The role of acidic phosphoproteins in biomineralization

Alvares, Keith

doi:10.3109/03008207.2013.867336

Cited by 33 publications

(24 citation statements)

References 64 publications

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“…Sequences of repeating DS and DSS residues seem to have a special susceptibility to phosphorylation in other proteins involved in biomineralization (24,27). An example of a protein containing such a motif is dentin phosphoprotein (DPP) (phosphophoryn), which is produced after digestion of dentin sialophosphoprotein, a functional analog of Stm.…”

Section: Discussionmentioning

confidence: 99%

“…Similar DS-rich regions are found in members of the small integrin-binding ligand N-linked glycoprotein family of proteins [known to be involved in bone and dentin formation (22)(23)(24)] and in biomineralization proteins of calcium carbonate shells [Aspein or Asprich (25,26)]. D residues are often responsible for the acidic nature of biomineralization proteins and affects binding of calcium ions, whereas S residues are frequently phosphorylated (27). Phosphorylation in these characteristic regions has been shown to influence calcium-binding ability and biomineralization activity (28).…”

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confidence: 82%

“…In particular, it has been shown that phosphorylation of Stm with casein kinase 2 (CK2) enhances its in vitro biomineralization activity and calcium-binding capacity (18,19). Proteins involved in biomineralization are frequently post-translationally modified, and phosphorylation is one of the most common modifications (27,29). In vivo phosphorylation of Stm, although highly probable, has not yet been studied.…”

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confidence: 99%

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In vivoandin vitroanalysis of starmaker activity in zebrafish otolith biomineralization

et al. 2019

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Otoliths are one of the biominerals whose formation is highly controlled by proteins. The first protein discovered to be involved in otolith biomineralization in zebrafish was starmaker (Stm). Previously, Stm was shown to be responsible for the preferential formation of aragonite, a polymorph of calcium carbonate, in otoliths. In this work, proteomic analysis of adult zebrafish otoliths was performed. Stm is the only highly phosphorylated protein found in our studies. Besides previously studied otolith proteins, we discovered several dozens of unknown proteins that reveal the likely mechanism of biomineralization. A comparison of aragonite and vaterite otoliths showed similarities in protein composition. We observed the presence of Stm in both types of otoliths. In vitro studies of 2 characteristic Stm fragments indicated that the DS‐rich region has a special biomineralization activity, especially after phosphorylation.—Kalka, M., Markiewicz, N., Ptak, M., Sone, E. D., Ożyhar, A., Dobryszycki, P., Wojtas, M. In vivo and in vitro analysis of starmaker activity in zebrafish otolith biomineralization. FASEB J. 33, 6877–6886 (2019). http://www.fasebj.org

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Section: Discussionmentioning

confidence: 99%

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confidence: 82%

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confidence: 99%

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In vivoandin vitroanalysis of starmaker activity in zebrafish otolith biomineralization

et al. 2019

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“…The genes encode osteopontin (OPN), dentin matrix protein-1 (DMP1), matrix extracellular phosphoglycoprotein (MEPE), bone sialoprotein (BSP), and dentin sialophosphoprotein (DSPP). The SIBLINGs comprise a subfamily of the secretory calcium-binding phosphoproteins (SCPP) that regulate tooth and bone formation [32, 33]. Analysis of secreted phosphoproteomes suggest that Fam20C may not be restricted to the phosphorylation of proteins involved in calcium binding because more than two-thirds of human serum [34], plasma [35] and cerebrospinal fluid [36] phosphoproteins contain phosphate within the S-x-E/pS motif.…”

Section: Fam20cmentioning

confidence: 99%

The secretory pathway kinases

Sreelatha

Kinch

Tagliabracci³

2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Protein phosphorylation is a nearly universal post-translation modification involved in a plethora of cellular events. Even though phosphorylation of extracellular proteins had been observed, the identity of the kinases that phosphorylate secreted proteins remained a mystery until recently. Advances in genome sequencing and genetic studies have paved the way for the discovery of a new class of kinases that localize within the endoplasmic reticulum, Golgi apparatus and the extracellular space. These novel kinases phosphorylate proteins and proteoglycans in the secretory pathway and appear to regulate various extracellular processes. Mutations in these kinases cause human disease, thus underscoring the biological importance of phosphorylation within the secretory pathway.

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“…Calcitic mineralization of the sea urchin tooth begins on the syncytial membranes. The mineral then grows into the syncytial spaces (Alvares et al, , Alvares, ).…”

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confidence: 99%

Expression of the invertebrate sea urchin P16 protein into mammalian MC3T3 osteoblasts transforms and reprograms them into “osteocyte‐like” cells

et al. 2015

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P16 is an acidic phosphoprotein important in both sea urchin embryonic spicule development and transient mineralization during embryogenesis, and 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.

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The role of acidic phosphoproteins in biomineralization

Cited by 33 publications

References 64 publications

In vivoandin vitroanalysis of starmaker activity in zebrafish otolith biomineralization

In vivoandin vitroanalysis of starmaker activity in zebrafish otolith biomineralization

The secretory pathway kinases

Expression of the invertebrate sea urchin P16 protein into mammalian MC3T3 osteoblasts transforms and reprograms them into “osteocyte‐like” cells

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