scholarly journals In situ localization and chromosomal mapping of the AG1 (Dmp1) gene.

1994 ◽  
Vol 42 (12) ◽  
pp. 1527-1531 ◽  
Author(s):  
A George ◽  
J Gui ◽  
N A Jenkins ◽  
D J Gilbert ◽  
N G Copeland ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Type I Collagen ◽  
Chromosomal Mapping ◽  
Human Tooth ◽  
Type I ◽  
Dentin Matrix Protein ◽  
Biomineralization Process ◽  
Tooth Mineralization ◽  
The Matrix

Dentinogenesis is being used as a model for understanding the biomineralization process. The odontoblasts synthesize a structural matrix comprised of Type I collagen fibrils which define the basic architecture of the tissue. The odontoblasts also synthesize and deliver a number of dentin-specific acidic macromolecules into the extracellular compartment. These acidic macromolecules may be involved in regulating the ordered deposition of hydroxyapatite crystals within the matrix. AG1 is the first tooth-specific acidic macromolecule to have been cloned and sequenced. To identify which cells of the rat incisor pulp/odontoblast complex were responsible for synthesis of AG1, in situ hybridization was used. Digoxigenin labeled sense and anti-sense AG1 riboprobes were prepared. The AG1 mRNA was found to be expressed in the mature secretory odontoblasts. Neither pulp cells nor pre-odontoblasts showed any staining with the anti-sense probes. Chromosomal localization studies placed the AG1 gene on mouse chromosome 5q21, in tight linkage with Fgf5. AG1 has been renamed Dmp1 (dentin matrix protein 1) in accordance with present chromosomal nomenclature. Mouse 5q21 corresponds to the 4q21 locus in humans. This is the locus for the human tooth mineralization disorder dentinogenesis imperfecta Type II (DI-II). These data suggest that the Dmp1 gene is involved in mineralization and is a candidate gene for DI-II.

Type I collagen regulated dentin matrix protein-1 (Dmp-1) and osteocalcin (OCN) gene expression of rat dental pulp cells

2003 ◽  
Vol 88 (6) ◽  
pp. 1112-1119 ◽  
Author(s):  
Morimichi Mizuno ◽  
Tetsuro Miyamoto ◽  
Keinoshin Wada ◽  
Sanae Watatani ◽  
Gui Xia Zhang
Keyword(s):  
Gene Expression ◽  
Dental Pulp ◽  
Matrix Protein ◽  
Type I Collagen ◽  
Type I ◽  
Dental Pulp Cells ◽  
Dentin Matrix Protein 1 ◽  
Dentin Matrix Protein ◽  
Pulp Cells ◽  
Dentin Matrix

scholarly journals Immunocytochemical detection of dentin matrix proteins in primary teeth from patients with dentinogenesis imperfecta associated with osteogenesis imperfecta

2014 ◽  
Author(s):  
G. Orsini ◽  
A. Majorana ◽  
A. Mazzoni ◽  
A. Putignano ◽  
M. Falconi ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Matrix Protein ◽  
Primary Teeth ◽  
Type I Collagen ◽  
Immunohistochemical Analysis ◽  
Matrix Proteins ◽  
Type I ◽  
Dentinogenesis Imperfecta ◽  
Dentin Matrix Protein ◽  
Dentin Matrix

Dentinogenesis imperfecta determines structural alterations of the collagen structure still not completely elucidated. Immunohistochemical analysis was used to assay Type I and VI collagen, various non-collagenous proteins distribution in human primary teeth from healthy patients or from patients affected by type I dentinogenesis imperfecta (DGI-I) associated with osteogenesis imperfecta (OI). In sound primary teeth, an organized well-known ordered pattern of the type I collagen fibrils was found, whereas atypical and disorganized fibrillar structures were observed in dentin of DGI-I affected patients. Expression of type I collagen was observed in both normal and affected primary teeth, although normal dentin stained more uniformly than DGI-I affected dentin. Reactivity of type VI collagen was significantly lower in normal teeth than in dentin from DGI-I affected patients (P<0.05). Expressions of dentin matrix protein (DMP)-1 and osteopontin (OPN) were observed in both normal dentin and dentin from DGI-I affected patients, without significant differences, being DMP1 generally more abundantly expressed. Immunolabeling for chondroitin sulfate (CS) and biglycan (BGN) was weaker in dentin from DGI-I-affected patients compared to normal dentin, this decrease being significant only for CS. This study shows ultrastructural alterations in dentin obtained from patients affected by DGI-I, supported by immunocytochemical assays of different collagenous and non-collagenous proteins.

scholarly journals BMP1 and TLL1 Are Required for Maintaining Periodontal Homeostasis

2017 ◽  
Vol 96 (5) ◽  
pp. 578-585 ◽  
Author(s):  
J. Wang ◽  
D. Massoudi ◽  
Y. Ren ◽  
A.M. Muir ◽  
S.E. Harris ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Significant Loss ◽  
Tartrate Resistant Acid Phosphatase ◽  
Type I ◽  
Dentin Matrix Protein ◽  
Morphogenetic Protein ◽  
Periodontal Breakdown

Mutations in bone morphogenetic protein 1 (BMP1) in humans or deletion of BMP1 and related protease tolloid like 1 (TLL1) in mice lead to osteogenesis imperfecta (OI). Here, we show progressive periodontal defects in mice in which both BMP1 and TLL1 have been conditionally ablated, including malformed periodontal ligament (PDL) (recently shown to play key roles in normal alveolar bone formation), significant loss in alveolar bone mass ( P < 0.01), and a sharp reduction in cellular cementum. Molecular mechanism studies revealed a dramatic increase in the uncleaved precursor of type I collagen (procollagen I) and a reduction in dentin matrix protein 1 (DMP1), which is partially responsible for defects in extracellular matrix (ECM) formation and mineralization. We also showed a marked increase in the expression of matrix metallopeptidase 13 (MMP13) and tartrate-resistant acid phosphatase (TRAP), leading to an acceleration in periodontal breakdown. Finally, we demonstrated that systemic application of antibiotics significantly improved the alveolar bone and PDL damage of the knockdown phenotype, which are thus shown to be partially secondary to pathogen-induced inflammation. Together, identification of the novel roles of BMP1 and TLL1 in maintaining homeostasis of periodontal formation, partly via biosynthetic processing of procollagen I and DMP1, provides novel insights into key contributions of the extracellular matrix environment to periodontal homeostasis and contributes toward understanding of the pathology of periodontitis.

Hyper-expression of Osteocalcin mRNA in Odontoblasts of Hyp Mice

2005 ◽  
Vol 84 (1) ◽  
pp. 84-88 ◽  
Author(s):  
T. Onishi ◽  
T. Ogawa ◽  
T. Hayashibara ◽  
T. Hoshino ◽  
R. Okawa ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Type I Collagen ◽  
Tooth Germ ◽  
Type I ◽  
Wild Type ◽  
Gene Expressions ◽  
Dentin Matrix Protein ◽  
Osteocalcin Gene ◽  
Dentin Matrix

The Hyp mouse is a murine homologue of human X-linked hypophosphatemia that displays hypo-mineralization in bone and dentin. In this study, we tested the hypothesis that the defect in Hyp mice leads to alterations in the expression of dentin matrix proteins that may be associated with the hypo-mineralization changes in the tissues. Quantitative RT-PCR analyses showed that expression of the osteocalcin gene in Hyp mice tooth germ samples was significantly higher than in wild-type mice, whereas the gene expressions of osteonectin, osteopontn, dentin matrix protein 1, and type I collagen in both types of mice were similar. Further, cultured Hyp mice tooth germ samples exhibited a higher expression of the osteocalcin gene than did those from wild-type mice, which was in accord with the results of our in vivo analysis. These findings suggest that osteocalcin mRNA is highly expressed in Hyp mice odontoblasts and may be associated with dentin hypo-mineralization.

Rapamycin inhibits fibronectin-induced migration of the human arterial smooth muscle line (E47) through the mammalian target of rapamycin

2005 ◽  
Vol 288 (6) ◽  
pp. H2861-H2868 ◽  
Author(s):  
Kenji Sakakibara ◽  
Bo Liu ◽  
Scott Hollenbeck ◽  
K. Craig Kent
Keyword(s):  
Smooth Muscle ◽  
Signaling Pathway ◽  
Matrix Protein ◽  
Type I Collagen ◽  
Critical Role ◽  
Mammalian Target Of Rapamycin ◽  
Target Of Rapamycin ◽  
Type I ◽  
Downstream Effector ◽  
The Matrix

The matrix protein fibronectin (FN) is a potent agoinst of vascular smooth muscle cell (SMC) migration. The role of rapamycin and the mammalian target of rapamycin (mTOR) in matrix protein-induced migration has not yet been defined. In these studies, we found that rapamycin (10 nM) markedly diminished chemotaxis of E47 cells (a cell line derived from human atherosclerotic plaques) and rat aortic SMCs toward FN as well as type I collagen and laminin; however, a period of preincubation >20 h was required. Subsequently, we showed that treatment with FN induced a rapid activation of mTOR as well as its downstream effector, S6 kinase (S6K). Moreover, FN-induced activation of both proteins was inhibited by preincubation with rapamycin for only 30 min. We then explored the upstream signaling pathway through which FN might mediate mTOR activation. A blocking antibody to αvβ3 inhibited FN-induced mTOR/S6K activation as well as E47 cell chemotaxis, implicating αvβ3 as the integrin receptor responsible for initiating FN-induced migration. Moreover, preincubation of E47 cells with wortmannin or LY-294002 blocked FN-induced mTOR/S6K activation, demonstrating that phosphatidylinositol 3-kinase (PI3K) plays a critical role in this rapamycin-sensitive signaling pathway. It has been previously suggested that rapamycin's effect on migration maybe related to enhancement of p27kip1. However, treatment of E47 cells with rapamycin did not alter the level of p27kip1 in the presence or absence of FN. Taken together, our data demonstrate that rapamycin inhibits FN-induced SMC migration through a pathway that involves at least αvβ3-integrin, PI3K, mTOR, and S6K.

Hereditary Dentin Defects

2007 ◽  
Vol 86 (5) ◽  
pp. 392-399 ◽  
Author(s):  
J.-W. Kim ◽  
J.P. Simmer
Keyword(s):  
Matrix Protein ◽  
Type I Collagen ◽  
Rare Condition ◽  
Type I ◽  
Gene Encoding ◽  
Apparent Lack ◽  
Post Translational Modifications ◽  
Dentin Matrix Protein ◽  
Genes Encoding ◽  
Secreted Phosphoprotein 1

By the Shields classification, articulated over 30 years ago, inherited dentin defects are divided into 5 types: 3 types of dentinogenesis imperfecta (DGI), and 2 types of dentin dysplasia (DD). DGI type I is osteogenesis imperfecta (OI) with DGI. OI with DGI is caused, in most cases, by mutations in the 2 genes encoding type I collagen. Many genes are required to generate the enzymes that catalyze collagen’s diverse post-translational modifications and its assembly into fibers, fibrils, bundles, and networks. Rare inherited diseases of bone are caused by defects in these genes, and some are occasionally found to include DGI as a feature. Appreciation of the complicated genetic etiology of DGI associated with bony defects splintered the DGI type I description into a multitude of more precisely defined entities, all with their own designations. In contrast, DD-II, DGI-II, and DGI-III, each with its own pattern of inherited defects limited to the dentition, have been found to be caused by various defects in DSPP (dentin sialophosphoprotein), a gene encoding the major non-collagenous proteins of dentin. Only DD-I, an exceedingly rare condition featuring short, blunt roots with obliterated pulp chambers, remains untouched by the revolution in genetics, and its etiology is still a mystery. A major surprise in the characterization of genes underlying inherited dentin defects is the apparent lack of roles played by the genes encoding the less-abundant non-collagenous proteins in dentin, such as dentin matrix protein 1 ( DMP1), integrin-binding sialoprotein ( IBSP), matrix extracellular phosphoglycoprotein ( MEPE), and secreted phosphoprotein-1, or osteopontin ( SPP1, OPN). This review discusses the development of the dentin extracellular matrix in the context of its evolution, and discusses the phenotypes and clinical classifications of isolated hereditary defects of tooth dentin in the context of recent genetic data respecting their genetic etiologies.

scholarly journals The Matrix Protein of Nipah Virus Targets the E3-Ubiquitin Ligase TRIM6 to Inhibit the IKKε Kinase-Mediated Type-I IFN Antiviral Response

2016 ◽  
Vol 12 (9) ◽  
pp. e1005880 ◽  
Author(s):  
Preeti Bharaj ◽  
Yao E. Wang ◽  
Brian E. Dawes ◽  
Tatyana E. Yun ◽  
Arnold Park ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Matrix Protein ◽  
Nipah Virus ◽  
E3 Ubiquitin Ligase ◽  
Antiviral Response ◽  
Type I ◽  
Type I Ifn ◽  
The Matrix

Cytoskeleton and thyroglobulin expression change during transformation of thyroid epithelium to mesenchyme-like cells

Development ◽  
1988 ◽  
Vol 102 (3) ◽  
pp. 605-622 ◽  
Author(s):  
G. Greenburg ◽  
E.D. Hay
Keyword(s):  
Type I Collagen ◽  
Collagen Gel ◽  
Type I ◽  
Basal Cells ◽  
Collagen Gels ◽  
Expression Change ◽  
Cell Functions ◽  
The Matrix ◽  
3D Matrix ◽  
Mesenchymal Transformation

In considering the mechanism of transformation of epithelium to mesenchyme in the embryo, it is generally assumed that the ability to give rise to fibroblast-like cells is lost as epithelia mature. We reported previously that a definitive embryonic epithelium, that of the anterior lens, gives rise to freely migrating mesenchyme-like cells when suspended in type I collagen matrices. Here, we show that a highly differentiated epithelium that expresses cytokeratin changes to a vimentin cytoskeleton and loses thyroglobulin during epithelial-mesenchymal transformation induced by suspension in collagen gel. Using dispase and collagenase, we isolated adult thyroid follicles devoid of basal lamina and mesenchyme, and we suspended the follicles in 3D collagen gels. Cells bordering the follicle lumen retain epithelial polarity and thyroid phenotype, but basal cell surface organization is soon modified as a result of tissue multilayering and elongation of basal cells into the collagenous matrix. Cytodifferentiation, determined by thyroglobulin immunoreactivity, is lost as the basal epithelial cells move into the matrix after 3–4 days in collagen. By TEM, it can be seen that the elongating cells acquire pseudopodia, filopodia and mesenchyme-like nuclei and RER. Immunofluorescence examination of intermediate filaments showed that freshly isolated follicles and follicles cultured on planar substrata react only with anticytokeratin. However, all of the mesenchyme-like cells express vimentin and they gradually lose cytokeratin. These results suggest that vimentin may be necessary for cell functions associated with migration within a 3D matrix. The mesenchymal cells do not revert to epithelium when grown on planar substrata and the transformation of epithelium to mesenchyme-like cells does not occur within basement membrane gels. The results are relevant to our understanding of the initiation of epithelial-mesenchymal transformation in the embryo and the genetic mechanisms controlling cell shape, polarity and cytoskeletal phenotype.

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