Immunohistochemical localization of collagenase inhibitor in bovine dental pulp, pulp cells in monolayer culture, and in some oral connective tissues

Kishi, Jun; Kawai, T.; Hayakawa, Taro

doi:10.1016/0003-9969(85)90059-7

Cited by 11 publications

(1 citation statement)

References 14 publications

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“…Animal studies show gelatinolytic activity in predentin (Betti and Katchburian, 1982;Smith and Smith, 1984) and unidentified collagenase in dentin organic matrix (Fukae et al, 1991). A collagenase and a collagenase inhibitor are present in bovine pulp (Kishi and Hayakawa, 1982;Kishi et al, 1985), and cloned rabbit odontoblast-like cells produce latent collagenase (Sakamoto et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

The Expression of MMP-8 in Human Odontoblasts and Dental Pulp Cells is Down-regulated by TGF-β1

et al. 2000

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Recent findings show that matrix metalloproteinase-8 (MMP-8) is expressed, in addition to neutrophils, by human chondrocytes, cultured fibroblasts, and endothelial cells. We investigated the expression of MMP-8 in other human mesenchyme-derived cells, odontoblasts, and pulp tissue. Odontoblasts and pulp tissue were collected from extracted human teeth for MMP-8 mRNA analysis with reverse-transcription/polymerase chain-reaction (RT-PCR) and Southern blot. The expression, localization, and secretion of MMP-8 protein were studied with Western blot, immunohistochemistry, and immunofluorometric assay. The effect of TGF-beta1 (10 ng/mL) on the expression, secretion, and concentration of secreted MMP-8 was studied by odontoblast and pulp tissue culture methods (Tjäderhane et al., 1998a). RT-PCR demonstrated MMP-8 mRNA expression in native and cultured odontoblasts and pulp tissue and cultured pulp fibroblasts, with a 522-bp transcript comparable with that of bone marrow cells. The specificity of PCR was confirmed with Southern blot. Western blot with MMP-8-specific antibody detected 65- and 50-kDa proteins in native samples, representing latent and active forms of mesenchymal-type MMP-8, and in the conditioned odontoblast culture media, 50-kDa protein was observed. TGF-beta down-regulated the MMP-8 mRNA and concentration of secreted protein in both cultures. Immunohistochemical staining detected MMP-8 in odontoblasts. These findings indicate that mesenchyme-derived cells of the dentin-pulp complex express, synthesize, and activate MMP-8, which may, in concert with odontoblast-derived gelatinases, participate in organization of dentin organic matrix prior to mineralization.

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Section: Introductionmentioning

confidence: 99%

The Expression of MMP-8 in Human Odontoblasts and Dental Pulp Cells is Down-regulated by TGF-β1

et al. 2000

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Acid phosphatase activity and intracellular collagen degradation by fibroblasts in vitro

Yajima

1986

Cell Tissue Res.

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Human gingival fibroblasts were cultured with collagen fibrils. The precise process of collagen phagocytosis and the relationship between acid phosphatase activity and intracellular degradation of collagen were investigated by cytochemical methods at the ultrastructural level. The collagen fibrils were first engulfed at one end by cellular processes, or the cell membrane wrapped itself around the middle of the fibrils. Collagen phagocytosis induced acid phosphatase activity in the fibroblast Golgi-endoplasmic reticulum-lysosome system. By application of the tracer lanthanum, deposits were observed in the intercellular spaces and along the fibrils being phagocytosed. At this stage, primary lysosomes were seen in close proximity to the collagen being engulfed, but no signs of fusion were observed. When the fibrils had been interiorized in whole or in part, they ultimately became enclosed within phagosomes, and no tracer was observed along the interiorized portion of the fibrils. Primary lysosomes then fused with these collagen-containing phagosomes to form phagolysosomes. Collagen degradation occurred within these bodies even though the end of a fibril might have protruded outside of the cell. These results suggest that selective and controlled phagocytosis of collagen and intracellular digestion of it may play a central role in the physiological remodeling and metabolic breakdown of the collagen of connective tissues.

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Immunohistochemical demonstration of collagenase and tissue inhibitor of metalloproteinases (TIMP) in synovial lining cells of rheumatoid synovium

Okada

Gonoji

Nakanishi

et al. 1990

Virchows Archiv B Cell Pathol

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Immunohistochemical localization of collagenase inhibitor in bovine dental pulp, pulp cells in monolayer culture, and in some oral connective tissues

Cited by 11 publications

References 14 publications

The Expression of MMP-8 in Human Odontoblasts and Dental Pulp Cells is Down-regulated by TGF-β1

The Expression of MMP-8 in Human Odontoblasts and Dental Pulp Cells is Down-regulated by TGF-β1

Acid phosphatase activity and intracellular collagen degradation by fibroblasts in vitro

Immunohistochemical demonstration of collagenase and tissue inhibitor of metalloproteinases (TIMP) in synovial lining cells of rheumatoid synovium

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