Effects of non-collagenous proteins on the formation of apatite in calcium β-glycerophosphate solutions

Doi, Yutaka; Horiguchi, T.; Kim, Seug-Hyo; Moriwaki, Yuji; Wakamatsu, Nobukazu; Adachi, Masanori; Ibaraki, Kyomi; Moriyama, Keiji; Sasaki, Satoshi; Shimokawa, Hitoyata

doi:10.1016/0003-9969(92)90147-z

Cited by 34 publications

(27 citation statements)

References 28 publications

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“…Similarly, dephosphorylation of phosphophoryn reduces or completely abolishes its effects (both positive and negative) on HA formation (Nawrot et al, 1976;Fujisawa et al, 1987;Linde et al, 1989). It has also been shown that modification of carboxylate groups in mollusc shell aspartate-rich proteins with glycine methyl ester caused a reduction in the formation of oriented calcite crystals on polystyrene films (Addadi et al, 1987 (Termine and Conn, 1976;Hay et al, 1979;Termine et al, 1980;Doi et al 1992). The complete primary structure ofphosvitin has not been determined, but the amino acid composition and sequence data available suggest that it is much more similar to phosphophoryn than to the bone phosphoproteins (Taborsky, 1983).…”

Section: De Novo Hydroxyapaftte Formation In Solutionmentioning

confidence: 99%

“…The ACP-to-HA transformation has been reported to be promoted (Nawrot et al, 1976) and inhibited (Termine and Conn, 1976) by phosphophoryn. This protein has also been found to inhibit the de novo formation (Doi et al, 1992) and seeded growth (Termine et al, 1980;Boskey et al, 1990) of HA and the formation of octacalcium phosphate in double-diffusion agar gels (Fujisawa et al, 1987). De novo formation of HA in gelatin gels has been reported to be increased by low concentrations (< 1 ,ug/ml) and inhibited by higher concentrations (> 1 ,tg/ml) of phosphophoryn (Boskey et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

“…The bone proteins osteonectin and osteocalcin have been reported to inhibit the seeded growth (Menanteau et al, 1982;Romberg et al, 1986) and de novo formation (Doi et al, 1992) of HA. Another bone protein found to inhibit seeded growth of HA is albumin, but only at much higher concentrations than those reported for osteocalcin and osteonectin (Garnett and Dieppe, 1990).…”

Section: Introductionmentioning

confidence: 99%

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Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation

Hunter

Kyle

Goldberg

1994

Biochemical Journal

390

331

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Osteopontin is a phosphorylated sialoprotein containing a conserved sequence of contiguous aspartic acid residues. This protein is expressed at high levels in mineralized tissues and has previously been shown to inhibit the in vitro formation of hydroxyapatite (HA). In the present study, protein modification and model compound studies have been used to identify the structural features of osteopontin that are responsible for its crystal-modulating properties. Using metastable calcium phosphate solutions buffered by autotitration, osteopontin caused half-maximal inhibition of HA formation at a concentration (IC50) of 0.06 microgram/ml. The hen egg yolk phosphoprotein phosvitin was a much weaker inhibitor, while dextran sulphate had no effect. The synthetic polypeptide poly(aspartic acid) was almost as effective an inhibitor of HA formation as osteopontin (IC50 0.11 microgram/ml), whereas poly(glutamic acid) was more than a thousand times less potent (IC50 155 micrograms/ml). In a steady-state agarose gel system, much higher polypeptide concentrations were required for inhibition of HA formation, but a similar relative order of inhibitory effectiveness was observed. Treatment of osteopontin with alkaline phosphatase removed 84% of the covalently bound phosphate and reduced its HA-inhibiting activity by more than 40-fold. Treatment with glycine ethyl ester in the presence of carbodi-imide modified 86% of the carboxylate groups in osteopontin and reduced its inhibitory activity by 6-fold. These findings indicate that osteopontin is a potent inhibitor of HA formation. This activity requires phosphate and carboxylate groups, possibly including the conserved sequence of contiguous aspartic acid residues. Osteopontin may act as an inhibitor of phase separation in physiological fluids of high supersaturation.

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Section: De Novo Hydroxyapaftte Formation In Solutionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation

Hunter

Kyle

Goldberg

1994

Biochemical Journal

390

331

View full text Add to dashboard Cite

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“…Alkaline phosphatase (AP), which is found in matrix vesicles and the ossifying mesenchyme of hypertrophic cartilage, is an enzyme that catalyzes the release of inorganic phosphate groups (PO 4 3 À ) from organic phosphoesters via dephosphorylation [26,32,33]. AP was used here to provide controlled release of inorganic phosphate groups from a commercial organophosphate ester, rac-glycerol 1-phosphate.…”

Section: Introductionmentioning

confidence: 99%

Biomimetic mineralization of collagen via an enzyme-aided PILP process

Jee

Culver

et al. 2010

Journal of Crystal Growth

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“…Já a osteocalcina é encontrada mais tardiamente no processo de diferenciação celular, sendo importante na progressão da mineralização (2) e no controle da formação dos cristais de hidroxiapatita (3).…”

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Efeito da triiodotironina na expressão das proteínas ósseas durante a diferenciação osteogênica de células-tronco mesenquimais

Hell

Boeloni

Ocarino

et al. 2011

Arq Bras Endocrinol Metab

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RESUMOObjetivo: O objetivo deste estudo foi avaliar o efeito da T3 na expressão da osteocalcina, osteo pontina e colágeno I durante a diferenciação osteogênica das célulastronco mesenquimais (CTM). Materiais e métodos: As células da medula óssea de ratas Wistar jovens foram extraí das, cultivadas e separadas em cinco grupos: controle (indiferenciado), diferenciado (estímulo osteogênico) e diferenciado com T3 (10 3 nM, 10 2 nM e 100 nM). Para cada grupo, foram culti vadas quatro amostras que foram analisadas por RTPCR tempo real aos 7, 14 e 21 dias, para quantificação dos transcritos gênicos para osteocalcina, osteopontina e colágeno I. Resultados: Todos os grupos diferenciados sem T3 ou com T3 independentemente da concentração apre sentaram expressão de colágeno I significativamente menor e expressão de osteocalcina e os teopontina significativamente maior em comparação a das CTM indiferenciadas. Mas o grupo T3 100 nM apresentou concentração de osteocalcina mais elevada e semelhante à da cultura de osteoblastos. Conclusão: Concluise que a triiodotironina não altera a expressão de osteoponti na e de colágeno pelas CTM, mas aumenta a expressão da osteocalcina durante a diferenciação osteogênica in vitro, sendo esse efeito dosedependente. Arq Bras Endocrinol Metab. 2011;55(5):339-44 Descritores Célula-tronco; diferenciação osteogênica; triiodotironina; proteínas ósseas ABSTRACT Objective: The aim of this study was to evaluate the effect of T3 on the expression of osteocal cin, osteopontin and collagen I during osteogenic differentiation of mesenchymal stem cells (MSC). Materials and methods: The bone marrow cells of Wistar rats with 30 days of age were extracted, cultured and separated into five groups: control (undifferentiated), differentiated (os teogenic stimulus) and differentiated with T3 (10 3 nM, 10 2 nM and 100 nM). For each group, four samples were cultured and were analyzed by real time RTPCR at 7, 14 and 21 days for quantification of gene transcripts for osteocalcin, osteopontin and collagen I. Results: All the different groups without T3 or with T3 regardless of the concentration, showed the collagen I expression significantly lower expression, and osteocalcin and osteopontin expression signi ficantly greater than that of undifferentiated MSC. Nevertheless, the group T3 100 nM showed higher expression of osteocalcin and a similar expression of the osteoblast culture. Conclusion: In conclusion, the triiodothyronine does not affect the expression of osteopontin and collagen I, but increases ostecalcin expression during osteogenic differentiation in vitro of the MSC, and this effect is dosedependent. Arq Bras Endocrinol Metab. 2011;55(5):339-44

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Effects of non-collagenous proteins on the formation of apatite in calcium β-glycerophosphate solutions

Cited by 34 publications

References 28 publications

Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation

Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation

Biomimetic mineralization of collagen via an enzyme-aided PILP process

Efeito da triiodotironina na expressão das proteínas ósseas durante a diferenciação osteogênica de células-tronco mesenquimais

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