Immunoelectron Microscopic Localization of Collagenase Inhibitor in Bovine Dentin

Hoshino, Takao; Kishi, Jun-Ichi; Kawai, T.; Kobayashi, Kunihiko; Hayakawa, Taro

doi:10.1016/s0174-173x(86)80001-2

Cited by 16 publications

(7 citation statements)

References 18 publications

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“…The TIMPs may also regulate the growth of several different cell types (52). TIMPs synthesized by human mature odontoblasts and pulp tissue could be secreted into a border of predentin, as previously shown with TIMP-1 by Ishiguro et al (35) and Hoshino et al (57). They may be involved in the regulation of dentin mineralization by controlling MMP activities.…”

Section: Discussionmentioning

confidence: 77%

See 1 more Smart Citation

Expression profile of matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in mature human odontoblasts and pulp tissue

Palosaari

Pennington

Larmas

et al. 2003

European J Oral Sciences

161

132

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Previous studies have demonstrated that (at least) matrix metalloproteinase (MMP)-2, -8, -9, -14 and -20 are expressed by human odontoblasts. Here, we analysed the expression of 19 MMPs and their specific tissue inhibitors (TIMP)-1, -2 and -3) -1, -2 and -3 in mature human odontoblasts and pulp tissue. Since MMP-20 is almost exclusively expressed by the dentin-pulp complex cells, we further analysed the effect of transforming growth factor (TGF)-beta1 and bone morphogenetic protein (BMPs)-2 on its expression. Matrix metalloproteinase-9 served as a positive control for growth factor responsiveness. It was found that MMP-1, -2, -9, -10, -11, -13, -14, -15, -16, -17, -19, -20 and -23, in addition to TIMP-1, -2 and -3 were expressed by both odontoblasts and pulp tissue. Neither MMP-3 nor MMP-12 were expressed in odontoblasts or pulp tissue, and MMP-7, -8, -24 and -25 were expressed only in the odontoblasts; MMP-2, -10, -11, -14 and -20 were expressed more abundantly by odontoblasts, whereas pulp tissue expressed more MMP-13 and MMP-17. Transforming growth factor-beta1 (1 ng ml(-1)) and BMP-2 (100 ng ml(-1)) did not markedly affect MMP-20 mRNA expression. In contrast, TGF-beta1 alone and with BMP-2 significantly upregulated MMP-9 mRNA by 2.4-fold and by 2.6-fold, respectively, in odontoblasts, while in pulp tissue no effects could be detected. The wide-scale expression of MMPs and TIMPs by mature human odontoblasts and pulp tissue suggests that they may participate in dentin matrix organization prior to mineralization, and that growth factors may further control dentin matrix modeling by differentially regulating individual MMPs.

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Section: Discussionmentioning

confidence: 77%

“…(35) and H oshino et al . (57). They may be involved in the regulation of dentin mineralization by controlling MMP activities.…”

Section: Discussionmentioning

confidence: 99%

Expression profile of matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in mature human odontoblasts and pulp tissue

Palosaari

Pennington

Larmas

et al. 2003

European J Oral Sciences

161

132

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“…Hoshino et al [1986] demonstrated the presence of TIMP-1 on peritubular collagen fibrils in bovine dentine. Ishiguro et al [1994] identified TIMP-1 in cementum and root dentine of human teeth.…”

Section: Discussionmentioning

confidence: 88%

Host-Derived Proteinases and Degradation of Dentine Collagen in situ

Strijp¹,

Jansen

DeGroot³

et al. 2003

Caries Res

150

123

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Dentine root caries is a process of demineralization and degradation of the organic matrix by proteinases. In this in situ study, the presence and activity of the matrix metalloproteinases 1, 2 and 9 (MMP-1, MMP-2, MMP-9) in saliva and in completely demineralized dentine specimens were investigated. Furthermore, the activity of cathepsin B was determined in saliva. A correlation between these enzymes and the level of degraded collagen was investigated. Demineralized dentine specimens were mounted in the partial prosthesis of 17 volunteers. Saliva samples were taken at 0, 2 and 4 weeks. After 4 weeks, the enzymes were extracted from the dentine specimens and the collagen loss was assessed. The collagen loss varied between 0 and 40.3%. Zymography of the saliva and the dentine extract samples showed that (pro-)MMP-2 and (pro-)MMP-9 were present. The levels of active MMPs were assessed, using fluorogenic MMP-specific substrates. All but 3 of the 51 saliva samples showed MMP-1 activity ranging from 1.5 to 101.1 relative fluorescence units (RFU)/s. Forty-eight saliva samples showed gelatinolytic MMP-2/MMP-9 activity (1.7–141.1 RFU/s). MMP-1 activity was shown in all dentine extracts varying between 3.5 and 295.0 RFU/s. From the dentine extracts, 15 showed MMP-2/MMP-9 activity (0.2–13.7 RFU/s). The MMP activity from both saliva and dentine extracts did not correlate with the collagen loss. The activity of salivary cathepsin B varied from 4.8 to 42.2 arbitrary units/min. A positive correlation was found between salivary MMP activity and cathepsin B activity. This study revealed that gelatinolytic enzyme activity was present both in saliva and dentine collagen. No correlation could be observed, however, between the level of enzyme activity and the collagen loss of the dentine specimens.

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“…Even though MMP-13 expression in mature human odontoblasts and especially in pulp tissue is strong (71), attempts to detect it in mineralized dentin have not been successful (65). TIMP-1, -2, and -3 are expressed in odontoblasts and in pulp tissue (58) and TIMP-1 is also found in predentin and dentin (54,72,73).…”

Section: Mmps In Mineralized Dentinmentioning

confidence: 99%

A review of the nature, role, and function of dentin non‐collagenous proteins. Part II: enzymes, serum proteins, and growth factors

Mazzoni¹,

Breschi²,

Carrilho³

et al. 2009

Endodontic Topics

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Part I was an overview of the role and function of proteoglycans and glycoproteins in the pulpo–dentin complex; part II will focus on enzymes, serum proteins, and growth factors. This review will discuss current knowledge regarding matrix metalloproteinases (MMPs), cathepsins, serum proteins, and growth factors in dentin and the related dentin–pulp complex in an attempt to better understand their nature, role, and function in the dentin extracellular matrix (ECM) environment. Dentin formation in physiological and pathological conditions has been widely studied. However, the regulation and involvement of non‐collageneous enzymes, serum proteins, and growth factors are still not completely elucidated. MMPs, a family of 23 endopeptidases in humans, are collectively capable of degrading virtually all ECM components, and their specific tissue inhibitors (TIMPs: tissue inhibitors of matrix metalloproteinases) participate in organo‐ and morphogenesis, physiological tissue turnover, and pathological tissue destruction. Similarly, the lysosomal cysteine proteinases (cathepsins) are capable of degrading ECM proteins such as collagen, laminin, fibronectin, and proteoglycans. These enzymes are implicated in a variety of pathological conditions, especially in diseases involving tissue re‐modeling states. Dentin also contains serum‐derived proteins (such as albumin, immunoglobulins, and transferrin), and a variety of growth factors in the mineralized ECM are available for release during demineralization or other injury. A detailed description of the components of the above‐mentioned dentin non‐collageneous proteins will be summarized in this literature review.

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Immunoelectron Microscopic Localization of Collagenase Inhibitor in Bovine Dentin

Cited by 16 publications

References 18 publications

Expression profile of matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in mature human odontoblasts and pulp tissue

Expression profile of matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in mature human odontoblasts and pulp tissue

Host-Derived Proteinases and Degradation of Dentine Collagen in situ

A review of the nature, role, and function of dentin non‐collagenous proteins. Part II: enzymes, serum proteins, and growth factors

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