Utility of the dentin matrix protein 1 (DMP1) gene for resolving mammalian intraordinal phylogenetic relationships

Bussche, Ronald A. Van Den; Reeder, Serena A.; Hansen, Eric W.; Hoofer, Steven R.

doi:10.1016/s1055-7903(02)00297-x

Cited by 27 publications

(11 citation statements)

References 29 publications

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“…comparisons among a variety of species suggest that the DMP1 gene is one of the most rapidly evolving genes examined to date (32)(33)(34). However, one of the most conserved regions in the DMP1 protein is localized at the cleavage site demonstrated in the current study to be utilized by the BMP-1/Tolloid-like proteinases (Fig.…”

Section: Bmp-1/tolloid-like Enzymes Process Dmp1mentioning

confidence: 66%

Bone Morphogenetic Protein-1/Tolloid-like Proteinases Process Dentin Matrix Protein-1

Steiglitz

Ayala

Narayanan

et al. 2004

Journal of Biological Chemistry

125

131

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Bone morphogenetic protein-1 (BMP-1)/Tolloid-like metalloproteinases play key roles in formation of mammalian extracellular matrix (ECM), through the biosynthetic conversion of precursor proteins into their mature functional forms. These proteinases probably play a further role in formation of bone through activation of transforming growth factor ␤-like BMPs. Dentin matrix protein-1 (DMP1), deposited into the ECM during assembly and involved in initiating mineralization of bones and teeth, is thought to undergo proteolysis in vivo to generate functional cleavage fragments found in extracts of mineralized tissues. Here, we have generated recombinant DMP1 and demonstrate that it is cleaved, to varying extents, by all four mammalian BMP-1/ Tolloid-like proteinases, to generate fragments similar in size to those previously isolated from bone. Consistent with possible roles for the BMP-1/Tolloid-like proteinases in the physiological processing of DMP1, NH 2 -terminal sequences of products generated by BMP-1 cleavage of DMP1 match those predicted from processing at the predicted DMP1 site that shows greatest cross-species conservation of sequences. Moreover, fibroblasts derived from mouse embryos homozygous null for genes encoding three of the four mammalian BMP-1/Tolloid-like proteinases appear to be deficient in processing of DMP1. Thus, a further role for BMP-1-Tolloidlike proteinases in formation of mineralized tissues is indicated, via proteolytic processing of DMP1.Bone morphogenetic protein-1 (BMP-1) 1 is the prototype of a family of metalloproteinases involved in morphogenesis in a broad range of species (1). These proteinases mediate morphogenetic effects in part by biosynthetic processing of precursors into the mature functional forms of proteins necessary to formation of the extracellular matrix. For example, they provide the procollagen C-proteinase activity that excises the carboxylterminal propeptides of procollagens I-III, to yield the major fibril-forming components of the extracellular matrix (ECM) (2-6). They also participate in the biosynthetic processing of the minor fibrillar collagens V and XI (6 -8), which in turn further regulate the physical properties of types I and II collagen fibers (9, 10). The BMP-1/Tolloid-like proteinases have also been shown to process a precursor to produce the small leucinerich proteoglycan biglycan (11), a molecule that positively regulates bone growth, influences type I collagen fibril morphology, and also may influence dentin mineralization (12-14). The BMP-1/Tolloid-like proteinases have also been implicated in the biosynthetic processing of laminin 5 (15, 16) and type VII collagen (17) and shown to proteolytically activate lysyl oxidase (18), an enzyme required for covalent cross-linking of collagen and elastin fibers. These metalloproteinases may thus be central regulators in the formation of ECM.Type I collagen is the major organic component of mineralized ECM and serves as the template upon which mineral is deposited in tissues such as bone and dentin. Noncol...

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Section: Bmp-1/tolloid-like Enzymes Process Dmp1mentioning

confidence: 66%

Bone Morphogenetic Protein-1/Tolloid-like Proteinases Process Dentin Matrix Protein-1

Steiglitz

Ayala

Narayanan

et al. 2004

Journal of Biological Chemistry

125

131

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“…Other characters shared between Myzopoda and the Pteropodiformes included character 6, character 28, and character 79. That chromosomal evolution in Myzopoda has, in part, been characterized by the retention of sympleisiomorphic characters (e.g., character 74) lends support to the consideration of the family as one of the more primitive members of the Vespertilioniformes (Van Den Bussche and Hoofer 2001;Hoofer et al 2003;Van Den Bussche et al 2003).…”

Section: Phylogenomic Relationships Between Myzopoda and Other Chiropmentioning

confidence: 95%

“…Cladistic analyses of morphological data place Myzopoda either basal to the Nataloidea (sensu Simmons 1998) and Vespertilionoidea (Smith 1976), within the Nataloidea (Simmons and Geisler 1998), or within the Vespertilionoidea (Koopman 1994). In contrast, molecular studies, using a concatenation of three mitochondrial (12S rRNA, tRNA val , 16S rRNA; Van Den Bussche and Hoofer 2001) and/or two nuclear (RAG2 and dentin matrix protein 1, Hoofer et al 2003;Van Den Bussche et al 2003) genes are congruent in placing the Myzopodidae as the most ancestral family within the Vespertilioniformes, sister to Emballonuridae. In addition, using only RAG2 sequence data, Van Den Bussche et al (2003) retrieved an alternate topology positioning Myzopoda within the Emballonuridae.…”

Section: Introductionmentioning

confidence: 99%

“…In contrast, molecular studies, using a concatenation of three mitochondrial (12S rRNA, tRNA val , 16S rRNA; Van Den Bussche and Hoofer 2001) and/or two nuclear (RAG2 and dentin matrix protein 1, Hoofer et al 2003;Van Den Bussche et al 2003) genes are congruent in placing the Myzopodidae as the most ancestral family within the Vespertilioniformes, sister to Emballonuridae. In addition, using only RAG2 sequence data, Van Den Bussche et al (2003) retrieved an alternate topology positioning Myzopoda within the Emballonuridae. Further molecular analyses, based on nuclear markers (PRCK1, SPTBN, STAT5A, THY), position Myzopoda within the Vespertilionoidea (Eick et al 2005).…”

Section: Introductionmentioning

confidence: 99%

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Cross-species chromosome painting in bats from Madagascar: the contribution of Myzopodidae to revealing ancestral syntenies in Chiroptera

et al. 2010

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The chiropteran fauna of Madagascar comprises eight of the 19 recognized families of bats, including the endemic Myzopodidae. While recent systematic studies of Malagasy bats have contributed to our understanding of the morphological and genetic diversity of the island's fauna, little is known about their cytosystematics. Here we investigate karyotypic relationships among four species, representing four families of Chiroptera endemic to the Malagasy region using cross-species chromosome painting with painting probes of Myotis myotis: Myzopodidae (Myzopoda aurita, 2n = 26), Molossidae (Mormopterus jugularis, 2n = 48), Miniopteridae (Miniopterus griveaudi, 2n = 46), and Vespertilionidae (Myotis goudoti, 2n = 44). This study represents the first time a member of the family Myzopodidae has been investigated using chromosome painting. Painting probes of M. myotis were used to delimit 29, 24, 23, and 22 homologous chromosomal segments in the genomes of M. aurita, M. jugularis, M. griveaudi, and M. goudoti, respectively. Comparison of GTG-banded homologous chromosomes/chromosomal segments among the four species revealed the genome of M. aurita has been structured through 14 fusions of chromosomes and chromosomal segments of M. myotis chromosomes leading to a karyotype consisting solely of bi-armed chromosomes. In addition, chromosome painting revealed a novel X-autosome translocation in M. aurita. Comparison of our results with published chromosome maps provided further evidence for karyotypic conservatism within the genera Mormopterus, Miniopterus, and Myotis. Mapping of chromosomal rearrangements onto a molecular consensus phylogeny revealed ancestral syntenies shared between Myzopoda and other bat species of the infraorders Pteropodiformes and Vespertilioniformes. Our study provides further evidence for the involvement of Robertsonian (Rb) translocations and fusions/fissions in chromosomal evolution within Chiroptera.

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“…In fact, we are unaware of any other protein that shows such length polymorphisms. Length polymorphisms in the coding region for dentin matrix protein 1 (DMP1) proved useful in defining phylogenetic relationships among closely related species of bat 39) , but DMP1 size heterogeneity at the protein level has not been reported. DPP isolated from our dentin extracts shows up as multiple (usually 4) bands migrating between 96-kDa and 100-kDa on SDS-PAGE.…”

Section: Dentin Phosphoprotein (Dpp)mentioning

confidence: 99%

Dentin Sialophosphoprotein (DSPP) and Dentin

Yamakoshi¹

2008

J. Oral Biosci.

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The revolution in genetics disclosed the types of malformations that occur when expression of a particular gene is lost. In the case of tooth dentin, mutations in the two genes encoding type I collagen cause osteogenesis imperfecta, a bone condition that often includes dentin malformations. Besides collagen, there are a number of non-collagenous proteins in dentin. Among the genes encoding the dentin non-collagenous proteins, only mutations in DSPP (dentin sialophosphoprotein) cause inherited dental malformations. DSPP mutations cause dentinogenesis imperfecta types II and III, and dentin dysplasia type II. DSPP is the most abundant non-collagenous protein in dentin. DSPP protein is necessary for proper dentin formation, and understanding its structure and function should yield important insights into how dentin forms and biomineralization is controlled. DSPP is expressed and secreted by odontoblasts, the cells that make tooth dentin and that also maintain cell processes extending into the mineralized tissue. Following its secretion, DSPP is cleaved into smaller pieces by multiple extracellular proteases. For the last five years I have devoted myself to characterizing DSPP-derived proteins. DSPP is cleaved by proteases into three main parts : dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP). We have learned that DSP is a proteoglycan that forms covalent dimers, DGP is a phosphorylated glycoprotein, and DPP is a highly phosphorylated intrinsically disordered protein that shows extensive length polymorphisms due to the genetic heterogeneity of its coding region.

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Utility of the dentin matrix protein 1 (DMP1) gene for resolving mammalian intraordinal phylogenetic relationships

Cited by 27 publications

References 29 publications

Bone Morphogenetic Protein-1/Tolloid-like Proteinases Process Dentin Matrix Protein-1

Bone Morphogenetic Protein-1/Tolloid-like Proteinases Process Dentin Matrix Protein-1

Cross-species chromosome painting in bats from Madagascar: the contribution of Myzopodidae to revealing ancestral syntenies in Chiroptera

Dentin Sialophosphoprotein (DSPP) and Dentin

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