjected to limited proteolysis by collagenase it showed antigenic cross-reactivity with collagen type II. The same cross-reactivity was observed with hemolytically active C1q in synovial fluids of patients with rheumatoid arthritis (RA), whereas C1q from synovial fluids of patients with osteoarthritis (OA), villo-nodular synovitis and ankylosing spondylitis was not recognized by this antibody. However, incubation of synovial fluid C1q of OA patients with synovial fluid leucocytes from RA patients led to an alteration of OA-C1q which was now recognized by the anti-collagen type II antibody.

Animals↗
PubMed2000

Differences in type II collagen degradation between peripheral and central cartilage of rat stifle joints after cranial cruciate ligament transection.

OBJECTIVE: Type II collagen degradation is thought to be the key process in cartilage degradation during the development of osteoarthritis (OA). In this study, we investigated the kinetics of type II collagen degradation during surgically induced OA. METHODS: Experimental OA was induced in male Wistar rats by transecting the cranial (anterior) cruciate ligament (CCL). Hematoxylin and eosin staining was used to study overall cartilage degradation, while immunostained sections were used to demonstrate denatured type II collagen (Col2-3/4m antibody) and the collagenase cleavage site in type II collagen (Col2-3/ 4Cshort antibody). RESULTS: During the first 3-4 weeks, cartilage destruction, associated with chondrocyte death, proteoglycan depletion, and a marked increase in the collagenase cleavage neoepitope, was mainly located at the margins of the cartilage. From weeks 3-4, the central part of the cartilage showed increased surface fibrillation and apparent chondrocyte death. In these areas, increased denatured type II collagen staining but little cleavage-site staining was present. CONCLUSION: These results indicate that cartilage degradation after CCL transection in the rat consists of 2 phases. An early phase located at the cartilage margins and a late phase located at the central part of the cartilage. In the early phase, collagenase-dependent cartilage damage occurred. During the late phase, the level of type II collagen denaturation increased.

Animals↗
PubMed1980

Collagen-induced polyarthritis in rats: a study of native type II collagen for adjuvant activity.

Collagen-induced polyarthritis in rats is a new experimental model that shares clinical and histologic features with adjuvant arthritis. To determine whether collagen-induced arthritis is a form of adjuvant disease and to further exclude contamination of collagen with an adjuvant substance, native type II collagen was studied for adjuvant properties. IgM and IgG PFC activity and PBMC [3H]TdR incorporation were studied in rats after injection with TNP-OA combined with IFA, IFA and CII, or CFA. In general, humoral and CMI responses to TNP-OA were lower in rats injected with IFA/CII compared with those with IFA; the presence of CII during primary immunization failed to significantly enhance PFC activity to TNP after a boost. CFA-injected rats gave maximal values in both studies. Mice pretreated with BII in the absence of oil gave PFC responses below control after sensitization with SRC. Furthermore, CII was unable to replace mycobacteria in the induction of EAE in rats and was devoid of mitogenic or polyclonal stimulatory properties. It is concluded that collagen-induced arthritis is a distinct entity from adjuvant arthritis and is dependent upon the unique immunogenicity of type II collagen in rats rather than upon an adjuvant effect.

Animals↗
PubMed1989

Immunohistochemical localization of type II collagen in cartilage-forming tumors.

The presence and distribution of type II collagen was studied in 36 cartilage and cartilage-related tumors, including five osteosarcomas and one chordoma. A monoclonal antibody prepared from chicken type II collagen was used with paraffin sections, employing the ABC (avidin biotinylated horseradish peroxidase complex) peroxidase technique. Fetal cartilage and fracture callus were used as control materials. Type II collagen was present in the matrix of all the cartilage tumors. The reaction was strongest in areas of well-differentiated cartilage and weakest in the poorly differentiated tissue of high-grade chondrosarcomas. Areas of mineralization or ossification, and areas of eosinophilic, fibrous, or degenerated cartilage gave a negative reaction.

Cartilage↗
PubMed2002

[Effect of interleukin I receptor antigonist gene therapy on arthritis induced by type II collagen in mice].

OBJECTIVE: To investigate the effect of interleukin-1 receptor antagonist gene therapy on type II collagen induced arthritis in DBA/1 mice. METHODS: Plasmid pcDI-IL-1ra that expresses IL-1ra in eukaryotes was constructed by inserting human IL-1ra cDNA into the eukaryotic expression vector pcDI. Eukaryotes were transfected with the plasmid pcDI-IL-1ra in vivo and in vitro. The expression of 8 IL-1ra was examined by ELISA and immunohistochemistry. Type II collagen was used to induced arthritis in 32 DBA/1 mice. This plasmid was injected into the muscles of DBA/1 mice with arthritis induced by type II collagen by gene gun (20 micro g/mouse) and into the muscle of 8 mice by intramuscular injection (200 micro g/mouse). After the administration, the condition of arthritis was observed. The serum IL-ira was examined 6 and 12 days after administration. The expression of IL-ira in muscles was tested by computerized imaging analysis. RESULTS: PCR and DNA sequencing proved the accuracy of the inserted fragment. ELISA and immunohistochemistry detected high expression of IL-ira in vivo and in vitro. The absorbance ( A ) 490 value of IL-ira in the mouse muscle was 0.52 +/- 0.03 in gene gun group, and 0.48 +/- 0.02 in intramuscular injection group, all higher than that in the control group (0.41 +/- 0.02,P < 0.01 and P < 0.05). The serum IL-ira values in the gene gun group and in tramuscular injection group 6 days and 12 days after therapy were all significantly higher than that in the control group (all P < 0.01; and P < 0.01 and P < 0.05). Since the 6 th day after therapy, the redness and swelling of joints in both therapies groups were alleviated. Pathological examination made 12 days after therapy showed relief at different degrees of the infiltration of inflammatory cells, hyperplasia of synovia, bone infiltration, and cartilage destruction, especially in the gene gun group. CONCLUSION: Gene therapy of IL-ira via non-virus eukaryotic expression vactor, especially by gene gun, is effective in treating arthritis induced by type II collagen.

Animals↗
PubMed1994

Epitope specificity and T cell receptor usage in type II collagen induced autoimmune ear disease.

An immune response directed against type II collagen (CII) has been reported in several autoimmune diseases including the animal models of collagen-induced arthritis (CIA) and collagen-induced autoimmune ear disease (CIAED). In this communication, we have found that T cells from type II collagen-immunized DBA/1-lac could transfer auricular chondritis to naive mice. The T cells from type II collagen-immunized H-2r and H-2q mice recognize different epitopes from the CB11 peptide of CII. The CII-specific T cells from H-2q background mice recognize peptide residues p121-147 (P1) but do not respond to residues p211-247 (P2). The T cells of H-2r mice immunized with CII respond better to P2 rather than P1. By altering certain amino acids within these epitopes, the response of CII-specific TCR to antigen has been increased or abolished. Our results suggest that the lysine residues at positions 129, 141, and 147 in P1, the arginine residue at position 227, and glutamic acid at position 230 in P2 might play an important role in the trimolecular interaction. Ten clonally distinct T cell hybridomas specific for CII have been established from H-2r B10.RIII mice and the beta chains of their TCR have been analyzed. Three subfamilies, V beta 1, V beta 6, and V beta 8, were utilized with dominant expression of V beta 8 (60%). This is quite similar to the pattern found in type II collagen-induced arthritis in H-2q mice. This preferential use of V beta 8 in CIAED implies that an immunotherapy may make it possible to control this autoimmune disease, even in a MHC-diverse situation.

Amino Acid Sequence↗
PubMed2003

Experimentally induced unilateral tooth loss: expression of type II collagen in temporomandibular joint cartilage.

PURPOSE: We sought to examine possible changes in pattern and concentration of type II collagen in the condylar cartilage and articular disc of the temporomandibular joint (TMJ) in response to unilateral extraction of mandibular teeth in a rabbit model as a means of elucidating the effects of unilateral mastication on the TMJ. METHODS: A total of 12 experimental rabbits were killed either 3 or 6 weeks after the extractions, and 3 additional rabbits without extractions were used as controls. TMJ blocks from both sides of each of the 15 animals were examined for type II collagen via an immunoperoxidase procedure. RESULTS: Anti-type II collagen antibody (Ab) binding was detected mainly in the hypertrophic chondroblast layer of the condylar cartilage of normal rabbits. At 3 weeks after unilateral extraction of teeth, anti-type II collagen Ab binding to the territorial matrix of the hypertrophic chondroblast layer of the condylar cartilage and to the disc was stronger than normal. The increase in Ab binding appeared more dramatic on the nonfunctional side than on the functional side of TMJ. Variations from the normal pattern of anti-type II collagen Ab binding in terms of distribution through the extracellular matrix and fibrillar appearance were also observed. CONCLUSION: The findings suggest that the condylar cartilage and disc adapt to the imbalance induced by unilateral extraction of teeth through chondrocyte repair responses involving collagen II expression that appear to differ between the functional and nonfunctional sides of the TMJ.

Animals↗
PubMed1984

Crystalline fibril structure of type II collagen in lamprey notochord sheath.

We report here the existence of a crystalline molecular packing of type II collagen in the fibrils of the lamprey notochord sheath. This is the first finding of a crystalline structure in any collagen other than type I. The lamprey notochord sheath has a composition similar to that of cartilage, with type II collagen, a minor collagen component with 1 alpha, 2 alpha and 3 alpha chains, and cartilage-like proteoglycan. The high degree of orientation of fibrils in the notochord makes it possible to use X-ray diffraction to determine collagen fibril organization in this type II-containing tissue. The low angle equatorial scattering shows the fibrils are all about 17 nm in diameter and have an average center-to-center separation of 31 nm. These results are supported by electron microscope observations. A set of broad equatorial diffraction maxima at higher angles represents the sampling of the collagen molecular transform by a limited crystalline lattice, extending over a lateral dimension close to the diameter of one fibril. This indicates that each 17 nm fibril contains a crystalline array of molecules and, although a unit cell is difficult to determine because of the broad overlapping reflections, it is clear that the quasi-hexagonal triclinic unit cell of type I collagen in rat tail tendon is not consistent with the data. The meridional diffraction pattern showed 26 orders with the characteristic 67 nm periodicity found for tendon. However, the intensities of these reflections differ markedly from those found for tendon and cannot be explained by an unmodified gap/overlap model within each 67 nm period. Both X-ray diffraction and electron microscope data indicate a low degree of contrast along the fibril axis and are consistent with a periodic binding of a non-collagenous component in such a way as to obscure the gap region.

Animals↗
PubMed2003

Cross-linked type I and type II collagenous matrices for the repair of full-thickness articular cartilage defects--a study in rabbits.

The physico-chemical properties of collagenous matrices may determine the tissue response after insertion into full-thickness articular cartilage defects. In this study, cross-linked type I and type II collagen matrices, with and without attached chondroitin sulfate, were implanted into full-thickness defects in the femoral trochlea of adolescent rabbits. The tissue response was evaluated 4 and 12 weeks after implantation by general histology and two semi-quantitative histological grading systems. Four weeks after implantation, type I collagenous matrices were completely filled with cartilage-like tissue. By contrast, type II collagenous matrices revealed predominantly cartilaginous tissue only at the superficial zone and at the interface of the matrix with the subchondral bone, leaving large areas of the matrix devoid of tissue. Attachment of chondroitin sulfate appeared to promote cellular ingrowth and cartilaginous tissue formation in both types of collagen matrices. Twelve weeks after implantation, the differences between the matrices were less pronounced. The deep parts of the subchondral defects were largely replaced by new bone with a concomitant degradation of the matrices. The original cartilage contours in defects with type I collagen-based matrices were repaired with fibro-cartilaginous tissue. Defects containing type II matrices showed an increase in the amount of superficial cartilage-like tissue. The original contour, however, was not completely restored in all animals, occasionally leaving a central depression or fissure. It is concluded that different types of collagen matrices induce different tissue responses in full-thickness articular cartilage defects. Type I collagen-based matrices are superior to guide progenitor cells from a subchondral origin into the defect. In type II collagen-based matrices cell migration is less, but invading cells are directed into a chondrocyte phenotype. Based on these observations it is suggested that a composite matrix consisting of a deep layer of type I collagen and a more superficial layer of type II collagen may be the matrix of choice for cartilage regeneration.

Animals↗
PubMed1990

Low affinity antibodies against collagen type II are associated with pathology in collagen-induced arthritis in mice.

The relationship between the functional affinity of antibodies against type II collagen (CII) and the development of arthritis was studied in mice with collagen-induced arthritis. The responses of DBA/1 strain mice were compared with those of mice selectively bred to produce antibodies of high functional affinity (HA mice) and low functional affinity (LA mice). HA and LA mice did not develop arthritis in response to immunization with CII whereas 86% of DBA/1 mice did, with 33% showing severe and 53% mild disease. Anti-CII antibodies of the highest titre, the lowest functional affinity, and the greatest affinity heterogeneity were associated with the development of the severest arthritis in DBA/1 mice: even in DBA/1 mice with moderate or no disease the amount of antibody and heterogeneity were higher and functional affinity lower than in either HA or LA mice. Antibodies of the G1, 2a, 2b and 3 subclasses were produced in all mice, and none of these alone accounted for the overall difference in IgG antibody titres or affinity in the groups of mice. Antibodies of the IgG2a subclass showed the closest association with the development of arthritis in the different groups. It is concluded that anti-CII antibodies of low functional affinity, and presumably also of the IgG2a subclass, influence the disease process in collagen arthritis.

Animals↗
PubMed1997

Serial analysis of autoantibody responses to the collagen-like region of Clq, collagen type II, and double stranded DNA in patients with systemic lupus erythematosus.

OBJECTIVE: To compare autoantibody responses to the collagen-like region of Clq (ClqCLR) with responses to double stranded DNA (dsDNA) and native rat collagen type II during changes of disease activity in patients with systemic lupus erythematosus (SLE). METHODS: IgG antibodies to ClqCLR, dsDNA, and collagen type II were determined by ELISA in serial samples from 33 patients with SLE with different disease manifestations. Antibodies to dsDNA were also detected with the Crithidia luciliae test. RESULTS: Distinct antibody responses in conjunction with flare were observed, but the markers were more clearly related to clinical groups and to severity of disease than to changes of disease activity. Anti-ClqCLR antibodies were detected in 2/10 patients with mild flares, 7/12 patients with severe extrarenal flares, and in 10/11 of the patients with active lupus glomerulonephritis. Findings with regard to anti-dsDNA antibodies were similar. Antibody responses to collagen type II were detected in 7/12 of the patients with severe extrarenal disease, and were less frequently found in the other patients. ELISA absorption and elution experiments with anti-ClqCLR antibodies in the patient sera did not suggest cross reactivity with collagen type II and dsDNA. CONCLUSION: Serial investigation of 33 patients with SLE showed that antibodies to ClqCLR and dsDNA are markers of severe SLE, particularly SLE with kidney involvement. Antibodies to collagen type II are possible markers of severe extrarenal SLE with vasculitis and serositis. Analysis of anti-ClqCLR antibodies provided no evidence of cross reactivity with collagen type II and dsDNA.

Antibodies, Antinuclear↗
PubMed1994

Studies on type II collagen and aggrecan production in human articular chondrocytes in vitro and effects of transforming growth factor-beta and interleukin-1beta.

Type II collagen and aggrecan are major components of the extracellular matrix of articular cartilage. Their biosynthesis and catabolism are regulated by chondrocytes. They may be used as markers of chondrocyte phenotype for cells cultured in vitro. Type II collagen gene expression was detected by amplification of type II collagen-specific sequences, using cDNA produced by reverse transcription of mRNA extracted from freshly isolated and cultured human articular chondrocytes by the polymerase chain reaction (PCR). The synthesis of gene product was confirmed by immunohistochemical localization of type II collagen in cartilage sections and in cultured chondrocytes. Aggrecan core protein was also immunolocalized in cartilage sections and in chondrocytes in culture. Expression of type II collagen or aggrecan was not detected immunohistochemically in skin or bone. These results demonstrate that human articular chondrocytes can be characterized in culture, by the combined application of PCR and immunohistochemistry. Interleukin-1beta (IL-1beta) may play an important role in the destruction of cartilage matrix in arthritis, whereas transforming growth factor-beta (TGFbeta) may have an opposing effect and their combined actions may modulate chondrocyte phenotype. The effect of rhIL-1beta and rhTGFbeta on the production of type II collagen by chondrocytes in culture was investigated. It was shown that TGFbeta enhanced the production of type II collagen, localized immunocytochemically, in cultured chondrocytes. IL-1beta inhibited expression of mRNA for type II collagen. The implications of this study, in terms of a better understanding of degenerative cartilage disease, are discussed.

Aggrecans↗
PubMed1997

Synergistic action of transforming growth factor-beta and insulin-like growth factor-I induces expression of type II collagen and aggrecan genes in adult human articular chondrocytes.

Reexpression of aggrecan and type II collagen genes in dedifferentiated adult human articular chondrocytes (AHAC) in suspension culture varied widely depending on the specific lot of bovine serum used to supplement the culture medium. Some lots of serum provided strong induction of aggrecan and type II collagen expression by AHAC while others did not stimulate significant production of these hyaline cartilage extracellular matrix molecules even following several weeks in culture. Addition of 50 ng/ml insulin-like growth factor-I (IGF-I) to a deficient serum lot significantly enhanced its ability to induce aggrecan and type II collagen mRNA. Given this observation, IGF-I and other growth factors were tested in defined serum-free media for their effects on the expression of these genes. Neither IGF-I nor insulin nor transforming growth factor beta (TGF-beta) alone stimulated induction of aggrecan or type II collagen production by dedifferentiated AHAC. However, TGF-beta 1 or TGF-beta 2 combined with IGF-I or insulin provided a strong induction as demonstrated by RNase protection and immunohistochemical assays. Interestingly, type I collagen, previously shown to be downregulated in serum supplemented suspension cultures of articular chondrocytes, persisted for up to 12 weeks in AHAC cultured in defined medium supplemented with TGF-beta and IGF-I.

Adult↗
PubMed1987

Inhibitory effects of anti-inflammatory drugs on type II collagen induced arthritis in rats.

The effects of steroidal and non-steroidal anti-inflammatory drugs on the established lesion of type II collagen induced arthritis in rats were evaluated by measuring the hind paw oedema and anti-type II collagen antibody titre. Dexamethasone, a steroidal anti-inflammatory drug, reduced the anti-type II collagen antibody titre and markedly suppressed the established lesion of type II collagen induced arthritis in rats. A rebound of the arthritis, i.e., a rapid recovery of the hind paw swelling took place after withdrawal of the treatment with steroidal anti-inflammatory drugs, including dexamethasone, prednisolone, and hydrocortisone. On the other hand, indomethacin, benoxaprofen, piroxicam, and tiflamizole, which are cyclo-oxygenase inhibitors in prostaglandin synthesis, had no effect on anti-type II collagen antibody titre, but suppressed the established lesion of the arthritis without causing an apparent rebound of the arthritis after withdrawal of the drug treatment. These results suggest that the level of anti-type II collagen antibodies has no relation to the intensity of hind paw swelling in the established lesion of the arthritis, though the antibodies contribute to the incidence of the arthritis. It also indicates that non-steroidal anti-inflammatory drugs having inhibitory action on cyclo-oxygenase are useful antiarthritic drugs without causing the rebound phenomenon, an untoward side effect after withdrawal of steroidal anti-inflammatory drugs.

Animals↗
PubMed2005

Abnormal response to physical activity in femurs after heterozygous inactivation of one allele of the Col2a1 gene for type II collagen in mice.

The objective of this study was to evaluate the influence of heterozygous inactivation of one allele of the type II collagen gene (Col2a1) on biomechanical properties and mineral density of bone under physical loading conditions. C57BL/6-TGN mice with heterozygous knockout (HZK) inactivation of Col2a1 gene and their nontransgenic littermate controls were housed in individual cages with running wheels for 9 and 15 months. The running activity of each mouse was monitored continuously throughout the experiment. Bone mineral density (BMD) of mice femora was measured using dual-energy X-ray absorptiometry (DXA) and peripheral quantitative computerized tomography (pQCT). Biomechanical properties were determined using three-point bending tests. Vertebral bone samples were prepared for quantitative polarized light microscopy and digital densitometry of proteoglycans. The concentration of total collagen and collagen cross-links were analyzed using high-performance liquid chromatograpy (HPLC). The average daily running distance was shorter for the HZK mice between the age of 4 and 15 months as compared with normal runners (P < 0.05). The ultimate breaking force was 14.8% and 23.6% (9 vs. 15 months) lower in HZK-runners than in wild-type runners. BMD of the femur was 6.1% lower in HZK-runners at the age of 9 months (P < 0.05). Physical activity increased cortical BMD in wild-type runners but not in the HZK runners at the age of 9 months. The collagen network of the HZK mice was less organized. There were only minor changes in BMD and mechanical and structural properties between sedentary HZK mice and their wild-type controls. Increased physical activity induced significantly lower bone density, mechanical properties, and organization of collagen fibers in male HZK mice. However, there were no major differences in biomechanical parameters between sedentary HZK and wild-type male mice. This suggests an important guiding role of collagen type II in bone remodelling and maturation.

Animals↗
PubMed2001

Type II collagen degradation in articular cartilage fibrillation after anterior cruciate ligament transection in rats.

OBJECTIVE: To investigate the kinetics of early cartilage changes in mechanically induced osteoarthritis (OA) and the association of these changes with damage to the type II collagen network. METHODS: Experimental OA was induced by anterior cruciate ligament transsection in the rat knee joint (ACLT-OA). Animals were sacrificed after 2, 7, 14, 28 and 70 days. Knee joints were evaluated using routine histology and immunohistochemistry for denatured (unwound) type II collagen to detect collagen damage. An antibody recognizing the collagenase cleavage site in type II collagen was used to study the role of collagenase in this process. RESULTS: The first changes of the articular cartilage after anterior cruciate ligament transection occurred in the superficial zone. These changes included loss of superficial chondrocytes, swelling of the remaining chondrocytes and superficial fibrillation. The swelling of the chondrocytes did not result from a change towards the hypertrophic phenotype, since these cells did not stain for type X collagen. A marked increase in denatured type II collagen staining was present in the fibrillated areas. Staining of the collagenase cleavage site showed the same distribution as denatured collagen but was clearly less intense. Collagen damage could never be detected before fibrillation occurred and was not present in non-fibrillated areas. CONCLUSIONS: These results indicate that in this model cartilage degeneration starts at the articular surface and that this degeneration is associated with a localized expression of type II collagen degradation products.

Animals↗
PubMed2006

Evaluation of biodegradable polyesters modified by type II collagen and Arg-Gly-Asp as tissue engineering scaffolding materials for cartilage regeneration.

Synthetic biodegradable polyesters poly(L-lactide) (PLLA) and poly(D,L-lactide-coglycolide) (PLGA) (50:50) modified by porcine type II collagen and an Arg-Gly-Asp (RGD)-containing protein were evaluated as scaffolds for cartilage regeneration in this study. Cytocompatibility of the polymer films was tested using immortalized chondrocytes. Neocartilage formation in vitro on cell-seeded scaffolds was further examined using primary porcine chondrocytes. The inflammatory response of the scaffolds was evaluated subcutaneously in rats. A pilot animal study was conducted, in which rabbit allogeneic chondrocyte-seeded scaffolds were implanted to repair the defected rabbit knee cartilage. The results demonstrated that PLGA as well as its blends with PLLA had better cell growth than pure PLLA, and that type II collagen enhanced, but RGD inhibited cell proliferation. Scaffolds made of blended PLLA/PLGA had larger dynamic compressive modulus compared to scaffolds made of PLLA or PLGA single polymer. Chondrocyte-seeded scaffolds modified by type II collagen without RGD had the greater number of cells as well as higher glycosaminoglycan (GAG) and collagen contents compared to scaffolds without type II collagen modification or scaffolds further modified with RDG. Type II collagen modification prevented infiltration by host tissue and capsule formation. Unmodified PLLA and PLLA/PLGA constructs demonstrated persisting inflammatory response after 6 months, while all type II collagen-modified PLLA/PLGA constructs showed complete repair and no inflammation. Partial or full repair was observed after 2 months of postimplantation in type II collagen-modified PLLA/PLGA constructs, with equal cellularity and 75-80% matrix contents of a normal rabbit articular cartilage. It was concluded that PLLA/PLGA blended scaffolds modified by type II collagen were a potential tissue engineering scaffold for cartilage regeneration.

Analysis of Variance↗