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Article ; Online: The role of acidic phosphoproteins in biomineralization.

Alvares, Keith

2014 Volume 55, Issue 1, Page(s) 34–40

Abstract: Biomineralization is the process by which living organisms deposit mineral in the extracellular matrix. In nature, almost 50% of biominerals are calcium-bearing minerals. In addition to calcium, we find biominerals formed from silica and magnetite. ... ...

Abstract	Biomineralization is the process by which living organisms deposit mineral in the extracellular matrix. In nature, almost 50% of biominerals are calcium-bearing minerals. In addition to calcium, we find biominerals formed from silica and magnetite. Calcium-containing biominerals could be either calcium phosphate as in apatite found in vertebrates or calcium carbonate as in calcite and aragonite found in many invertebrates. Since all biomineralization is matrix mediated, an understanding of the nature of the proteins involved is essential in elucidating its mechanism. This review will discuss some of the proteins involved in the process of biomineralization involving calcium. Two proteins, dentin matrix protein 1 and dentin phosphoprotein (Phosphophoryn) will serve as models for the vertebrate system, and two others - P16 and phosphodontin will serve as models for the invertebrate system.
MeSH term(s)	Acids/metabolism ; Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Humans ; Invertebrates/metabolism ; Molecular Sequence Data ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Vertebrates/metabolism
Chemical Substances	Acids ; Phosphoproteins
Language	English
Publishing date	2014-01-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	185551-7
ISSN	1607-8438 ; 0091-1690 ; 0300-8207
ISSN (online)	1607-8438
ISSN	0091-1690 ; 0300-8207
DOI	10.3109/03008207.2013.867336
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Article ; Online: Antitumor agent cabozantinib decreases RANKL expression in osteoblastic cells and inhibits osteoclastogenesis and PTHrP-stimulated bone resorption.

Stern, Paula H / Alvares, Keith

Journal of cellular biochemistry

2014 Volume 115, Issue 11, Page(s) 2033–2038

Abstract: Cabozantinib, an inhibitor of vascular endothelial growth factor and hepatocyte growth factor signaling, decreases bone lesions in patients with prostate cancer. To determine direct effects of cabozantinib on bone, resorption in neonatal mouse bone organ ...

Abstract	Cabozantinib, an inhibitor of vascular endothelial growth factor and hepatocyte growth factor signaling, decreases bone lesions in patients with prostate cancer. To determine direct effects of cabozantinib on bone, resorption in neonatal mouse bone organ culture and on gene expression, proliferation, and phenotypic markers in osteoblast and osteoclast cell lines were examined. Cabozantinib, 0.3 and 3 µM, prevented PTHrP-stimulated calcium release from neonatal mouse calvaria. Since the effect on resorption could reflect effects on osteoblasts to prevent osteoclast activation, or direct inhibition of osteoclasts, responses in osteoblastic and osteoclast precursor cell lines were examined. Twenty-four-hour treatment of osteoblastic MC3T3-E1 cells with 3 µM cabozantinib decreased expression of receptor activator of NFkB ligand (RANKL) and alkaline phosphatase. Forty-eight-hour treatment of MC3T3-E1 cells with 3 µM cabozantinib inhibited cell proliferation and decreased MTT activity. Effects on alkaline phosphatase activity were biphasic, with small stimulatory effects at concentrations below 3 µM. When RAW 264.7 osteoclast precursor cells differentiated with 20 ng/ml RANKL were co-treated for 24 h with 3 µM cabozantinib, expression of RANK, TRAP, cathepsin K, alpha v or beta 3 integrin, or NFATc1 were unaffected. Five-day treatment of RANKL-treated RAW 264.7 cells with 3 µM cabozantinib decreased TRAP and MTT activity. The results suggest that the osteoblast could be the initial target, with subsequent direct and indirect effects on osteoclastogenesis leading to decreased resorption. The multiple effects of cabozantinib on the cell microenvironment of bone are consistent with its effectiveness in reducing lesions from prostate cancer metastases.
MeSH term(s)	3T3 Cells ; Anilides/pharmacology ; Animals ; Bone Resorption/chemically induced ; Bone Resorption/drug therapy ; Cell Line ; Cell Proliferation/drug effects ; Down-Regulation ; Mice ; Osteoblasts/cytology ; Osteoblasts/drug effects ; Osteoclasts/cytology ; Osteoclasts/drug effects ; Osteogenesis/drug effects ; Parathyroid Hormone-Related Protein/adverse effects ; Pyridines/pharmacology ; RANK Ligand/metabolism
Chemical Substances	Anilides ; Parathyroid Hormone-Related Protein ; Pyridines ; RANK Ligand ; Tnfsf11 protein, mouse ; cabozantinib (1C39JW444G)
Language	English
Publishing date	2014-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.24879
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Article ; Online: Commentary on "biomineralization--an active or passive process?".

Alvares, Keith / Veis, Arthur

Connective tissue research

2012 Volume 53, Issue 6, Page(s) 437

MeSH term(s)	Animals ; Calcification, Physiologic ; Calcinosis/metabolism ; Humans ; Tooth Calcification
Language	English
Publishing date	2012
Publishing country	England
Document type	Comment ; Journal Article
ZDB-ID	185551-7
ISSN	1607-8438 ; 0091-1690 ; 0300-8207
ISSN (online)	1607-8438
ISSN	0091-1690 ; 0300-8207
DOI	10.3109/03008207.2012.747301
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Article ; Online: The unique biomineralization transcriptome and proteome of Lytechinus variegatus teeth.

Alvares, Keith / DeHart, Caroline J / Thomas, Paul M / Kelleher, Neil L / Veis, Arthur

Connective tissue research

2018 Volume 59, Issue sup1, Page(s) 20–29

Abstract: Background: Matrix-regulated biomineralization involves the specific nucleation and growth of mineral phases within or upon preformed structured organic matrices. We hypothesized that there might be a general mechanism whereby anionic, phosphorylated ... ...

Abstract	Background: Matrix-regulated biomineralization involves the specific nucleation and growth of mineral phases within or upon preformed structured organic matrices. We hypothesized that there might be a general mechanism whereby anionic, phosphorylated mineral ion-binding proteins assist in specifically locating the mineral ions with respect to the mineralizing structural organic matrix. Here we extended these studies to invertebrate mineralization in Lytechinus variegatus (Lv) teeth. Materials and methods: The tooth proteins were extracted and the phosphoproteins occluded in the mineral were enriched by passage through a ProQ Diamond phosphoprotein enrichment column, and subjected to MS/MS analysis. A Lv RNA-seq derived transcriptome database was generated. The MS/MS data found 25 proteins previously classified as "Predicted uncharacterized proteins" and many of the spicule matrix proteins. As these 25 proteins were also identified with the transcriptome analysis, and were thus no longer "hypothetical" but real proteins in the Lv tooth. Each protein was analyzed for the presence of a signal peptide, an acidic pI≤4, and the ability to be phosphorylated. Results: Four new Lv tooth specific Pro-Ala-rich proteins were found, representing a new class of proteins. Conclusion: The tooth is different from the spicules and other urchin skeletal elements in that only the tooth contains both "high" and "very high" magnesium calcite, [Ca(1-X) Mg(X) CO3], where X is the mole fraction of Mg. We speculate that our newly discovered proline-alanine rich proteins, also containing sequences of acidic amino acids, may be involved in the formation of high magnesium and very high magnesium calcite.
MeSH term(s)	Animals ; Biomineralization/physiology ; Lytechinus/metabolism ; Proteome/metabolism ; Tooth/metabolism ; Transcriptome/physiology
Chemical Substances	Proteome
Language	English
Publishing date	2018-05-10
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	185551-7
ISSN	1607-8438 ; 0091-1690 ; 0300-8207
ISSN (online)	1607-8438
ISSN	0091-1690 ; 0300-8207
DOI	10.1080/03008207.2017.1408605
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Article ; Online: Expression of the invertebrate sea urchin P16 protein into mammalian MC3T3 osteoblasts transforms and reprograms them into "osteocyte-like" cells.

Alvares, Keith / Ren, Yinshi / Feng, Jian Q / Veis, Arthur

Journal of experimental zoology. Part B, Molecular and developmental evolution

2016 Volume 326, Issue 1, Page(s) 38–46

Abstract: P16 is an acidic phosphoprotein important in both sea urchin embryonic spicule development and transient mineralization during embryogenesis, syncytium formation, and mineralization in mature urchin tooth. Anti-P16 has been used to localize P16 to the ... ...

Abstract	P16 is an acidic phosphoprotein important in both sea urchin embryonic spicule development and transient mineralization during embryogenesis, syncytium formation, and mineralization in mature urchin tooth. Anti-P16 has been used to localize P16 to the syncytial membranes and the calcite mineral. Specific amino acid sequence motifs in P16 are similar to sequences in DSPP, a protein common to all vertebrate teeth, and crucial for their mineralization. Here, we examine the effect of P16 on vertebrate fibroblastic NIH3T3 cells and osteoblastic MC3T3 cells. Transfection of NIH3T3 cells with P16 cDNA resulted in profound changes in the morphology of the cells. In culture, the transfected cells sent out long processes that contacted processes from neighboring cells forming networks or syncytia. There was a similar change in morphology in cultured osteoblastic MC3T3 cells. In addition, the MC3T3 developed numerous dendrites as found in osteocytes. Importantly, there was also a change in the expression of the osteoblast and osteocyte specific genes. MC3T3 cells transfected with P16 showed an 18-fold increase in expression of the osteocyte specific Dentin matrix protein (DMP1) gene, accompanied by decreased expression of osteoblast specific genes: Bone sialoprotein (BSP), osteocalcin (OCN), and β-catenin decreased by 70%, 64%, and 68 %, respectively. Thus, invertebrate urchin P16 with no previously known analog in vertebrates was able to induce changes in both cell morphology and gene expression, converting vertebrate-derived osteoblast-like precursor cells to an "osteocyte-like" phenotype, an important process in bone biology. The mechanisms involved are presently under study.
MeSH term(s)	3T3 Cells ; Animals ; Calcification, Physiologic ; Cell Differentiation ; Gene Expression Regulation ; Giant Cells/cytology ; Mice ; NIH 3T3 Cells ; Osteoblasts/cytology ; Osteoblasts/physiology ; Osteocytes/cytology ; Osteocytes/physiology ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Sea Urchins/metabolism ; Transfection
Chemical Substances	Phosphoproteins
Language	English
Publishing date	2016-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2103823-5
ISSN	1552-5015 ; 0022-104X ; 1552-5007
ISSN (online)	1552-5015
ISSN	0022-104X ; 1552-5007
DOI	10.1002/jez.b.22663
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Article: Culture of and experiments with sea urchin embryo primary mesenchyme cells.

Moreno, Bradley / DiCorato, Allessandra / Park, Alexander / Mobilia, Kellen / Knapp, Regina / Bleher, Reiner / Wilke, Charlene / Alvares, Keith / Joester, Derk

Methods in cell biology

2019 Volume 150, Page(s) 293–330

Abstract: Skeletogenesis in the sea urchin embryo gives rise to a pair of intricate endoskeletal spicules. Deposition of these skeletal elements in the early larva is the outcome of a morphogenetic program that begins with maternal inputs in the early zygote and ... ...

Abstract	Skeletogenesis in the sea urchin embryo gives rise to a pair of intricate endoskeletal spicules. Deposition of these skeletal elements in the early larva is the outcome of a morphogenetic program that begins with maternal inputs in the early zygote and results in the specification of the large micromere-primary mesenchyme cell (PMC) lineage. PMCs are of considerable interest as a model system, not only to dissect the mechanism of specific developmental processes, but also to investigate their evolution and the unrivaled level of control over the formation of a graded, mechanically robust, yet single crystalline biomineral. The ability to study gene regulatory circuits, cellular behavior, signaling pathways, and molecular players involved in biomineralization is significantly boosted by the high level of autonomy of PMCs. In fact, in the presence of horse serum, micromeres differentiate into PMCs and produce spicules in vitro, separated from the embryonic milieu. PMC culture eliminates indirect effects that can complicate the interpretation of experiments in vivo, offers superior spatiotemporal control, enables PMC-specific readouts, and is compatible with most imaging and characterization techniques. In this chapter, we provide an updated protocol, based on the pioneering work by Okazaki and Wilt, for the isolation of micromeres and subsequent culture of PMCs, as well as protocols for fixation and staining for fluorescent microscopy, preparation of cell cultures for electron microscopy, and the isolation of RNA.
MeSH term(s)	Animals ; Cytological Techniques/methods ; Embryo, Nonmammalian/cytology ; Gene Expression Regulation, Developmental/physiology ; Mesoderm/cytology ; Sea Urchins/cytology ; Signal Transduction/physiology
Language	English
Publishing date	2019-02-11
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ISSN	0091-679X
ISSN	0091-679X
DOI	10.1016/bs.mcb.2019.01.002
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Article ; Online: Dentin phosphoprotein binds annexin 2 and is involved in calcium transport in rat kidney ureteric bud cells.

Alvares, Keith / Stern, Paula H / Veis, Arthur

The Journal of biological chemistry

2013 Volume 288, Issue 18, Page(s) 13036–13045

Abstract: Dentin phosphoprotein (DPP) is the most abundant noncollagenous protein in the dentin, where it plays a major role in the mineralization of dentin. However, we and others have shown that in addition to being present in the dentin, DPP is also present in ... ...

Abstract	Dentin phosphoprotein (DPP) is the most abundant noncollagenous protein in the dentin, where it plays a major role in the mineralization of dentin. However, we and others have shown that in addition to being present in the dentin, DPP is also present in nonmineralizing tissues like the kidney, lung, and salivary glands, where it conceivably has other functions such as in calcium transport. Because annexins have been implicated as calcium transporters, we examined the relationships between DPP and annexins. In this report, we show that DPP binds to annexin 2 and 6 present in a rat ureteric bud cell line (RUB1). Immunofluorescence studies show that annexin 2 and DPP colocalize in these cells. In addition, DPP and annexin 2 colocalize in the ureteric bud branches of embryonic metanephric kidney. In the RUB1 cells and ureteric bud branches of embryonic kidney, colocalization was restricted to the cell membrane. Studies on calcium influx into RUB cells show that in the presence of anti-DPP, there was a 40% reduction of calcium influx into these cells. We postulate that DPP has different functions in the kidney as compared with the odontoblasts. In the odontoblasts, its primary function is in the extracellular mineralization of dentin, whereas in the kidney it may participate in calcium transport.
MeSH term(s)	Animals ; Annexin A2/genetics ; Annexin A2/metabolism ; Calcium/metabolism ; Cell Line ; Embryo, Mammalian/cytology ; Embryo, Mammalian/metabolism ; Extracellular Matrix Proteins/genetics ; Extracellular Matrix Proteins/metabolism ; Ion Transport/physiology ; Kidney/cytology ; Kidney/embryology ; Kidney/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Rats ; Sialoglycoproteins/genetics ; Sialoglycoproteins/metabolism
Chemical Substances	Annexin A2 ; Extracellular Matrix Proteins ; Phosphoproteins ; Sialoglycoproteins ; dentin sialophosphoprotein ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2013-03-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M112.389627
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Article ; Online: On the formation and functions of high and very high magnesium calcites in the continuously growing teeth of the echinoderm Lytechinus variegatus: development of crystallinity and protein involvement.

Veis, Arthur / Stock, Stuart R / Alvares, Keith / Lux, Elizabeth

Cells, tissues, organs

2011 Volume 194, Issue 2-4, Page(s) 131–137

Abstract: Sea urchin teeth grow continuously and develop a complex mineralized structure consisting of spatially separate but crystallographically aligned first stage calcitic elements of high Mg content (5-15 mol% mineral). These become cemented together by ... ...

Abstract	Sea urchin teeth grow continuously and develop a complex mineralized structure consisting of spatially separate but crystallographically aligned first stage calcitic elements of high Mg content (5-15 mol% mineral). These become cemented together by epitaxially oriented second stage very high Mg calcite (30-40 mol% mineral). In the tooth plumula, ingressing preodontoblasts create layered cellular syncytia. Mineral deposits develop within membrane-bound compartments between cellular syncytial layers. We seek to understand how this complex tooth architecture is developed, how individual crystalline calcitic elements become crystallographically aligned, and how their Mg composition is regulated. Synchrotron microbeam X-ray scattering was performed on live, freshly dissected teeth. We observed that the initial diffracting crystals lie within independent syncytial spaces in the plumula. These diffraction patterns match those of mature tooth calcite. Thus, the spatially separate crystallites grow with the same crystallographic orientation seen in the mature tooth. Mineral-related proteins from regions with differing Mg contents were isolated, sequenced, and characterized. A tooth cDNA library was constructed, and selected matrix-related proteins were cloned. Antibodies were prepared and used for immunolocaliztion. Matrix-related proteins are acidic, phosphorylated, and associated with the syncytial membranes. Time-of-flight secondary ion mass spectroscopy of various crystal elements shows unique amino acid, Mg, and Ca ion distributions. High and very high Mg calcites differ in Asp content. Matrix-related proteins are phosphorylated. Very high Mg calcite is associated with Asp-rich protein, and it is restricted to the second stage mineral. Thus, the composition at each part of the tooth is related to architecture and function.
MeSH term(s)	Animals ; Calcium Carbonate/metabolism ; Crystallization ; Giant Cells/metabolism ; Lytechinus/cytology ; Lytechinus/growth & development ; Lytechinus/metabolism ; Lytechinus/ultrastructure ; Magnesium/metabolism ; Proteins/metabolism ; Staining and Labeling ; Tolonium Chloride/metabolism ; Tooth/cytology ; Tooth/growth & development ; Tooth/metabolism ; Tooth/ultrastructure
Chemical Substances	Proteins ; Tolonium Chloride (15XUH0X66N) ; Calcium Carbonate (H0G9379FGK) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2011-05-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1468141-9
ISSN	1422-6421 ; 1422-6405
ISSN (online)	1422-6421
ISSN	1422-6405
DOI	10.1159/000324227
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Article ; Online: Echinoderm phosphorylated matrix proteins UTMP16 and UTMP19 have different functions in sea urchin tooth mineralization.

Alvares, Keith / Dixit, Saryu N / Lux, Elizabeth / Veis, Arthur

The Journal of biological chemistry

2009 Volume 284, Issue 38, Page(s) 26149–26160

Abstract: Studies of mineralization of embryonic spicules and of the sea urchin genome have identified several putative mineralization-related proteins. These predicted proteins have not been isolated or confirmed in mature mineralized tissues. Mature Lytechinus ... ...

Abstract	Studies of mineralization of embryonic spicules and of the sea urchin genome have identified several putative mineralization-related proteins. These predicted proteins have not been isolated or confirmed in mature mineralized tissues. Mature Lytechinus variegatus teeth were demineralized with 0.6 N HCl after prior removal of non-mineralized constituents with 4.0 M guanidinium HCl. The HCl-extracted proteins were fractionated on ceramic hydroxyapatite and separated into bound and unbound pools. Gel electrophoresis compared the protein distributions. The differentially present bands were purified and digested with trypsin, and the tryptic peptides were separated by high pressure liquid chromatography. NH2-terminal sequences were determined by Edman degradation and compared with the genomic sequence bank data. Two of the putative mineralization-related proteins were found. Their complete amino acid sequences were cloned from our L. variegatus cDNA library. Apatite-binding UTMP16 was found to be present in two isoforms; both isoforms had a signal sequence, a Ser-Asp-rich extracellular matrix domain, and a transmembrane and cytosolic insertion sequence. UTMP19, although rich in Glu and Thr did not bind to apatite. It had neither signal peptide nor transmembrane domain but did have typical nuclear localization and nuclear exit signal sequences. Both proteins were phosphorylated and good substrates for phosphatase. Immunolocalization studies with anti-UTMP16 show it to concentrate at the syncytial membranes in contact with the mineral. On the basis of our TOF-SIMS analyses of magnesium ion and Asp mapping of the mineral phase composition, we speculate that UTMP16 may be important in establishing the high magnesium columns that fuse the calcite plates together to enhance the mechanical strength of the mineralized tooth.
MeSH term(s)	Amino Acid Sequence ; Animal Structures/embryology ; Animals ; Apatites/metabolism ; Calcification, Physiologic/physiology ; Cloning, Molecular ; Extracellular Matrix Proteins/genetics ; Extracellular Matrix Proteins/metabolism ; Gene Library ; Genome/physiology ; Lytechinus/embryology ; Lytechinus/genetics ; Molecular Sequence Data ; Protein Binding
Chemical Substances	Apatites ; Extracellular Matrix Proteins
Language	English
Publishing date	2009-07-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M109.024018
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Article: Expression and potential role of dentin phosphophoryn (DPP) in mouse embryonic tissues involved in epithelial-mesenchymal interactions and branching morphogenesis.

Alvares, Keith / Kanwar, Yashpal S / Veis, Arthur

Developmental dynamics : an official publication of the American Association of Anatomists

2006 Volume 235, Issue 11, Page(s) 2980–2990

Abstract: Dentin sialophosphoprotein (DSPP) is synthesized in both mesenchyme and epithelium at varying stages of tooth development. At the tooth cap stage, corresponding to embryonic day (E) 13.5 of mouse embryonic life, the phosphophoryn (DPP) portion of DSPP ... ...

Abstract	Dentin sialophosphoprotein (DSPP) is synthesized in both mesenchyme and epithelium at varying stages of tooth development. At the tooth cap stage, corresponding to embryonic day (E) 13.5 of mouse embryonic life, the phosphophoryn (DPP) portion of DSPP was immunohistochemically localized to the enamel organ with intense staining of oral ectoderm but no expression in dental follicle mesenchyme. Surprisingly, DPP was also expressed in ureteric bud branches of embryonic metanephric kidney and alveolar epithelial buds of developing lung. Reverse transcriptase-polymerase chain reaction analysis verified the presence of DSPP mRNA with identical sequences in the tooth, lung, and kidney. The DSPP(-/-) mouse with ablated DPP expression in the teeth, also exhibited aberrant organogenesis in kidney and lung. In the kidney, malformed metanephric S-shaped bodies and increased mesenchymal apoptosis were observed. Inclusion of anti-DPP antibodies in organ culture of metanephroi, harvested from E13.5 wild-type mice, likewise resulted in altered ureteric bud morphogenesis, suggesting a role for DPP in epithelial-mesenchymal interactions in meristic tissues during embryonic development.
MeSH term(s)	Animals ; Antibodies/immunology ; Antibodies/pharmacology ; Embryo, Mammalian/chemistry ; Embryo, Mammalian/metabolism ; Epithelium/chemistry ; Epithelium/embryology ; Epithelium/metabolism ; Extracellular Matrix Proteins ; Immunohistochemistry ; Kidney/chemistry ; Kidney/embryology ; Kidney/metabolism ; Lung/chemistry ; Lung/embryology ; Lung/metabolism ; Mesoderm/chemistry ; Mesoderm/metabolism ; Mice ; Morphogenesis/drug effects ; Phosphoproteins/analysis ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; RNA, Messenger/analysis ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	Antibodies ; Extracellular Matrix Proteins ; Phosphoproteins ; RNA, Messenger ; dentin matrix protein 2 ; phosphophoryn
Language	English
Publishing date	2006-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1102541-4
ISSN	1097-0177 ; 1058-8388
ISSN (online)	1097-0177
ISSN	1058-8388
DOI	10.1002/dvdy.20935
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