Immunohistochemical and biochemical assay of versican in human sound predentine/dentine matrix

Ruggeri, Alessandra; Orsini, Giovanna; Mazzoni, Annalisa; Nato, Fernando; Papa, Verónica; Piccirilli, Marcello; Putignano, Angelo; Mazzotti, Giovanni; Dorigo, E; Breschi, Lorenzo

doi:10.4081/ejh.2009.125

Cited by 12 publications

(10 citation statements)

References 41 publications

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“…PGs play a crucial role in dentin mineralization [11, 12] and the structural integrity of collagen fibrils [13]. They are classified into two distinct categories: the large aggregating chondroitin/keratan sulfate family, composed of molecules such as versican and aggregan, and the family of small leucine-rich proteoglycans (SLRPs) [14–16].…”

Section: Extracellular Matrix Components Relevant To Dentin Biomodmentioning

confidence: 99%

Dentin biomodification: strategies, renewable resources and clinical applications

et al. 2014

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Objectives The biomodification of dentin is a biomimetic approach, mediated by bioactive agents, to enhance and reinforce the dentin by locally altering the biochemistry and biomechanical properties. This review provides an overview of key dentin matrix components, targeting effects of biomodification strategies, the chemistry of renewable natural sources, and current research on their potential clinical applications. Methods The PubMed database and collected literature were used as a resource for peer-reviewed articles to highlight the topics of dentin hierarchical structure, biomodification agents, and laboratorial investigations of their clinical applications. In addition, new data is presented on laboratorial methods for the standardization of proanthocyanidin-rich preparations as a renewable source of plant-derived biomodification agents. Results Biomodification agents can be categorized as physical methods and chemical agents. Synthetic and naturally occurring chemical strategies present distinctive mechanism of interaction with the tissue. Initially thought to be driven only by inter- or intra-molecular collagen induced non-enzymatic collagen cross-linking, multiple interactions with other dentin components are fundamental for the long-term biomechanics and biostability of the tissue. Oligomeric proanthocyanidins show promising bioactivity, and their chemical complexity requires systematic evaluation of the active compounds to produce a fully standardized intervention material from renewable resource, prior to their detailed clinical evaluation. Significance Understanding the hierarchical structure of dentin and the targeting effect of the bioactive compounds will establish their use in both dentin-biomaterials interface and caries management.

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Section: Extracellular Matrix Components Relevant To Dentin Biomodmentioning

confidence: 99%

Dentin biomodification: strategies, renewable resources and clinical applications

et al. 2014

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“…Labeling of versican was revealed as green reflective spots using light microscopy (a) or white spherical spots under FEI ‐ SEM (b). Labeling was obtained in accordance with R uggeri et al., 2009 .…”

Section: Dentin Proteoglycansmentioning

confidence: 99%

A review of the nature, role, and function of dentin non‐collagenous proteins. Part 1: proteoglycans and glycoproteins

Orsini¹,

Ruggeri²,

Mazzoni³

et al. 2009

Endodontic Topics

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Dentin is a collagen‐based mineralized tissue consisting of inorganic apatite crystallites embedded in an extracellular matrix. In addition to type I collagen, the dentin organic matrix contains several proteins and proteoglycans, collectively referred to as non‐collagenous proteins, that play fundamental roles in actively promoting, controlling, and regulating fibrillogenesis, crystal growth, and mineralization during dentinogenesis. Similarly to collagen fibrils, non‐collagenous proteins are synthesized and secreted by odontoblasts and some of them are detectable in both predentin and mineralized dentin while others are only within the dentin layer. Non‐collagenous components include proteoglycans (such as decorin, biglycan, fibromodulin, lumican, osteoadherin, and versican) and several glycoproteins such as osteocalcin, osteonectin, and the SIBLING proteins (i.e. osteopontin, bone sialoprotein, dentin matrix protein‐1, dentin sialophosphoprotein, and matrix extracellular phosphoglycoprotein). The first part of this review offers an overview of the nature of the above‐mentioned non‐collagenous proteins of the dentin organic matrix and their postulated functions, since a better understanding of the biological dynamics of the extracellular macromolecules is fundamental to clarifying the properties and function of the human mature sound dentin.

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“…Sections were then processed for immunohistochemical analysis. 29 Briefly, sections were rinsed for 5 min in distilled water, pre-treated with 0.5 M ethylenediaminetetraacetic acid (EDTA) for 30 min at RT, rinsed for 10 min in distilled water, rinsed in 1X phosphate buffered saline (PBS, GIBCO, Life Technologies, Carlsbad, CA, USA; pH 7.6) twice for 10 min at RT, incubated for 10 min in the peroxidase blocking solution included in the horseradish peroxidase (HRP)-based detection system selected for secondary labeling (UltraVision Quanto Detection System HRP DAB, Thermo Fisher Scientific, Fremont, CA, USA). Specimens were then rinsed in PBS three times for 10 min at RT, pre-incubated with normal goat serum (NGS) in PBS for 30 min at RT, then incubated overnight at 4°C either with a mouse monoclonal antibody anti-DMP1 at 1:50 (Santa Cruz Biotechnology, Santa Cruz, CA, USA) or with a rabbit polyclonal antibody anti-DSPP (Sigma Aldrich, St. Louis, MO, USA).…”

Section: Methodsmentioning

confidence: 99%

“…29,30,31 In brief, specimens were longitudinally cut using a low speed diamond saw (Sawing and Grinding System, Remet) under continuous water-cooling to obtain 1 mm-thick dentin sections. Samples were then polished by increasing grid SiC paper under constant deionized water irrigation and ultrasonically cleaned in 0.05 M Tris HCl (Trizma Hydrocloride, Sigma Aldrich) buffer solution (TBS) at pH 7.6.…”

Section: Methodsmentioning

confidence: 99%

Dentin matrix protein 1 and dentin sialophosphoprotein in human sound and carious teeth: an immunohistochemical and colorimetric assay

Martini

Trirè²,

Breschi

et al. 2013

Eur J Histochem

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Dentin matrix protein 1 (DMP1) and dentin sialophosphoprotein (DSPP) are extracellular matrix proteins produced by odontoblasts involved in the dentin mineralization. The aim this study was to compare the distribution of DMP1 and DSPP in human sound dentin vs human sclerotic dentin. Sixteen sound and sixteen carious human molars were selected, fixed in paraformaldehyde and processed for immunohistochemical detection of DMP1 and DSPP by means of light microscopy, transmission electron microscopy (TEM) and high-resolution field emission in-lens scanning electron microscopy (FEI-SEM). Specimens were submitted to a pre-embedding or a post-embedding immunolabeling technique using primary antibodies anti DMP1 and anti-DSPP and gold-conjugated secondary antibodies. Other samples were processed for the detection of DMP1 and DSPP levels. Dentin from these samples was mechanically fractured to powder, then a protein extraction and a protein level detection assay were performed. DMP1 and DSPP were more abundant in carious than in sound samples. Immunohistochemical analyses in sclerotic dentin disclosed a high expression of DMP1 and DSPP inside the tubules, suggesting an active biomineralization of dentin by odontoblasts. Furthermore, the detection of small amounts of these proteins inside the tubules far from the carious lesion, as shown in the present study, is consistent with the hypothesis of a preventive defense of all dentin after a noxious stimulus has undermined the tooth.

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Immunohistochemical and biochemical assay of versican in human sound predentine/dentine matrix

Cited by 12 publications

References 41 publications

Dentin biomodification: strategies, renewable resources and clinical applications

Dentin biomodification: strategies, renewable resources and clinical applications

A review of the nature, role, and function of dentin non‐collagenous proteins. Part 1: proteoglycans and glycoproteins

Dentin matrix protein 1 and dentin sialophosphoprotein in human sound and carious teeth: an immunohistochemical and colorimetric assay

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