Type II collagen distribution in rodents

Yoo, T.J.; Tomoda, Koichi

doi:10.1288/00005537-198811000-00019

Cited by 33 publications

(16 citation statements)

References 21 publications

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“…3H). These findings are quite coincident with those of the previous reports [30,33]. Moreover, the marginal region with the absence of the type II collagen immunolabeling in the IM joint cartilage matrices was complementally stained with the CS-56 antibody (Fig.…”

Section: Discussionsupporting

confidence: 92%

“…The SV joint, on the contrary, where the stapes footplate articulates the vestibular window through the annular ligament is quite different from the other ossicular joints, although both the vestibular surface and the rim of the stapes footplate are also covered with hyaline cartilage. So far, some reports are available on immunohistochemical investigations of the cartilage matrices, such as collagen type II [32,33] and chondroitin sulfate [29] immunostainings. In addition, Ye et al [29] suggested that chondroitin sulfate may play an important role in the development of otosclerotic lesions.…”

Section: Introductionmentioning

confidence: 99%

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Histochemical Characterization of the Rat Ossicular Joint Cartilage with a Special Reference to Stapediovestibular Joint

Ohashi

Sawaguchi

Ide

et al. 2005

Acta Histochem. Cytochem

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The stapes footplate articulates the vestibular window (stapediovestibular joint; SV joint). The SV joint is known as crucial region of otosclerosis. To shed a light on pathogenesis of otosclerosis, we have examined the histochemical characteristics of the rat ossicular joint cartilage. Interestingly, glycoconjugate histochemistry revealed that the cartilage matrix components of the SV joint were significantly different from those of the other ossicular joints, i.e. incudomalleolar (IM) and incudostapedial (IS) joints. Alcian blue, pH 2.5 and high-iron diamine procedures vividly stained the cartilage matrices of the IM and IS joints, while those of the SV joint were faintly stained. Chondroitin sulfate immunohistochemistry revealed intense labeling of the cartilage of the IM and IS joints, while the immunolabeling of the SV joint was negligible. On the contrary, keratan sulfate immunolabeling was discernible on the cartilage matrices of the SV joint, but not on those of the IM and IS joints. Type II collagen immunolabeling revealed that the marginal region of the IM and IS joint cartilage matrices was devoid of the immunostaining, while the SV joint cartilage matrices were uniformly labeled with this antibody. In this study, we have succeeded in demonstrating the histochemical characteristics of the rat SV joint cartilage matrices of which is quite different from those of the other ossicular joints.

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Section: Discussionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Histochemical Characterization of the Rat Ossicular Joint Cartilage with a Special Reference to Stapediovestibular Joint

Ohashi

Sawaguchi

Ide

et al. 2005

Acta Histochem. Cytochem

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“…Autoimmune response to the components of connec tive tissue, in particular CII, has long been recognized as important in arthritis, but it was also proposed as impor tant in human ear diseases [9], CII is known as the major component of cartilage but immunohistochemical studies of the ear tissue in rodents have revealed its distribution in the following regions: the enchondral layer and globuli interossei of the otic capsule, osseous spiral lamina, spiral ligament, limbus, tectorial membrane, endolymphatic duct, and other tissue structures [36][37][38][39][40]. Autoimmune response to CII with animal models was originally described as collagen-induced arthritis in rats and mice [21,39], It is known that the onset of arthritis is recognized by redness and swelling of the paws 4-6 weeks after immunization with CII.…”

Section: Discussionmentioning

confidence: 99%

Molecular Basis of Type II Collagen Autoimmune Disease: Observations of Arthritis, Auricular Chondritis and Tympanitis in Mice

Fujiyoshi

Cheng

Krug

et al. 1997

ORL

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A type II collagen autoimmune response results in arthritis, auricular chondritis and tympanosclerosis in humans and animals. The purpose of this study is to further define the molecular and pathogenic events involved in these lesions in rodents. Type II collagen fragment CB11-specific monoclonal antibodies induced lesions in joints, ear lobes and tympanic membranes. In immunized mice, the thickness of tympanic membranes increased to two- to fourfold normal size. Electron micrography showed that the arrangement of collagen fibers is irregular in both radial and auricular layers, containing fibroblasts, a homogeneous materal resembling low-density cholesterol crystals and cell infiltration. The mice with auricular chondritis had lymphocytes expressing Vβ-8 T cell receptor (TCR) in arthritic joints and lymphocytes expressing Vβ-6 TCR in ear lobe lesions. A monoclonal antibody specific to the TCR Vβ-8 subfamily suppressed the onset of arthritis. Sequence analyses of the Vβ structure of TCR involved in the lesions confirm the immunohistologic study.

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“…This report supports the hypothesis that these two proteins interact with each other. Several types of collagen have been detected in the ECM of the inner ear [Yoo et al, 1988;Slepecky et al, 1992;Usami et al, 2008]. Of these subtypes, type II collagen is responsible for the fibrous structure and appears to play a critical role in maintaining structural stability in the cochlea and vestibule [Slepecky et al, 1992].…”

Section: Discussionmentioning

confidence: 99%

Ultrastructural Localization of Cochlin in the Rat Cochlear Duct

et al. 2009

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Cochlin, a product of the COCH gene, is a major constituent of the inner ear extracellular matrix. Type II collagen, a protein that contributes to structural stability, is also a component of this extracellular matrix. In this study, using the postembedding immunogold method, we demonstrate the localization of cochlin and type II collagen in the cochlear duct at the ultrastructural level. The immunolabeling of cochlin was observed in the fibrillar substance in the spiral limbus, beneath the inner sulcus cells, and in the basilar membrane, the spiral prominence and the spiral ligament. Immunolabeling of type II collagen was observed in the same fibrillar substance in the extracellular matrix of the cochlear duct. This localization of cochlin is consistent with the expected localization of type II collagen. The localization of cochlin and type II collagen indicates the important roles played by these proteins in the hearing process.

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Type II collagen distribution in rodents

Cited by 33 publications

References 21 publications

Histochemical Characterization of the Rat Ossicular Joint Cartilage with a Special Reference to Stapediovestibular Joint

Histochemical Characterization of the Rat Ossicular Joint Cartilage with a Special Reference to Stapediovestibular Joint

Molecular Basis of Type II Collagen Autoimmune Disease: Observations of Arthritis, Auricular Chondritis and Tympanitis in Mice

Ultrastructural Localization of Cochlin in the Rat Cochlear Duct

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