Immunofluorescence localization of type I and type III collagen and fibronectin in mouse dental tissues in late development and during molar eruption

Takita, Kaoruko; Ohsaki, Yasuyoshi; Nakata, M.; Kurisu, Kojiro

doi:10.1016/0003-9969(87)90021-5

Cited by 46 publications

(18 citation statements)

References 22 publications

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“…Although the function of the collagen remains to be established, the distribution of the molecule in the connective tissues suggests a role in linking the major-banded collagen fibre bundles while, at the same time perhaps, providing structural unity for the tissue. Our observations demonstrate a distinct heterogeneity in the distribution of collagen type VI in the periodontal ligament of the continuously erupting rat incisor and the erupting molar, which contrasts not only with the uniform staining of the ligament in the adjacent erupted molar, but also with the more homogeneous distribution of the stain for collagen type I observed here and elsewhere (Tung et al, 1985;Takita et al, 1987;Becker et al, 1991).…”

Section: Discussioncontrasting

confidence: 46%

An immunohistochemical study examining the role of collagen type VI in the rodent periodontal ligament

Sloan

Carter

Cm³

et al. 1993

Histochem J

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The distribution of collagen types I and VI has been examined in the periodontal ligaments of rat incisor and molar teeth using cryosections and immunohistochemical staining procedures. The stain for collagen type I was uniform in all the ligaments examined. Uniform staining for collagen type VI was evident only in the ligament of the fully erupted molars, and the stain was absent from the mid-zone of the ligaments of the erupting molars and incisors. The staining pattern of the collagen type VI antibodies is consistent with previous reports which have suggested that the removal of collagen type VI precedes the degradation of major banded collagen fibrils in remodelling connective tissues. The removal of collagen type VI from the mid-zone of the incisor ligament may precede the remodelling events which facilitate tooth eruption.

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Section: Discussioncontrasting

confidence: 46%

An immunohistochemical study examining the role of collagen type VI in the rodent periodontal ligament

Sloan

Carter

Cm³

et al. 1993

Histochem J

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“…Antibody to calf skin type III procollagen was raised in guinea pigs (22,27). Deparaffinized sections were incubated in a 0.025% solution of protease type VII (Sigma, St. Louis, USA) in phosphate buffered saline, pH 7.3 (PBS) for 20 min at room temperature.…”

Section: Methodsmentioning

confidence: 99%

Heterotopic bone formation in tumor stromal tissue. Immunohistochemical considerations.

Kumasa

Mori

et al. 1990

Acta Histochem. Cytochem

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Ectopic and heterotopic bone formation rarely occur in stromal tissues of various epithelial tumors. In the present study, ectopic bone forming tumors; calcifying epithelioma Malherbe (6), renal cell carcinoma (1), thyroid adenocarcinoma (1) and ovary carcinoma (1) were examined. The process of ectopic bone formation could be classified into 1) bone formation related to epithelial tissue as found in calcifying epithelioma of Malherbe, 2) bone formation from perivascular smooth muscle, and 3) that due to metaplasia occurring in stromal connective tissue of epithelial tumors. Immunohistochemical detection of proteoglycans (PG) was made in bone-forming matrix areas, and these areas were positive for chondrotin 4 and 6 sulfate, and dermatan and heparan sulfate PGs. Immunohistochemically, fibronectin, collagen III and bone sialoprotein as matrix proteins, and carbonic anhydrase as calcification marker were tested and they appeared in these pre-calcifying tissues.

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“…Q p e I11 collagen is not a normal matrix component of mineralized dentin [Linde, 19891. Whether type I11 (pro)collagen is present in normal predentin (nonmineralized dentin matrix next to pulp tissue) is somewhat controversial [Cournil et al, 1979;Thesleff et al, 1979;Wright and Leblond, 1980;Becker et al, 1986;Takita et al, 1987;Andujar et al, 19881. In type I1 DD, type 111 collagen could not be demonstrated using specific antibodies to type I11 collagen and the N-terminal propeptide of type 111 procollagen [Ranta et al, 19901. At present, no information about the gene defect(s) in dentin dysplasias is available.…”

Section: Dentin Dysplasia Wpementioning

confidence: 98%

Heritable dentin defects: Nosology, pathology, and treatment

1993

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Heritable dentin defects have been divided into 2 main categories: dentinogenesis imperfecta (DI) and dentin dysplasia (DD). Recent studies have shown that they share many features in common. Of the connective tissue diseases, only osteogenesis imperfecta (OI) has been linked to these disorders. So far, no definitive relation between the type of OI and the dental involvement can be established. Familial occurrence of DI with OI cannot be comprehensively explained by mutations in type I collagen genes. No information about the gene defects in DD is available. At the ultrastructural level, the organization of the normally cross-striated collagen fibers in the dentin matrix varies markedly in patients affected by DI.

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Immunofluorescence localization of type I and type III collagen and fibronectin in mouse dental tissues in late development and during molar eruption

Cited by 46 publications

References 22 publications

An immunohistochemical study examining the role of collagen type VI in the rodent periodontal ligament

An immunohistochemical study examining the role of collagen type VI in the rodent periodontal ligament

Heterotopic bone formation in tumor stromal tissue. Immunohistochemical considerations.

Heritable dentin defects: Nosology, pathology, and treatment

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