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PubMed2003

Maturation-dependent thiol loss increases chondrocyte susceptibility to apoptosis.

The major aim of the current investigation was to evaluate the role of thiols during chondrocyte maturation and apoptosis. Using a thiol-sensitive fluorescent probe, we found that in chick growth plate chondrocytes, hypertrophy is accompanied by a decrease in the glutathione content. In this study, we show that the maturation-dependent loss of thiol, although not causing death of maturing chondrocytes, drastically increases susceptibility to apoptosis by oxidative and nitrosoactive stress. To investigate how the loss of thiol content in cultured chondrocytes affects the expression of the hypertrophic phenotype, we chemically manipulated intracellular thiol levels and analyzed the expression of important maturation markers. We found that thiol depletion causes a decrease in the expression of osteopontin, type X and type II collagen and a significant loss of alkaline phosphatase activity, suggesting that the expression of the hypertrophic phenotype is tightly regulated by redox levels in chondrocytes. Furthermore, severe thiol depletion profoundly affected cell survival under oxidative and nitrosoactive stress. It was concluded that the loss of thiol reserve is not only linked to the expression of the hypertrophic phenotype but also influenced chondrocyte survival, linking chondrocyte maturation and the activation of the apoptotic pathway.

Acetylcysteine↗
PubMed1993

Direct extraction of gelatinases from rat bone.

Many studies have shown that gelatinases are secreted into the medium of cultures of various cell and tissue types, including bone cells. It is not clear, however, to what extent the culture process is responsible for inducing the expression of these proteases. In the present study, gelatinolytic enzymes were extracted directly from bone and other tissues and identified as bands of activity on SDS-PAGE enzymograms using gelatin as the substrate. Two forms of gelatinase (72-kDa and 92-kDa) were present in extracts of normal young rat bone. Yields were markedly higher from compact bone than from other tissues (blood, marrow, tendon, cancellous bone, articular cartilage, and skin). More 92-kDa than 72-kDa gelatinase was extracted from bone. The proteolytic specificity of the 92-kDa gelatinase isolated from the bone extract was shown to be similar to that reported for the enzyme isolated from tissue culture media. Native type I collagen was not cleaved but heat denatured type I collagen (gelatin) and native type IV, type V, type IX and type XI collagens were degraded. The proteolytic activity was inhibited by EDTA. The results indicate that more gelatinases can be extracted from bone tissue than from other tissues using mild extraction conditions. The cellular origin and function of these enzymes in bone remain to be defined.

Animals↗
PubMed2001

Pseudoachondroplasia and multiple epiphyseal dysplasia: New etiologic developments.

Pseudoachondroplasia (PSACH) (OMIM#177170) and multiple epiphyseal dysplasia (MED) are separate but overlapping osteochondrodysplasias. PSACH is a dominantly inherited disorder characterized by short-limb short stature, loose joints, and early-onset osteoarthropathy. The diagnosis is based on characteristic clinical and radiographic findings. Only mutations in the cartilage oligomeric matrix protein (COMP) gene have been reported in PSACH, and all family studies have been consistent with linkage to the COMP locus on chromosome 19. Multiple epiphyseal dysplasia (MED) is a relatively mild chondrodysplasia but like PSACH, MED causes early-onset joint degeneration, particularly of the large weight-bearing joints. Given the clinical similarity between PSACH and MED, it was not surprising that the first MED locus identified was the COMP gene (EDM1). Mutations causing MED have now been identified in five other genes (COL9A1, COL9A2, COL9A3, DTDST, and MATN3), making MED one of the most genetically heterogeneous disorders. This article reviews the clinical features of PSACH and MED, the known mutations, and the pathogenetic effect of COMP mutations on the cartilage extracellular matrix.

Achondroplasia↗
PubMed1997

Collagen IX.

Collagen IX was identified as a distinct component of cartilage about 10 years ago. Composed of three polypeptide chains, its heterotrimeric molecules are located on the surface of type II collagen fibrils in cartilage. The interaction between collagens II and IX is stabilized by covalent crosslinks. The location of collagen IX molecules on fibril surfaces suggests that they represent macromolecular bridges between fibrils and other matrix components in cartilage, and that collagen IX is important for the cohesive and compressive properties of cartilage. Transgenic mice with mutations in a type IX gene develop normally, but show degenerative changes in articular cartilage after birth. Additional evidence for the importance of collagen IX in human articular cartilage comes from the recent finding that a mutation in one of the collagen IX genes causes multiple epiphyseal dysplasia. The mild complaints in affected individuals with the mutation suggest that mutations in type IX collagen genes may represent genetic risk factors for late onset osteoarthritis.

Animals↗
PubMed1986

The effects of mechanical stability on the macromolecules of the connective tissue matrices produced during fracture healing. I. The collagens.

The distribution of types I, II, III, V and IX collagens in healing fractures of the rabbit tibia has been demonstrated by immunofluorescent techniques. It has also been shown that the mechanical stability of the healing fracture affects both the distribution and types of the collagens present. The initial fibrous matrix contains types III and V collagens; type I collagen was only located in this matrix if unfixed tissue was used. In mechanically stable fractures, cancellous bone forms over the entire periosteal surface by 5-7 days; type I collagen is laid down within the previous fibrous matrix. The trabeculae are heterogeneous in their collagen content. The cavities contain a matrix of types III and V collagens. Small nodules of cartilage may be present between 7 and 14 days; these contain types II and IX collagens. In mechanically unstable fractures, cancellous bone is initially formed away from the fracture gap. The fibrous tissue over the gap is replaced by cartilage; types II and IX collagens are laid down on the pre-existing fibrous matrix. The cartilage is replaced by endochondral ossification. At the ossification front, type I collagen is found around the chondrocyte lacunae of the spicules of cartilage. The new trabeculae contain a core of cartilage which is surrounded by a bone matrix of types I and V collagens. The fracture gaps are invaded by fibrous tissue, which contain types III and V collagens. this is later replaced by cancellous bone.

Animals↗
PubMed1993

Transcriptional modulation of cartilage-specific collagen gene expression by interferon gamma and tumour necrosis factor alpha in cultured human chondrocytes.

To examine the possibility that cytokines produced in inflamed joint tissues may contribute to the loss of articular cartilage by causing inhibition of synthesis of cartilage-specific matrix macromolecules, we studied the effects of interferon gamma (IFN gamma) and tumour necrosis factor alpha (TNF alpha), alone and in combination, on the expression of the genes for types-II, -IX and -XI collagens in cultured human chondrocytes. Chondrocytes isolated from human fetal epiphyseal cartilage by sequential enzymic digestions were cultured in the presence of IFN gamma (30 pM), TNF alpha (15 pM) or a combination of suboptimal concentrations of both cytokines (1.5 pM IFN gamma plus 0.3 pM TNF alpha). IFN gamma caused a maximal decrease of 23.3-32.6% in the biosynthesis of collagen by chondrocytes. TNF alpha was a more potent inhibitor causing a 42.8-45.3% decrease at one-half the concentration of IFN gamma. A synergistic inhibitory effect of 58.2% was observed with the combination of 1.5 pM IFN gamma plus 0.3 pM TNF alpha. Electrophoretic analysis of the biosynthesized proteins showed a co-ordinate decrease in the production of the three cartilage-specific collagen types II, IX and XI. These effects were accompanied by parallel changes in the steady-state levels of their corresponding mRNAs. In vitro transcription assays showed that the collagen inhibitory effects of the cytokines occurred largely at the transcriptional level. Similar effects of the cytokines were observed on biosynthesis of types-II, -IX and -XI collagens and steady-state mRNA levels for type-II collagen by chondrocytes obtained from adult articular cartilage. These observations indicate that IFN gamma and TNF alpha can induce a synergistic inhibition of the synthesis of cartilage-specific collagens by fetal and adult human chondrocytes and suggest that these effects may contribute to the articular cartilage loss that occurs in inflammatory joint diseases.

Cartilage, Articular↗
PubMed2006

Chondrocyte phenotype in engineered fibrous matrix is regulated by fiber size.

A biomaterial scaffold acting as a functional substitute for the native extracellular matrix provides space for cell accommodation. In this study, we seeded chondrocytes, isolated from 4- to 6-month-old calves, in 2 types of poly(L-lactide) scaffolds, composed of micro- and nanofibers, and compared the effects on cellular activities. Scanning electron microscopy revealed a well-spread morphology for chondrocytes grown on microfibers. In contrast, chondrocytes on the nanofibers were found to have a rounded morphology and displayed a disorganized actin cytoskeletal structure compared to the organized cytoskeleton seen in well-spread chondrocytes culture on the microfibrous scaffold. Both scaffolds supported chondrocyte proliferation, with a higher rate seen in cultures in nanofibrous scaffold. Quantitative reverse transcription-polymerase chain reaction analysis showed that both cultures supported expression of collagen types I and II and aggrecan. Biochemical analysis showed a higher level of sulfated glycosaminoglycan in the nanofiber culture, confirmed by more intense alcian blue histologic staining. The nanofiber cultures also showed higher immunostaining for collagen types II and IX, aggrecan, and cartilage proteoglycan link protein. Based on these results, we conclude that chondrocytes respond differently to fibrous scaffolds of varying diameters, and that the scaffolds made of nanofibrous biomaterial promote efficient cell-based cartilage tissue engineering.

Aggrecans↗
PubMed1990

Isolation of bovine type X collagen and immunolocalization in growth-plate cartilage.

Type X collagen was extracted with 1 M-NaCl and 10 mM-dithiothreitol at neutral pH from fetal-bovine growth cartilage and purified to homogeneity by using f.p.l.c. gel filtration on a Superose 12 column, followed by ion-exchange chromatography on a Mono Q column. The purified protein migrates in SDS/polyacrylamide gels with an apparent Mr of 58,000 under reducing conditions and as a high-Mr oligomer in its unreduced form. The amino acid composition is similar to the published composition of chick type X collagen. Pepsin digestion at 4 degrees C decreases the Mr of the monomer to 43,000; purified bacterial collagenase digests most of the molecule, leaving a non-collagenous domain of apparent Mr 15,000, which probably represents the C-terminal globular domain. The IgG fraction from a rabbit antiserum raised against purified bovine type X collagen was specific for this collagen by the criteria of e.l.i.s.a. and immunoblotting after immunoabsorption with collagen types I, II, IX and XI. Immunofluorescence localization of type X collagen in sections of fetal-bovine and human cartilage was possible after acetone fixation of sections and hyaluronidase treatment. Type X collagen was restricted to the zone of hypertrophic and calcified cartilage inside the bone spicules of the growth plate.

Amino Acids↗
PubMed1996

Identification and immunolocalization of type X collagen at the ligament-bone interface.

In some ligaments, ligamentous collagen fibrils attach to bone by first passing through non-mineralized and mineralized fibrocartilage present at the ligament-bone interface. To understand better the function of these fibrocartilages, collagens present at the femoral insertion of the bovine medial collateral ligament were isolated and characterized. Types II and IX collagens were identified in pepsin digests of the tissue in addition to type X collagen originally thought to be associated with the cartilages undergoing endochondral bone formation. Presence of type X collagen was confirmed by immunoblotting and by immunofluorescence localization using laser confocal microscopy. Type X collagen was localized predominantly in the mineralized zone of the ligament insertion. These data indicated that type X collagen may play a role in ligament attachment to bone.

Animals↗
PubMed1998

Articular cartilage: tissue design and chondrocyte-matrix interactions.

The unique biologic and mechanical properties of articular cartilage depend on the design of the tissue and the interactions between the chondrocytes and the matrix that maintain the tissue. Chondrocytes form the macromolecular framework of the tissue matrix from three classes of molecules: collagens, proteoglycans, and noncollagenous proteins. Type II, IX, and XI collagens form a fibrillar meshwork that gives the tissue as form and tensile stiffness and strength. Type VI collagen forms part of the matrix immediately surrounding the chondrocytes and may help the chondrocytes to attach to the macromolecular framework of the matrix. Large aggregating proteoglycans (aggrecans) give the tissue its stiffness to compression and its resilience and contribute to its durability. Small proteoglycans, including decorin, biglycan, and fibromodulin, bind to other matrix macromolecules and thereby help to stabilize the matrix. They may also influence the function of the chondrocytes and bind growth factors. Anchorin CII, a noncollagenous protein, appears to help to anchor chondrocytes to the matrix. Cartilage oligomeric protein may have value as a marker of turnover and degeneration of cartilage, and other noncollagenous proteins, including tenascin and fibronectin, can influence interactions between the chondrocytes and the matrix. The matrix protects the cells from injury due to normal use of the joint, determines the types and concentrations of molecules that reach the tells and helps to maintain the chondrocyte phenotype. Throughout life, the tissue undergoes continual internal remodeling as the cells replace matrix macromolecules lost through degradation. The available evidence indicates that normal matrix turnover depends on the ability of chondrocytes to detect alterations in the macromolecular composition and organization of the matrix, including the presence of degraded molecules, and to respond by synthesizing appropriate types and amounts of new molecules. In addition, the matrix acts as a signal transducer for the cells. Loading of the tissue due to use of the joint creates mechanical, electrical, and physicochemical signals that help to direct the synthetic and degradative activity of chondrocytes. A prolonged severe decrease in the use of the joint leads to alterations in the composition of the matrix and eventually to loss of tissue structure and mechanical properties, whereas use of the joint stimulates the synthetic activity of chondrocytes and possibly the internal tissue remodeling Aging leads to alterations in the composition of the matrix and the activity of the chondrocytes, including the ability of the cells to respond to a variety of stimuli such as growth factors. These alterations may increase the probability of degeneration of the cartilage.

Animals↗
PubMed2001

Discoidin domain receptor (DDR) 1 and 2: collagen-activated tyrosine kinase receptors in the cornea.

Discoidin domain receptor (DDR) 1 and 2 have recently been found to serve as receptors for several collagen types. These receptors have been found to modulate cell proliferation and metalloprotease expression in response to collagen stimulation. The purpose of this study was to examine expression of DDR1 and DDR2 in the cornea and to determine the effect of several collagen types on proliferation and response to pro-apoptotic cytokines by corneal fibroblasts. DDR1 and DDR2 mRNAs were detected by RT-PCR. Proteins were detected by immunocytochemistry and immunoprecipitation with Western blotting. Cell proliferation in response to acetic acid-solubilized collagen type I, II, IV, IX or X was determined by cell counting. The effect of these collagen types on Fas-stimulating antibody-induced cell death was determined by trypan blue assay. DDR1 and DDR2 mRNAs were detected in each major human cell type of the cornea. Both were also detected in ex vivo human corneal epithelium. DDR1 and DDR2 proteins were detected in all three major cell types in culture and in human corneal tissue. Collagen types I, II, IV, IX and X stimulated proliferation, but had no effect on Fas-mediated apoptosis, of corneal fibroblasts. DDR1 and DDR2 tyrosine kinase receptors are expressed in the cornea. Collagen-stimulated mitosis of corneal fibroblasts in culture is likely mediated by the DDR receptors. Collagen had no effect on Fas-mediated apoptosis of corneal fibroblasts.

Analysis of Variance↗
PubMed1998

[Matrix gene expression pattern as indicators of the biology of cartilage-forming tumors].

Mesenchymal cells can be characterized by the expression of specific sets of extracellular matrix (ECM) proteins. The aim of our study was to identify such expression pattern in cartilage-forming tumours in order to elucidate the biology of these neoplasms. In situ hybridisation and immunohistochemistry for various ECM components were performed on enchondromas, conventional chondrosarcomas of various grades and dedifferentiated chondrosarcomas. Chondroid areas of all investigated neoplasms showed strong expression of cartilage collagen types II and IX and aggrecan core and link protein. Focally, also the expression of other collagen subtypes such as collagen type X and collagen types I and III was observed. Non-chondroid areas of dedifferentiated chondrosarcomas lacked any expression of the cartilage-typical gene products and were instead positive for interstitial collagen types I, III, and VI. The hallmark of all investigated cartilaginous neoplasms was the expression of the chondrocyte-typical genes. Neoplastic chondrocytes showed the differentiation facettes similar to their physiological counterparts resulting in the high heterogeneity, which is characteristic for chondrogenic neoplasms. A different biology is suggested for dedifferentiated chondrosarcomas, in which the "dedifferentiated" portion is proposed to have a separate (e.g. fibroblastic) mesenchymal origin.

Bone Neoplasms↗
PubMed1990

Fibroblast-derived J1 adhesion glycoproteins show binding properties to extracellular matrix constituents different from those of central nervous system origin.

The J1 extracellular adhesion molecule from mouse brain consists of several immunochemically related glycoproteins of different molecular weights and distinct functional properties. Like the brain J1 glycoproteins, the fibroblast-derived J1 glycoproteins interact with all collagen types tested (collagen G and types I-IV and IX), as measured by binding of 125I-labeled J1 glycoproteins to immobilized collagens. As tested for collagen type I, this binding can be inhibited more effectively by chondroitin sulfate than by heparin. After electrophoretic separation and transfer to nitrocellulose, fibroblast-derived J1 only binds to a limited number of collagen types (collagen types I, VI, and IX and G), whereas brain-derived J1 glycoproteins bind to all collagen types tested (collagen types I-VI and IX and G). These results show that fibroblast-derived J1 glycoproteins, although immunochemically related to J1 glycoproteins from brain, differ from these in their binding specificities to extracellular matrix constituents.

Animals↗
PubMed1999

Composition of the extracellular matrix in human cricoarytenoid joint articular cartilage.

The extracellular matrix of the human cricoarytenoid joint articular cartilage is involved in different pathological changes. Interestingly, in contrast to the limb joints, the extracellular matrix composition of the healthy cricoarytenoid joint articular cartilage has not yet been elucidated except by some light microscopical investigations. The present study investigates the extracellular matrix components of the cricoarytenoid joint articular cartilage by means of light microscopy, immunohistochemistry, transmission electron microscopy and scanning electron microscopy and compares them with the limb joints for a better understanding of their involvement in joint disease. Chondrocytes near the joint surface of the cricoid and arytenoid cartilage differ from chondrocytes of deeper cartilage layers. The extracellular matrix of the articular cartilage contains chondroitin-4-sulfate, chondroitin-6-sulfate and keratansulfate as well as collagen types II, III, VI, IX and XI. Type-III-collagen shows a special distribution throughout the joint cartilage. In deeper cartilage layers, type-III-collagen occurs only pericellularly; in higher cartilage layers type-III-collagen is also located territorially and interterritorialy in small amounts. Scanning and transmission electron microscopy have revealed the articular surface of the cricoid and arytenoid cartilage to consist of a network of irregularly organized collagen fibrils, which are lined by a layer of electron dense material. The network coats subjacent collagen bundles which descend obliquely downward and intermingle at right angles in the middle part of the articular cartilage with collagen bundles of the deeper cartilage zones. The articular cartilage surface shows structural characteristics which differ from the underlying cartilage. The superficial electron dense layer possibly plays a role in the lubrication of the articular cartilage surface. The alignment of the fibrillar structures in the articular cartilage of the cricoarytenoid joint varies from those of the limb joints based on the different strain occurring during arytenoid movement. Nevertheless, the human cricoarytenoid joint articular cartilage can be compared with the joints of the limbs despite its extracellular matrix composition and its involvement in joint pathology. Evidence of type III collagen in the outermost layer of the articular cartilage of the cricoarytenoid joint presents a peculiarity, which has yet not be demonstrated in the articular cartilage of limb joints.

Adult↗
PubMed2004

Expression of collagen type I and type II in consecutive stages of human osteoarthritis.

In normal hyaline cartilage the predominant collagen type is collagen type II along with its associated collagens, for example, types IX and XI, produced by normal chondrocytes. In contrast, investigations have demonstrated that in vitro a switch from collagen type II to collagen type I occurs. Some authors have detected collagen type I in osteoarthritic cartilage also in vivo, especially in late stages of osteoarthritis, while others have not. In the light of these diverging results, we have attempted to elucidate which type of collagen, type I and/or type II, is synthesized in the consecutive stages of human osteoarthritis. We performed in situ hybridization and immunohistochemistry with cartilage tissue samples from patients suffering from various stages of osteoarthritis. Furthermore, we quantitated our results on the gene expression of collagen type I and type II with the help of real-time PCR. We found that with the progression of the disease not only collagen type II, but also increasing amounts of collagen type I mRNA were produced. This supports the conclusion that collagen type I gradually becomes one of the factors involved in the pathogenesis of osteoarthritis.

Aged↗
PubMed1989

Ascorbic acid induces alkaline phosphatase, type X collagen, and calcium deposition in cultured chick chondrocytes.

During the process of endochondral bone formation, proliferating chondrocytes give rise to hypertrophic chondrocytes, which then deposit a mineralized matrix to form calcified cartilage. Chondrocyte hypertrophy and matrix mineralization are associated with expression of type X collagen and the induction of high levels of the bone/liver/kidney isozyme of alkaline phosphatase. To determine what role vitamin C plays in these processes, chondrocytes derived from the cephalic portion of 14-day chick embryo sternae were grown in the absence or presence of exogenous ascorbic acid. Control untreated cells displayed low levels of type X collagen and alkaline phosphatase activity throughout the culture period. However, cells grown in the presence of ascorbic acid produced increasing levels of alkaline phosphatase activity and type X collagen mRNA and protein. Both alkaline phosphatase activity and type X collagen mRNA levels began to increase within 24 h of ascorbate treatment; by 9 days, the levels of both alkaline phosphatase activity and type X collagen mRNA were 15-20-fold higher than in non-ascorbate-treated cells. Ascorbate treatment also increased calcium deposition in the cell layer and decreased the levels of types II and IX collagen mRNAs; these effects lagged significantly behind the elevation of alkaline phosphatase and type X collagen. Addition of beta-glycerophosphate to the medium increased calcium deposition in the presence of ascorbate but had no effect on levels of collagen mRNAs or alkaline phosphatase. The results suggest that vitamin C may play an important role in endochondral bone formation by modulating gene expression in hypertrophic chondrocytes.

Alkaline Phosphatase↗
PubMed2002

Human articular chondrocytes immortalized by HPV-16 E6 and E7 genes: Maintenance of differentiated phenotype under defined culture conditions.

OBJECTIVE: To establish an immortalized normal human articular chondrocyte line which could be useful for a better understanding of cell molecular mechanisms relevant for the development of new therapeutic approaches in rheumatic diseases. DESIGN: Chondrocytes from human adult articular healthy cartilage were transfected in primary culture with a plasmid containing two human papilloma virus type 16 (HPV-16) early function genes: E6 and E7, using the highly efficient cationic liposome-mediated (lipofection) procedure. The transfection was verified by reverse transcriptase-polymerase chain reaction analysis of E7 mRNA and by immunofluorence localization of the E7 protein in the cell cytoplasm. The established chondrocyte cell line was examined in monolayer and in two culture conditions that were described to re-induce differentiated characteristics: culturing in a serum-free defined medium supplemented with an insulin-containing serum substitute and seeding on a hyaluronan-based non-woven structured biomaterial. The expression of markers characteristic of cartilage was shown in the mRNA by reverse transcriptase-polymerase chain reaction. Immunohistological staining and Western blotting analysis were performed to evaluate type II collagen synthesis. Proteoglycans deposition was detected by Alcian Blue staining. A Field Emission In Lens Scanning Microscopy was used to look at the morphology of the immortalized cells at very high magnification. RESULTS: Normal human articular chondrocytes were efficiently transfected leading to the establishment of an immortalized cell line as confirmed by HPV-16 E7 mRNA and protein detection. These cells were able to re-express type II collagen both at mRNA and protein levels under the two defined cultured conditions we used, still maintaining type I collagen expression. Collagen IX mRNA was present only in early primary culture while collagen type X and aggrecan transcripts were always detected. Alcian Blue staining showed a proteoglycan-rich matrix production. The ultrastructural analysis of the immortalized cells revealed that their morphology strictly resembled that of normal chondrocytes. CONCLUSIONS: The cell line that we obtained may be a useful tool for increasing our knowledge of the genetic and biochemical events involved in the processes of cartilage growth and differentiation. Moreover, it appears to be a suitable model for pharmacological and toxicological studies related to rheumatic diseases relevant to humans.

Blotting, Western↗
PubMed2001

Presence of autoantibodies in the sera of Meniere's disease.

We examined the sera of patients with Meniere's disease for the presence of antibodies against 8 inner ear antigens by enzyme-linked immunosorbent assay (ELISA). One hundred eight patients with Meniere's disease and 28 control subjects were studied. The antibodies against chicken type II collagen, bovine type II collagen, the cyanogen bromide cleaved peptide 11 (CB11) of each, type IX and XI collagens, C-Raf, and tubulin were measured by ELISA. The sensitivity of each antigen was between 37% and 60% individually, and was 91% when all 8 inner ear antigens were combined. These results showed that 91% of Meniere's disease sera have antibody activities to 1 or more of these inner ear antigens. The results suggest that performing ELISA for these 8 inner ear antigens was useful as a diagnostic tool for Meniere's disease. Further study is required for elucidating the role of these antigens in the pathogenesis of Meniere's disease, which might eventually result in better therapy.

Autoantibodies↗