Immunolocalization of the small proteoglycan decorin in human teeth

Yoshiba, Nagako; Yoshiba, Kunihiko; Iwaku, Masaaki; Ozawa, Hiroki

doi:10.1016/0003-9969(95)00138-7

Cited by 43 publications

(42 citation statements)

References 30 publications

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“…This resulted in the identification of C4S, C6S, KS, versican, and decorin in predentin, whereas in dentin only C4S and decorin epitopes' immunoreactivity was report-ed. This was confirmed by Yoshiba et al (1996), who also showed that decorin is present in dentin. Post-embedding immunogold electron microscopy allowed for the localization and quantification of GAGs and PGs in predentin and dentin.…”

Section: From Gags To Pgssupporting

confidence: 52%

“…In addition, both decorin and biglycan are capable of interacting with soluble growth factors, notably TGFj3, thereby modulating their functional activity (Iozzo and Murdoch, 1996), and also bind to cellsurface receptors influencing cell-cycle progression and the expression of gene products (lozzo, 1997). The role of decorin and biglycan in the mineralization process is not clear, but the GAG constituents of these PGs have a capacity to bind calcium and interact with hydroxyapatite and are present in pre-mineralized tissues such as osteoid (Robey, 1996) and predentin (Takagi et al, 1990;Yoshiba et al, 1996).…”

Section: (B) Small Leucine-rich Proteoglycansmentioning

confidence: 99%

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Proteoglycans in Dentinogenesis

Embery

Hall

Waddington

et al. 2001

Critical Reviews in Oral Biology & Medicine

169

158

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The predominant proteoglycans present in predentin and dentin are the chondroitin-sulphate-rich decorin and biglycan and the keratan-sulphate-rich lumican and fibromodulin. These are small, interstitial, leucine-rich proteoglycans which have recently been shown to exist in gradients across the predentin. Antibodies recognizing chondroitin sulphate show a decreasing gradient from the pulpal aspect toward the mineralizing front, the converse being true for keratan sulphate. Antidecorin shows an increase toward the mineralization front. Evidence from biochemical, autoradiographic, and immunohistochemical studies implies that such changes may be brought about by gradients of metalloproteinases. This offers the possibility that the proteoglycans organize the collagen network for receipt of phosphoproteins and phospholipids, the former being evident only at the onset of dentin formation. The suggestion is raised that glycosaminoglycan-depleted leucine-rich protein cores act as sequester points for receipt of phosphoproteins in particular. The rigid, spatially oriented glycosaminoglycan chains on decorin and biglycan are known to bind calcium and may feature directly in mineral initiation.Key words. Dentinogenesis, proteoglycans, phosphoconjugates, metalloproteinases, mineralization.(I) Introduction Jn recent years, there has been a wealth of new information on the group of non-collagenous glycoconjugates present in the extracellular matrix of most connective tissues, termed proteoglycans (PGs). These molecules are deemed to play structural and metabolic functional roles in both the soft and mineralized tissues of the body and are present in a wide variety of non-vertebrate and vertebrate species.Their presence in mineralized tissues, such as bone, has been evident for some time. Although the presence of PGs in predentin and, to a lesser extent, in dentin is well-established, it is only with the advent of contemporary biochemical and immunohistochemical procedures that their speciation, ultrastructural distribution, and possible biological roles in dentinogenesis are beginning to be elucidated.Within the last decade, there have been few reviews specifically addressing the function of PGs in relation to dentinogenesis. Research in this field has borrowed much of its knowledge from connective tissues in general, particularly the work on the aggregating PGs, such as aggrecan, present in cartilage. It The aspect of gradient distribution will be described in detail later and is of major significance, since it offers a functionality for such molecules during the structural transition of the extracellular matrix (ECM) of predentin, leading to the correct spatial assembly of the collagenous-non-coliagenous scaffold as a prelude for mineral deposition. For this reason, the review wili also deal with recent work on the potential of metalioproteinases (MMPs) to bring about such transition and the presence of phosphoprotein in dentin specifically hnked to mineralization. The absence of phosphoprotein from predentin an...

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Section: From Gags To Pgssupporting

confidence: 52%

Section: (B) Small Leucine-rich Proteoglycansmentioning

confidence: 99%

Proteoglycans in Dentinogenesis

Embery

Hall

Waddington

et al. 2001

Critical Reviews in Oral Biology & Medicine

169

158

View full text Add to dashboard Cite

show abstract

“…Proteoglycans belong to a family of glycoconjugates and contain one or more GAGs covalently attached to the protein core. The GAGs are known to bind calcium and interact with hydroxyapatite and are readily detectable by Alcian blue staining (23,28,36). Wider distribution of GAG staining observed in the predentin region of DsppϪ/Ϫ mice indicated the presence of proteoglycans.…”

Section: Discussionmentioning

confidence: 99%

Dentin Sialophosphoprotein Knockout Mouse Teeth Display Widened Predentin Zone and Develop Defective Dentin Mineralization Similar to Human Dentinogenesis Imperfecta Type III

Sreenath

Thyagarajan

Hall

et al. 2003

Journal of Biological Chemistry

370

348

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Dentin sialophosphoprotein (Dspp) is mainly expressed in teeth by the odontoblasts and preameloblasts. The Dspp mRNA is translated into a single protein, Dspp, and cleaved into two peptides, dentin sialoprotein and dentin phosphoprotein, that are localized within the dentin matrix. Recently, mutations in this gene were identified in human dentinogenesis imperfecta II (Online Mendelian Inheritance in Man (OMIM) accession number 125490) and in dentin dysplasia II (OMIM accession number 125420) syndromes. Herein, we report the generation of Dspp-null mice that develop tooth defects similar to human dentinogenesis imperfecta III with enlarged pulp chambers, increased width of predentin zone, hypomineralization, and pulp exposure. Electron microscopy revealed an irregular mineralization front and a lack of calcospherites coalescence in the dentin. Interestingly, the levels of biglycan and decorin, small leucine-rich proteoglycans, were increased in the widened predentin zone and in void spaces among the calcospherites in the dentin of null teeth. These enhanced levels correlate well with the defective regions in mineralization and further indicate that these molecules may adversely affect the dentin mineralization process by interfering with coalescence of calcospherites. Overall, our results identify a crucial role for Dspp in orchestrating the events essential during dentin mineralization, including potential regulation of proteoglycan levels.

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“…During development, decorin is deposited in collagen type I-rich extracellular matrices including the soft connective tissues, periosteum, and pericellular matrices of many odontogenic cell types (Bianco et al, 1990;Matsuki et al, 1995;Yoshiba et al, 1996;Zhang et al, 1995). Decorin is also expressed in adult dental and periodontal tissues including dentin, root cementum, alveolar bone (Cheng et al, 1999a;Robey, 1996), periodontal ligament, and gingiva (Häkkinen et al, 1993).…”

Section: Discussionmentioning

confidence: 99%