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PubMed1984

Type II collagen-induced arthritis in mice. II. Passive transfer and suppression by intravenous injection of anti-type II collagen antibody or free native type II collagen.

The passive transfer of high levels of anti-type II collagen antibody from mice with type II collagen-induced arthritis may transfer arthritis to syngeneic recipient animals. However, the transfer of either arthritogenic or sub-arthritogenic doses of polyclonal anti-type II collagen antibody, or non-arthritogenic monoclonal anti-type II collagen antibody may protect mice against the subsequent induction of arthritis by type II collagen. A protective effect was also observed in mice given free native type II collagen intravenously before the administration of collagen in an arthritogenic protocol.

Animals↗
PubMed1980

Demonstration of antibodies to denatured type I and type II collagen in juvenile rheumatoid arthritis, Still's syndrome and controls by [14C] collagen radioimmunoassay.

From 88 sera of patients with juvenile rheumatoid arthritis 30.6% showed antibodies to denatured type I collagen an 31.8% antibodies to type II collagen, a percentage which corresponds to radioimmunoassay results in adult RA. Rheumatoid factors were demonstrated with Waaler-Rose test in 14.7% and with latex test in 6.8% of investigated patients. Results of investigations with collagen types I and II correlated in 73.7%. Whilst type I collagen antibodies were found with equal frequency in active and non-active stages, type II antibodies were twice as frequent in active stages as in non-active stages. Sixteen sera of children with non-rheumatoid diseases had no collagen antibodies. JRA sera and controls differed with statistical significance in regard to collagen antibodies. 36 sera of children with Still's syndrome showed antibodies to type I collagen in 13.8% and antibodies to type II collagen in 33.3%. Both types of antibodies appeared more frequently in clinically active stages. The sera differed from controls with statistical significance in regard to collagen antibodies.

Adolescent↗
PubMed1989

Widespread distribution of type II collagen during embryonic chick development.

Type II collagen is a major component of hyaline cartilage, and has been suggested to be causally involved in promoting chondrogenesis during embryonic development. In the present study we have performed an immunohistochemical analysis of the distribution of type II collagen during several early stages of embryonic chick development. Unexpectedly, we have found that type II collagen is widely distributed in a temporally and spatially regulated fashion in basement membranes throughout the trunk of the embryo at stages 14 through 19, including regions with no apparent relationship to chondrogenesis. Immunohistochemical staining with two different monoclonal antibodies against type II collagen, as well as with an affinity-purified polyclonal antibody, is detectable in the basement membranes of the neural tube, notochord, auditory vesicle, dorsal/lateral surface ectoderm, lateral/ventral gut endoderm, mesonephric duct, and basal surface of the splanchnic mesoderm subjacent to the dorsal aorta, and at the interface between the epimyocardium and endocardium of the developing heart. In contrast, immunoreactive type IX collagen is detectable only in the perinotochordal sheath in the trunk of the embryo at these stages of development. Thus type II collagen is much more widely distributed during early development than previously thought, and may be fulfilling some as yet undefined function, unrelated to chondrogenesis, during early embryogenesis.

Animals↗
PubMed1982

Type II collagen autoimmunity in otosclerosis and Meniere's Disease.

Antibodies to collagen types I, II, and IV were measured in patients with otosclerosis and patients with Meniere's disease. Levels of antibodies to type II collagen were significantly higher in these patients than in control subjects, while no differences were found among levels of antibodies to collagen type I or type IV. These observations suggest a possible role for type II collagen autoimmunity in the etiology of otosclerosis and Meniere's disease.

Autoantibodies↗
PubMed1989

Common epitopes in Clq and collagen type II.

An epitope common for collagen type II and Clq was demonstrated by specific binding of a monoclonal anti-collagen type II antibody, MAb B1, to purified Clq. This was further substantiated by the affinity shown between F(ab')2 fragments of anti-Clq antibodies and rat chondrosarcoma collagen type II. The interaction between MAb B1 and Clq was demonstrated in hemolytic assays, in an enzyme-linked biotin-avidin assay and by the binding of Clq to MAb B1 immobilized on Sepharose 4B beads. MAb B1 recognized only purified Clq and not the macromolecular Cl complex, indicating that the epitope for MAb B1 was situated in the collagen-like region in Clq, where Clq and Cls are anchored. The binding of the purified collagen-like fragment of Clq to radiolabelled MAb B1 confirmed these findings. The affinity between MAb B1 and Clq was significantly increased if Clq was first reacted with heat aggregated IgG, indicating a demasking of the reactive epitope on binding to the aggregated IgG. The present findings raise the question of the pathogenetic significance of the presence of anti-collagen type II antibodies and free Clq, both of which are frequently seen in high amounts in rheumatoid arthritis.

Animals↗
PubMed1989

Origin of the autoreactive anti-type II collagen response. II. Specificities, antibody isotypes and usage of V gene families of anti-type II collagen B cells.

Autoantibodies play an important role in the pathogenesis of type II collagen-induced arthritis in mice. We have earlier reported a high frequency of cells producing anti-CII autoantibodies and a low frequency of cells producing multispecific antibodies, in regional lymph nodes 9 to 11 days after primary immunization with CII. It is shown here that anti-CII antibodies produced during primary immune response are IgG-antibodies mainly of IgG2a, IgG1 and IgG2b subclasses while IgM antibodies dominate primary responses elicited by OVA and denatured CII as analyzed with a large panel of hybridomas. Anti-CII antibodies generated during the primary response recognize at least five different epitopes on the CII molecule. The specificities of these antibodies for various epitopes result from combinational association of products encoded by genes derived from various VH and VK families and/or by the occurrence of somatic mutations. It is suggested that the primary anti-CII autoantibody response involves activation of memory B cells and is in this aspect different from the origin of "natural" autoantibodies.

Animals↗
PubMed2003

Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen.

The functional integrity of articular cartilage is dependent on the maintenance of the extracellular matrix (ECM), a process which is controlled by chondrocytes. The regulation of ECM biosynthesis is complex and a variety of substances have been found to influence chondrocyte metabolism. In the present study we have investigated the effect of degraded collagen on the formation of type II collagen by mature bovine chondrocytes in a cell culture model. The culture medium was supplemented with collagen hydrolysate (CH) and biosynthesis of type II collagen by chondrocytes was compared to control cells treated with native type I and type II collagen and a collagen-free protein hydrolysate. The quantification of type II collagen by means of an ELISA technique was confirmed by immunocytochemical detection as well as by the incorporation of (14)C-proline in the ECM after a 48 h incubation. Chondrocytes in the control group were maintained in the basal medium for 11 days. The presence of extracellular CH led to a dose-dependent increase in type II collagen secretion. However, native collagens as well as a collagen-free hydrolysate of wheat proteins failed to stimulate the production of type II collagen in chondrocytes. These results clearly indicate a stimulatory effect of degraded collagen on the type II collagen biosynthesis of chondrocytes and suggest a possible feedback mechanism for the regulation of collagen turnover in cartilage tissue.

Animals↗
PubMed1986

Gastric administration of type II collagen delays the onset and severity of collagen-induced arthritis in rats.

Rats were per-gastrically dosed by gavage with collagen type II (CII) in solution and were shown, as a result, to be subsequently resistant to the induction of disease by CII administered parenterally in Freund's incomplete adjuvant. Disease onset was delayed and the severity was reduced. There was no concomitant reduction in the systemic antibody response to CII. Gavage with CII did not in itself induce systemic anti-CII antibodies and did not cause symptoms of arthritis. The results indicate that materials specifically cross-reactive with autoantigens can be absorbed through the gut and can modify susceptibility to autoimmune disease.

Animals↗
PubMed1997

Type II collagen serology: a guide to clinical responsiveness to oral tolerance?

A double-blind placebo-controlled randomized trial of oral collagen type II (CII) treatment in rheumatoid arthritis was completed in Berlin. Anti-CII antibody titres were measured before and after the treatment. They showed that: (1) the titre prior to treatment did not identify a responder subgroup, (2) the treatment reduced CII antibody titres, but only in those patients making a clinical response and (3) administration of 10 mg CII per day reduced the titre in these subsets more effectively than 1 mg per day. Although the data are limited, they suggest that a titre drop may be useful for identifying those patients who respond to this form of treatment and that the drop may be a valid parameter for detecting the impact of the treatment on the immune system.

Administration, Oral↗
PubMed1997

Skeletal development in transgenic mice expressing a mutation at Gly574Ser of type II collagen.

Skeletal development of transgenic mice with a type II collagen mutation was analyzed and compared with wild-type littermates. The single base substitution in Col2a1 resulted in a glycine to serine mutation within the helical domain and corresponded to one previously identified in a patient with the lethal human chondrodysplasia, hypochondrogenesis (Horton et al. [1992] Proc. Natl. Acad. Sci. U.S.A. 89:4583-4587). Skeletal staining of embryos from 14.5 through 18.5 days of gestation demonstrated a dwarf phenotype in the transgenic embryos, most notably short limb bones and vertebral column that was first detected at 15.5 days post-coitus. In addition to the reduced length, the extent of ossification was less in the transgenic mice. The architecture of the long bone growth plate was abnormal in the transgenic tissue, in particular there was no discernible proliferative zone. There were few stacks of characteristically flattened cells and the overall length of the growth plate in the mutant embryos was reduced. At the ultrastructural level, there were fewer collagen fibrils present in the transgenic mouse cartilage compared to that of wild-type littermates. Ultrastructural localization of collagen types II, IX and XI revealed a similar pattern between the transgenic and wild-type pups, suggesting that the collagen fibrils present in the matrix of littermates with both phenotypes had a similar composition. Skeletal analysis and cartilage histochemistry indicated that effect of the type II collagen mutation was to reduce the density of the collagen fibrils within the cartilage matrix which was associated with delayed bone formation and resulted in a short-limbed phenotype.

Animals↗
PubMed1989

Covalent structure of collagen. Amino acid sequence of an arthritogenic cyanogen bromide peptide from type II collagen of bovine cartilage.

Bovine articular type II collagen was prepared by limited pepsin digestion, differential salt fractionation and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type II collagen alpha chains yielded twelve distinct peptides designated CB1-12. The peptide alpha 1(II)-CB11 was isolated by carboxymethylcellulose chromatography and Sephadex G-75S gel filtration. Automated Edman degradation together with chymotrypsin, thermolysin and trypsin digestion enabled identification of its complete amino acid sequence. Compared with type I and type III collagen, the data show similarity with alpha 1(I)-CB8 and alpha 1(III)-CB6-1-8-10-2 peptides, respectively. The peptide is located within residues 124-402 of the alpha 1(II) collagen chain and with its identification, now extends the known amino acid sequence of bovine type II cartilage collagen to 660 amino acid residues including alpha 1(II)-CB1-2-6-12-11-8-10 (partial). This corresponds to alpha 1(I)-CB0-1-2-4-5-8-3-7 (partial; 1-660) and alpha 1(III)-CB3A-3B-3C-7-6-1-8-10-2-4-5 (partial; 1-660) of bovine alpha 1(I) and alpha 1(III) collagen chains.

Amino Acid Sequence↗
PubMed2002

Epitope-specific recognition of type II collagen by rheumatoid arthritis antibodies is shared with recognition by antibodies that are arthritogenic in collagen-induced arthritis in the mouse.

OBJECTIVE: To analyze the fine specificity of IgG autoantibodies in sera from rheumatoid arthritis (RA) patients for type II collagen (CII) epitopes that are arthritogenic in collagen-induced arthritis (CIA), a relevant murine model of RA. METHODS: For enzyme-linked immunosorbent assay (ELISA) analysis of conformation-dependent autoantibody binding, recombinant chimeric collagens that harbor the respective CII epitopes as an insertion within the frame of a constant type X collagen triple helix were constructed. In addition, synthetic peptides mimicking the native collagen structures were applied for the first time in the ELISA assessment of humoral CII autoimmunity. RESULTS: The pathogenicity of IgG responses to certain CII determinants in CIA was demonstrated by arthritis development in BALB/c mice upon the combined transfer of 2 mouse monoclonal antibodies specific for precisely mapped conformational CII epitopes (amino acid residues 359-369 [C1(III)] and 551-564 [J1]), whereas antibodies to another epitope (F4) were not arthritogenic. To test whether human autoimmune responses are similarly directed to these conserved CII determinants, serum IgG was analyzed. The prevalence of sera with increased IgG binding to the C1(III) epitope was significantly higher in RA compared with sera from healthy donors or from patients with other rheumatic conditions, e.g., osteoarthritis (OA), systemic lupus erythematosus (SLE), or relapsing polychondritis (RP), whereas levels of antibodies specific for the nonarthritogenic F4 epitope were associated with OA rather than RA. CONCLUSION: Autoimmunity to CII, although detectable in different rheumatic conditions, differs in fine specificity between distinct disease entities. In RA, in contrast to degenerative joint disease, RP, and SLE, autoantibody responses are directed to an evolutionary conserved CII structure that is also targeted by pathogenic autoimmune responses in murine models of arthritis.

Animals↗
PubMed1989

Anti-type II collagen antibody in naturally occurring canine joint diseases.

Autoimmunity to collagen was investigated in several naturally occurring arthropathies of the dog. Increased levels of serum anti-native collagen type II antibody, as assessed by ELISA, were shown in 72.4% of dogs with rheumatoid arthritis (RA), 88% of dogs with infective arthritis (IA) and 52% of dogs with osteoarthritis (OA) (p less than 0.001). The mean levels of antibody in cruciate disease patients (CR) were also significantly increased compared to control dogs (p less than 0.01). Serum anti-collagen antibody in OA dogs correlated with that in precipitated serum immune complexes. There was also a correlation between anti-collagen antibody level in synovial fluid and in synovial fluid complexes in dogs with rupture of the cranial cruciate ligament. In all patient groups, collagenase digestion of polyethylene glycol (PEG) precipitates from sera and synovial fluids caused a significant rise in specific antibody levels to collagen, indicating the presence of collagen-anti-collagen complexes in all arthropathies. In dogs with RA, the levels of collagen-specific antibody in synovial fluid complexes correlated with the total IgG in these complexes. These findings implicate collagen-anti-collagen complexes in the pathogenesis of naturally occurring joint diseases in the dog, but they are unlikely to be the primary aetiological mechanism.

Animals↗
PubMed1988

Type II collagen distribution in rodents.

The anatomical distribution of type II collagen in animal ears was studied by immunohistochemical techniques, using defined monoclonal antibodies to type II collagen. Type II collagen was observed in the cartilage plate of the auricle and external auditory meatus, tympanic annulus, lamina propria of tympanic membrane (pars tensa), interossicular joints, stapes footplate, eustachian tube cartilage, enchondral layer and globuli interossei of the otic capsule, Rosenthal canal, cribriform base, osseous spiral lamina, spiral ligament, limbus, tectorial membrane, semicircular canal membrane and subepithelial layer of the ampullary crista, utricular and saccular maculae, and the endolymphatic duct and proximal part of the sac.

Animals↗
PubMedDate not supplied

[Therapy with oral type II collagen as a new possibility of selective immunosuppression in therapy of rheumatoid arthritis].

Suppressor T cells in the mucosa of the gut are activated by absorbed antigen in order to avoid a systemic immune response to this antigen. This long known phenomenon of oral tolerance is now used in the treatment of rheumatoid arthritis with oral collagen type II which is the most important protein of cartilage. Although the role of collagen II in initiating and maintaining the immune response in the joint is not clear, these suppressor CD8+T cells can be stimulated in a trigger-specific and effector-nonspecific way by contact with collagen II in the joint. It is assumed that a local immunosuppression then takes place through the secretion of inhibitory cytokines, mainly TGF beta. Clinical studies in the treatment of rheumatoid arthritis are presently being conducted in Boston and Berlin.

Administration, Oral↗
PubMed1992

Activation of collagen type II expression in osteoarthritic and rheumatoid cartilage.

In situ hybridization and immunohistochemical techniques were applied to investigate gene expression and extracellular deposition of collagen type II in normal, osteoarthritic and rheumatoid human articular cartilage. Normal cartilage showed an essentially even extracellular distribution of type II collagen with poly- and monoclonal antibodies, while only a few cells were positive for alpha 1(II) collagen mRNA. In situ hybridization of osteoarthritic and rheumatoid cartilage, however, showed strong enhancement of type II collagen gene expression; transcripts were observed predominantly in the upper middle zone of the articular cartilage while the upper layer was mostly negative and correlated with a zone of reduced proteoglycan staining. The elevated mRNA levels frequently coincided with pericellular immunostaining for type II collagen, indicative for enhanced synthesis of the protein. In two samples, however, pericellular loss of collagen type II staining was found despite positive cytoplasmic signals with the alpha 1(II) RNA probe, suggesting enhanced collagen destruction. Control hybridization with a probe for 18S rRNA revealed very few negative cells throughout both normal and arthritic cartilage samples, ruling out major cell necrosis in the specimens investigated. Thus, our observations identify sites of activated type II collagen synthesis in osteoarthritic cartilage that were predicted by previous biochemical studies and support the notion that damaged cartilage attempts to restore matrix by enhanced synthesis of its components.

Adolescent↗
PubMed2006

Autoimmunity to citrullinated type II collagen in rheumatoid arthritis.

The production of autoantibodies to citrullinated type II collagen and the citrullination of type II collagen were analyzed in rheumatoid arthritis. Autoantibodies to citrullinated type II collagen were detected in 78.5% of serum samples from 130 rheumatoid arthritis patients. Autoantibodies to native noncitrullinated type II collagen were detected in 14.6% of serum samples, all of which were positive for anti-citrullinated type II collagen antibodies. Serum samples were also positive for anti-citrullinated type II collagen antibodies in 1 of 31 systemic lupus erythematosus patients and 2 of 55 patients with osteoarthritis of the knee. In contrast, sera samples from 24 systemic sclerosis patients, 21 dermatomyositis/polymyositis patients, 21 ankylosing spondylitis patients, and 18 psoriatic arthritis patients were all negative for anti-citrullinated type II collagen antibodies. Anti-citrullinated type II collagen antibodies and fragments of citrullinated type II collagen were found in the synovial fluid obtained from affected knee joints of 15 rheumatoid arthritis patients. Moreover, anti-citrullinated type II collagen antibodies were isolated from the synovium of affected knee joints in 8 rheumatoid arthritis patients using antigen/antibody immunocomplex dissociation buffer but not by using standard buffers. These findings indicate that autoantibodies that react with citrullinated type II collagen are specifically produced and that immunocomplexes composed of fragments of citrullinated type II collagen and autoantibodies are deposited in the inflamed articular synovium in rheumatoid arthritis patients. Assaying for the presence of anti-citrullinated type II collagen antibodies may therefore be useful for diagnosing rheumatoid arthritis, and the deposition of these immunocomplexes in the articular synovium may be involved in pathogenesis.

Antigen-Antibody Complex↗