Distribution of non‐collagenous dentin matrix proteins and proteoglycans, and their relation to calcium accumulation in bisphosphonate‐affected rat incisors

Ohma, Noriko; Takagi, Yasuaki; Takano, Yoshiro

doi:10.1034/j.1600-0722.2000.108003222.x

Cited by 15 publications

(9 citation statements)

References 16 publications

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“…In total, these dentin changes suggest a role for OPN in regulating the pace of dentinogenesis and influencing the extent of tissue mineralization. This is consistent with previous studies that supported a role for ECM phosphoproteins in directing circumpulpal dentin mineralization [67–69], or demonstrated OPN interaction with matrix vesicles in mantle dentin [6,27]. Moreover, these observations of OPN effects on dentin are supportive of findings pointing to increased OPN deposition in pathologies of dentin hypomineralization, e.g.…”

Section: Discussionsupporting

confidence: 92%

Osteopontin regulates dentin and alveolar bone development and mineralization

Foster

Salmon

et al. 2018

Bone

112

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The periodontal complex is essential for tooth attachment and function and includes the mineralized tissues, cementum and alveolar bone, separated by the unmineralized periodontal ligament (PDL). To gain insights into factors regulating cementum-PDL and bone-PDL borders and protecting against ectopic calcification within the PDL, we employed a proteomic approach to analyze PDL tissue from progressive ankylosis knock-out (Ank) mice, featuring reduced PP, rapid cementogenesis, and excessive acellular cementum. Using this approach, we identified the matrix protein osteopontin (Spp1/OPN) as an elevated factor of interest in Ank mouse molar PDL. We studied the role of OPN in dental and periodontal development and function. During tooth development in wild-type (WT) mice, Spp1 mRNA was transiently expressed by cementoblasts and strongly by alveolar bone osteoblasts. Developmental analysis from 14 to 240days postnatal (dpn) indicated normal histological structures in Spp1 comparable to WT control mice. Microcomputed tomography (micro-CT) analysis at 30 and 90dpn revealed significantly increased volumes and tissue mineral densities of Spp1 mouse dentin and alveolar bone, while pulp and PDL volumes were decreased and tissue densities were increased. However, acellular cementum growth was unaltered in Spp1 mice. Quantitative PCR of periodontal-derived mRNA failed to identify potential local compensators influencing cementum in Spp1 vs. WT mice at 26dpn. We genetically deleted Spp1 on the Ank mouse background to determine whether increased Spp1/OPN was regulating periodontal tissues when the PDL space is challenged by hypercementosis in Ank mice. Ank; Spp1 double deficient mice did not exhibit greater hypercementosis than that in Ank mice. Based on these data, we conclude that OPN has a non-redundant role regulating formation and mineralization of dentin and bone, influences tissue properties of PDL and pulp, but does not control acellular cementum apposition. These findings may inform therapies targeted at controlling soft tissue calcification.

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Section: Discussionsupporting

confidence: 92%

Osteopontin regulates dentin and alveolar bone development and mineralization

Foster

Salmon

et al. 2018

Bone

112

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“…Similar findings have been obtained in rat incisors (Ohma et al 2002) and molars (Sasano et al 2001;Hosoya et al 2003). Tadatomo et al (2002) and Matias et al (2003b) have also presented micrographs in which dentin is almost completely immuno-negative for BSP in rat molars.…”

Section: Discussionsupporting

confidence: 83%

“…Following an examination of previous light-microscopic studies, we have found that studies supporting our findings involve the use of buffered-paraformaldehyde for fixation and EDTA for demineralization (Sasano et al 2001;Ohma et al 2002;Tadatomo et al 2002;Hosoya et al 2003), whereas most other studies employ other chemicals: 95% ethanol (Somerman et al 1990b), Bouin's fixative (MacNeil et al 1994(MacNeil et al , 1995b, and 10% formalin (Ivanovski et al 2001) for fixation; acetic acid (MacNeil et al 1994(MacNeil et al , 1995b and 0.2N HCl (Chen et al 1993;Lekic et al 1996aLekic et al , 1996b for demineralization. Bufferedparaformaldehyde and EDTA are generally recommended for the immunohistochemistry of mineralized tissue, because different chemicals often cause unstable and misleading immunoreactions.…”

Section: Discussionsupporting

confidence: 55%

Immunolocalization of proteoglycans and bone-related noncollagenous glycoproteins in developing acellular cementum of rat molars

et al. 2004

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To elucidate the roles of proteoglycans of (PGs), bone sialoprotein (BSP), and osteopontin (OPN) in cementogenesis, their distribution was investigated in developing and established acellular cementum of rat molars by an immunoperoxidase method. To characterize PGs, antibodies against five species of glycosaminoglycans (GAGS), chondroitin-4-sulfate (C4S), chondroitin-6-sulfate (C6S), unsulfated chondroitin (C0S), dermatan sulfate (DS), and keratan sulfate (KS) were used. Routine histological staining was also applied. With onset of dentin mineralization, the initial cementum appeared on the dentin surface as a hematoxylin-stained fibril-poor layer. Subsequently, primitive principal fibers attached to the initial cementum. As the acellular cementum containing extrinsic fibers covered the initial cementum, the intal cementum formed the cemento-dentinal junction. Following immunohistochemistry at the earliest time of cementogenesis, the initial cementum was intensely immunoreactive for C4S, C6S, C0S, BSP, and OPN. After the initial cementum was embedded, neither the cemento-dentinal junction nor the cementum was immunoreactive for any GAG species. However, the cementum was immunoreactive for any GAG species. However, the cementum and cemento-dentinal were consistently immunoreactive for BSP. Although the cemento-dentinal junction was consistently immunoreactive for OPN, the remaining cementum showed no significant immunoreactivity. Thus, initial acellular cementogenesis requires a dense accumulation of PGs, BSP, and OPN, which may be associated with the mineralization process independently of collagen fibrils and initial principal fiber attachment.

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“…Notably, circumpulpal dentin formation has been described as depending on other ECM proteins, including related SIBLING family members DMP1, DSP, and DPP (Bleicher et al, 1999; Gibson et al, 2013c; Lu et al, 2007; Ohma et al, 2000; Sreenath et al, 2003; Steinfort et al, 1989; Steinfort et al, 1990; Ye et al, 2004). Like BSP, these multifunctional SIBLINGs can both directly and indirectly affect mineralization, and may also be involved in cell signaling and differentiation, and other local or systemic effects (Gericke et al, 2010; Gibson et al, 2013a; He et al, 2003; Hunter et al, 1996; Siyam et al, 2012; Tartaix et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Mineralization defects in cementum and craniofacial bone from loss of bone sialoprotein

Foster¹,

Ao²,

Willoughby³

et al. 2015

Bone

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Bone sialoprotein (BSP) is a multifunctional extracellular matrix protein found in mineralized tissues, including bone, cartilage, tooth root cementum (both acellular and cellular types), and dentin. In order to define the role BSP plays in the process of biomineralization of these tissues, we analyzed cementogenesis, dentinogenesis, and osteogenesis (intramembranous and endochondral) in craniofacial bone in Bsp null mice and wild-type (WT) controls over a developmental period (1-60 days post natal; dpn) by histology, immunohistochemistry, undecalcified histochemistry, microcomputed tomography (microCT), scanning electron microscopy (SEM), transmission electron microscopy (TEM), and quantitative PCR (qPCR). Regions of intramembranous ossification in the alveolus, mandible, and calvaria presented delayed mineralization and osteoid accumulation, assessed by von Kossa and Goldner's trichrome stains at 1 and 14 dpn. Moreover, Bsp−/− mice featured increased cranial suture size at the early time point, 1 dpn. Immunostaining and PCR demonstrated that osteoblast markers, osterix, alkaline phosphatase, and osteopontin were unchanged in Bsp null mandibles compared to WT. Bsp−/− mouse molars featured a lack of functional acellular cementum formation by histology, SEM, and TEM, and subsequent loss of Sharpey's collagen fiber insertion into the tooth root structure. Bsp−/− mouse alveolar and mandibular bone featured equivalent or fewer osteoclasts at early ages (1 and 14 dpn), however, increased RANKL immunostaining and mRNA, and significantly increased number of osteoclast-like cells (2-5 fold) were found at later ages (26 and 60 dpn), corresponding to periodontal breakdown and severe alveolar bone resorption observed following molar teeth entering occlusion. Dentin formation was unperturbed in Bsp−/− mouse molars, with no delay in mineralization, no alteration in dentin dimensions, and no differences in odontoblast markers analyzed. No defects were identified in endochondral ossification in the cranial base, and craniofacial morphology was unaffected in Bsp−/− mice. These analyses confirm a critical role for BSP in processes of cementogenesis and intramembranous ossification of craniofacial bone, whereas endochondral ossification in the cranial base was minimally affected and dentinogenesis was normal in Bsp−/− molar teeth. Dissimilar effects of loss of BSP on mineralization of dental and craniofacial tissues suggest local differences in the role of BSP and/or yet to be defined interactions with site-specific factors.

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Distribution of non‐collagenous dentin matrix proteins and proteoglycans, and their relation to calcium accumulation in bisphosphonate‐affected rat incisors

Cited by 15 publications

References 16 publications

Osteopontin regulates dentin and alveolar bone development and mineralization

Osteopontin regulates dentin and alveolar bone development and mineralization

Immunolocalization of proteoglycans and bone-related noncollagenous glycoproteins in developing acellular cementum of rat molars

Mineralization defects in cementum and craniofacial bone from loss of bone sialoprotein

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