Dentin sialoprotein

Last updated

Dentin sialoprotein is a protein found in teeth. It is one of the two proteins produced by the segmentation of dentin sialophosphoprotein. Dentin sialoprotein can be found in the dentin immediately subjacent to cellular cementum, but not subjacent to acellular fibrous cementum. [1]

Contents

What is it?

DSP is found in the teeth Teeth by David Shankbone.jpg
DSP is found in the teeth

DSP is one of the dominant proteins found in dentin. It is dominantly expressed in odontoblasts and the peptides derived from DSP regulate gene expression and phosphorylation, causing dental primary and stem cell differentiation. [2] It was first discovered in 1981 but even now there is controversy about its functional significance. Since dentin sialoprotein (DSP) shares a similar makeup to bone sialoprotein (BSP) that is how it received its name. It is reported as a weak inhibitor of mineralization in dentin but its role is still unclear. [3] DSP is a glycoprotein that accounts for part of the non-collageneous proteins in dentin. It is one of the acidic NCP's that is identified in the extracellular matrix and is most abundant alongside DPP. DSP is a proteolytically processed product of DSPP and contains 6.2 phosphates per molecule. The phosphate per molecule value is relatively lower than expected in the presence of DPP since there are a large amount of potential phosphorylation sites available. Since multiple experiments have been conducted, it has been found that in the vitro formation of hydroxyapatite and the growth of mineral crystals, DSP has little to no effect on mineralization. [4]

Function

Dentin sialoprotein (DSP) is an extracellular matrix protein found in dentin. It is an uncommon marker of dentinogenesis that is involved in the differentiation of odontoblast and dentin mineralization. Lately, it has been shown that DSP can lead to the start of the differentiation and mineralization of periodontal ligament stem cells as well as in dental papilla mesenchymal cells while in vitro. It is also involved in rescuing dentin deficiency and increasing enamel mineralization in animals. [5] DSP appears at the mineralization front along with Phosphophoryn but only accounts for 5-8% of the dentin NCPs weight. The precise role is currently unknown but in situ studies, it is demonstrated that DSP is expressed in odontoblasts and preameloblasts but there is no information to directly explain the role in mineralization. [6] DSP's are small fragments that are distributed into different compartments of the teeth and tend to increase the rate of enamel mineralization and lead to the differentiation of dental pulp cells. [2] DSP is also responsible for pulp cell migration and differentiation. It can act as a structural protein or can take a part in modulating the formation of hydroxyapatite. Experiments have shown that the DSP expressed in odontoblasts is involved in dentin mineralization. The expression of DSP in preameloblasts and odontoblasts indicate that it might be able to induce the migration of dental pulp cells, odontoblast differentiation, and possibly dentin formation. [7]

Structure

DSP is found to have Glu, Asp, Ser, and Gly. Through sedimentation equilibrium and amino acid analyses, it is estimated that DSP has a weight of 53 kDa and has approximately 350 amino acids. Through Edman Degradation, the NH2-terminal sequence is found to be IPVPNLPL. [8] DSP is the amino-terminal part of DSPP, which is cleaved into DSP. [9] The full length and COOH-terminal of DSP regulate bone and tooth gene expression and causes kinase phosphorylation, dentin mesenchymal differentiation and DSPP gene expression. [2] It is a sialic acid-rich glycosated protein that is a member of the small integrin-binding ligand N-linked glycoproteins (SIBLING) family, which also includes bone sialoprotein (BSP), dentin matrix protein-1 (DMP-1), osteopontin (OPN), and matrix extracellular phosphoglycoprotein (MEPE). [9] Members of the SIBLING family typically contain the tripeptide RGD within the genes that bind to integrins and activate signal transduction but DSP lacks any of the RGD domain. [2] The amino acid residues are important in the binding to the integrin β6. This promotes the cell attachment, migration, differentiation, and mineralization of dental mesenechymal cells. The domain of DSP regulates DSPP expression and homeostasis of odontoblasts through a positive feedback loop. When mutations occur in the DSP domain, it can cause dentinogenesis imperfecta as well as dentin dysplasia which are the most common disorders in dentin. [2] It is reported that Porcine and Bovine DSP are chondroitin sulfate-type proteoglycans. Furthermore, since DSP is produced by the cleavage of DSPP, the DSP homozygous negative phenotype doesn't provide much information on the roles of DSP or DPP in dentin mineralization. [9] Mutations that are heterogenous in the coding domain of DSP can cause DGI-II as well as dentin dysplasia II which indicates that DSP, the NH2-terminus protein of DSPP is essential to dentinogenesis. The cleavage of DSPP into DSP and DPP is an activation step of the function of DSPP and without making the cleavage, it will result in dentin and periodontal development defects. DSP NH2-terminal fragments have been found to be weakly distributed into the mineralized dentin but the DSP COOH-terminal fragments are mainly restricted to the mineralized dentin. [10]

Analysis

DSP is expressed as a single mRNA transcript that codes for DSPP. DSP is a NCP which is found in bone and dentin and is very acidic. The NCPs are secreted into the ECM during formation and mineralization of the tissues and are thought to play key roles in osteogenesis and dentinogenesis. DSP contains roughly 30% of carbohydrates and 9% sialic acid. In an experiment that was conducted, it was found that DSP was also found in the long bones of rats in small quantities. It is estimated that the amount of DSP in the bone was 1/400 of the amount found in dentin and that larger quantities of DSP are found in dentin. Through DEAE-Sephacel chromatography analysis, the peak of DSP in dentin appears before the peak of DSP in bone does, which is likely from post-translational modifications. [11] DSP is only synthesized by odontoblasts and pulp cells and seems to be transported through odontoblastic cell processes into the predentin-dentin junction. Since DSP is only synthesized by odontoblasts, it confirms that DSP represents a cell specific marker. Although DSP is found in bone as well as dentin, it is not found in the brain, salivary glands, lungs, intestines, muscles, or any other organs. [12]

Related Research Articles

<span class="mw-page-title-main">Osteoblast</span> Cells secreting extracellular matrix

Osteoblasts are cells with a single nucleus that synthesize bone. However, in the process of bone formation, osteoblasts function in groups of connected cells. Individual cells cannot make bone. A group of organized osteoblasts together with the bone made by a unit of cells is usually called the osteon.

<span class="mw-page-title-main">Dentin</span> Calcified tissue of the body; one of the four major components of teeth

Dentin or dentine is a calcified tissue of the body and, along with enamel, cementum, and pulp, is one of the four major components of teeth. It is usually covered by enamel on the crown and cementum on the root and surrounds the entire pulp. By volume, 45% of dentin consists of the mineral hydroxyapatite, 33% is organic material, and 22% is water. Yellow in appearance, it greatly affects the color of a tooth due to the translucency of enamel. Dentin, which is less mineralized and less brittle than enamel, is necessary for the support of enamel. Dentin rates approximately 3 on the Mohs scale of mineral hardness. There are two main characteristics which distinguish dentin from enamel: firstly, dentin forms throughout life; secondly, dentin is sensitive and can become hypersensitive to changes in temperature due to the sensory function of odontoblasts, especially when enamel recedes and dentin channels become exposed.

<span class="mw-page-title-main">Pulp (tooth)</span> Part in the center of a tooth made up of living connective tissue and cells called odontoblasts

The pulp is the connective tissue, nerves, blood vessels, and odontoblasts that comprise the innermost layer of a tooth. The pulp's activity and signalling processes regulate its behaviour.

<span class="mw-page-title-main">Ameloblast</span>

Ameloblasts are cells present only during tooth development that deposit tooth enamel, which is the hard outermost layer of the tooth forming the surface of the crown.

<span class="mw-page-title-main">Enamel organ</span> Aggregate of cells involved in tooth development

The enamel organ, also known as the dental organ, is a cellular aggregation seen in a developing tooth and it lies above the dental papilla. The enamel organ which is differentiated from the primitive oral epithelium lining the stomodeum. The enamel organ is responsible for the formation of enamel, initiation of dentine formation, establishment of the shape of a tooth's crown, and establishment of the dentoenamel junction.

<span class="mw-page-title-main">Human tooth development</span> Process by which teeth form

Tooth development or odontogenesis is the complex process by which teeth form from embryonic cells, grow, and erupt into the mouth. For human teeth to have a healthy oral environment, all parts of the tooth must develop during appropriate stages of fetal development. Primary (baby) teeth start to form between the sixth and eighth week of prenatal development, and permanent teeth begin to form in the twentieth week. If teeth do not start to develop at or near these times, they will not develop at all, resulting in hypodontia or anodontia.

Amelogenesis is the formation of enamel on teeth and begins when the crown is forming during the advanced bell stage of tooth development after dentinogenesis forms a first layer of dentin. Dentin must be present for enamel to be formed. Ameloblasts must also be present for dentinogenesis to continue.

<span class="mw-page-title-main">Dental papilla</span>

In embryology and prenatal development, the dental papilla is a condensation of ectomesenchymal cells called odontoblasts, seen in histologic sections of a developing tooth. It lies below a cellular aggregation known as the enamel organ. The dental papilla appears after 8–10 weeks of intra uteral life. The dental papilla gives rise to the dentin and pulp of a tooth.

<span class="mw-page-title-main">Odontoblast</span> Type of cell that produces dentin in teeth

In vertebrates, an odontoblast is a cell of neural crest origin that is part of the outer surface of the dental pulp, and whose biological function is dentinogenesis, which is the formation of dentin, the substance beneath the tooth enamel on the crown and the cementum on the root.

Dentinogenesis is the formation of dentin, a substance that forms the majority of teeth. Dentinogenesis is performed by odontoblasts, which are a special type of biological cell on the outer wall of dental pulps, and it begins at the late bell stage of a tooth development. The different stages of dentin formation after differentiation of the cell result in different types of dentin: mantle dentin, primary dentin, secondary dentin, and tertiary dentin.

<span class="mw-page-title-main">Dentinogenesis imperfecta</span> Genetic disorder impairing tooth development

Dentinogenesis imperfecta (DI) is a genetic disorder of tooth development. It is inherited in an autosomal dominant pattern, as a result of mutations on chromosome 4q21, in the dentine sialophosphoprotein gene (DSPP). It is one of the most frequently occurring autosomal dominant features in humans. Dentinogenesis imperfecta affects an estimated 1 in 6,000-8,000 people.

<span class="mw-page-title-main">Osteonectin</span> Mammalian protein found in Homo sapiens

Osteonectin (ON) also known as secreted protein acidic and rich in cysteine (SPARC) or basement-membrane protein 40 (BM-40) is a protein that in humans is encoded by the SPARC gene.

<span class="mw-page-title-main">Dentin dysplasia</span> Medical condition

Dentin dysplasia (DD) is a rare genetic developmental disorder affecting dentine production of the teeth, commonly exhibiting an autosomal dominant inheritance that causes malformation of the root. It affects both primary and permanent dentitions in approximately 1 in every 100,000 patients. It is characterized by the presence of normal enamel but atypical dentin with abnormal pulpal morphology. Witkop in 1972 classified DD into two types which are Type I (DD-1) is the radicular type, and type II (DD-2) is the coronal type. DD-1 has been further divided into 4 different subtypes (DD-1a,1b,1c,1d) based on the radiographic features.

<span class="mw-page-title-main">Bone sialoprotein</span> Protein-coding gene in the species Homo sapiens

Bone sialoprotein (BSP) is a component of mineralized tissues such as bone, dentin, cementum and calcified cartilage. BSP is a significant component of the bone extracellular matrix and has been suggested to constitute approximately 8% of all non-collagenous proteins found in bone and cementum. BSP, a SIBLING protein, was originally isolated from bovine cortical bone as a 23-kDa glycopeptide with high sialic acid content.

<span class="mw-page-title-main">DMP1</span> Protein-coding gene in the species Homo sapiens

Dentin matrix acidic phosphoprotein 1 is a protein that in humans is encoded by the DMP1 gene.

<span class="mw-page-title-main">FAM20C</span> Protein-coding gene in the species Homo sapiens

Family with sequence similarity 20, member C also known as FAM20C or DMP4 is a protein which in humans is encoded by the FAM20C gene. Fam20C, a Golgi localized protein kinase, is a serine kinase that phosphorylates both casein and other highly acidic proteins and members of the small integrin-binding ligand, the N-linked glycoproteins (SIBLING) family at the target motif SerXGlu.

Dentin sialophosphoprotein is a precursor protein for other proteins found in the teeth. It is produced by cells (odontoblasts) inside the teeth, and in smaller quantities by bone tissues. It is required for normal hardening (mineralisation) of teeth. During teeth development, it is broken down into three proteins such as dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP). These proteins become the major non-collagenous components of teeth. Their distribution in the collagen matrix of the forming dentin suggests these proteins play an important role in the regulation of mineral deposition. Additional evidence for this correlation is phenotypically manifested in patients with mutant forms of dentin sialophosphoprotein. Such patients suffer dental anomalies including type III dentinogenesis imperfecta.

The family of non-collagenous proteins known as SIBLING proteins, standing for small integrin-binding ligand, N-linked glycoprotein, are components of the extracellular matrix of bone and dentin. Evidence shows that these proteins play key roles in the mineralization of these tissues.

<span class="mw-page-title-main">Pulp stone</span>

Pulp stones are nodular, calcified masses appearing in either or both the coronal and root portion of the pulp organ in teeth. Pulp stones are not painful unless they impinge on nerves.

<span class="mw-page-title-main">Regenerative endodontics</span> Dental specialty

Regenerative endodontic procedures is defined as biologically based procedures designed to replace damaged structures such as dentin, root structures, and cells of the pulp-dentin complex. This new treatment modality aims to promote normal function of the pulp. It has become an alternative to heal apical periodontitis. Regenerative endodontics is the extension of root canal therapy. Conventional root canal therapy cleans and fills the pulp chamber with biologically inert material after destruction of the pulp due to dental caries, congenital deformity or trauma. Regenerative endodontics instead seeks to replace live tissue in the pulp chamber. The ultimate goal of regenerative endodontic procedures is to regenerate the tissues and the normal function of the dentin-pulp complex.

References

  1. ↑ Letty Moss-Salentijn, Biology of Mineralized Tissue coursenotes, Columbia University College of Dental Medicine, 2009
  2. 1 2 3 4 5 Wan C, Yuan G, Luo D, Zhang L, Lin H, Liu H, et al. (July 2016). "The Dentin Sialoprotein (DSP) Domain Regulates Dental Mesenchymal Cell Differentiation through a Novel Surface Receptor". Scientific Reports. 6 (1): 29666. Bibcode:2016NatSR...629666W. doi:10.1038/srep29666. PMC   4949421 . PMID   27430624.
  3. ↑ Ritchie H (November 2018). "The functional significance of dentin sialoprotein-phosphophoryn and dentin sialoprotein". International Journal of Oral Science. 10 (4): 31. doi:10.1038/s41368-018-0035-9. PMC   6215839 . PMID   30393383.
  4. ↑ Qin C, Brunn JC, Baba O, Wygant JN, McIntyre BW, Butler WT (June 2003). "Dentin sialoprotein isoforms: detection and characterization of a high molecular weight dentin sialoprotein". European Journal of Oral Sciences. 111 (3): 235–242. doi:10.1034/j.1600-0722.2003.00043.x. PMID   12786955.
  5. ↑ Yuan GH, Yang GB, Wu LA, Chen Z, Chen S (January 2010). "Potential Role of Dentin Sialoprotein by Inducing Dental Pulp Mesenchymal Stem Cell Differentiation and Mineralization for Dental Tissue Repair". Dental Hypotheses. 1 (2): 69–75. doi:10.5436/j.dehy.2010.1.00012. PMC   3118649 . PMID   21698071.
  6. ↑ Ritchie HH, Ritchie DG, Wang LH (January 1998). "Six decades of dentinogenesis research. Historical and prospective views on phosphophoryn and dentin sialoprotein". European Journal of Oral Sciences. 106 Suppl 1 (S1): 211–220. doi:10.1111/j.1600-0722.1998.tb02178.x. PMID   9541228.
  7. ↑ Chuang SF, Chen YH, Ma PX, Ritchie HH (September 2022). "Dentin Sialoprotein/Phosphophoryn (DSP/PP) as Bio-Inductive Materials for Direct Pulp Capping". Polymers. 14 (17): 3656. doi: 10.3390/polym14173656 . PMC   9460548 . PMID   36080731.
  8. ↑ Butler WT, Ritchie H (February 1995). "The nature and functional significance of dentin extracellular matrix proteins". The International Journal of Developmental Biology. 39 (1): 169–179. PMID   7626404.
  9. 1 2 3 Suzuki S, Sreenath T, Haruyama N, Honeycutt C, Terse A, Cho A, et al. (May 2009). "Dentin sialoprotein and dentin phosphoprotein have distinct roles in dentin mineralization". Matrix Biology. 28 (4): 221–229. doi:10.1016/j.matbio.2009.03.006. PMC   2758621 . PMID   19348940.
  10. ↑ Yuan G, Chen L, Feng J, Yang G, Ni Q, Xu X, et al. (February 2017). "Dentin Sialoprotein is a Novel Substrate of Matrix Metalloproteinase 9 in vitro and in vivo". Scientific Reports. 7 (1): 42449. Bibcode:2017NatSR...742449Y. doi:10.1038/srep42449. PMC   5307955 . PMID   28195206.
  11. ↑ Qin C, Brunn JC, Cadena E, Ridall A, Butler WT (January 2003). "Dentin sialoprotein in bone and dentin sialophosphoprotein gene expressed by osteoblasts". Connective Tissue Research. 44 Suppl 1 (1): 179–183. doi:10.1080/03008200390152296. PMID   12952194. S2CID   44252832.
  12. ↑ Ritchie HH, Pinero GJ, Hou H, Butler WT (January 1995). "Molecular analysis of rat dentin sialoprotein". Connective Tissue Research. 33 (1–3): 73–79. doi:10.3109/03008209509016985. PMID   7554965.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.