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In Vitro Effects of Cementum Protein 1 (CEMP1) on Calcium Phosphate Crystal Formation and its Role During the Mineralization Process

Published online by Cambridge University Press:  31 January 2011

Enrique Romo-Arévalo ,
Eduardo Villarreal-Ramírez ,
Juan L. Chávez-Pacheco ,
Cristina Piña-Barba ,
M. Aguilar-Franco  and
Higinio Arzate
Enrique Romo-Arévalo
Affiliation:
Laboratorio de Biología de Periodontal y Tejidos Mineralizados, Facultad de Odontología, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510
Eduardo Villarreal-Ramírez
Affiliation:
Laboratorio de Biología de Periodontal y Tejidos Mineralizados, Facultad de Odontología, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510
Juan L. Chávez-Pacheco
Affiliation:
Laboratorio de Biología de Periodontal y Tejidos Mineralizados, Facultad de Odontología, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510
Cristina Piña-Barba
Affiliation:
Instituto de Investigación en Materiales, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510.
M. Aguilar-Franco
Affiliation:
Instituto de Física, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510.
Higinio Arzate
Affiliation:
Laboratorio de Biología de Periodontal y Tejidos Mineralizados, Facultad de Odontología, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510
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Abstract

Cementum contains specific molecules that could serve to identify, isolate and characterize the cementoblast lineage and to determine the cellular and molecular mechanisms that regulate the cementogenesis process, since it plays a key role during the periodontal regeneration process. One of these molecules is the human cementum protein 1 (CEMP1); which has a molecular weight of 25,9 kDa. In vitro experiments have shown that CEMP1 promotes cellular adhesion and differentiation. In addition, this protein has been implied in regulating the degree of deposition, composition and morphology of hydroxyapatite crystals formed by putative cementoblast in vitro. Therefore, it is possible that CEMP1 promotes the formation, growth and regulates the morphology of hydroxyapatite crystals in vitro. We have produced a human recombinant CEMP1 (hrCEMP1) in a prokaryotic system. The hrCEMP1 purification was realized using the column NiTA HisPrep FF/16. Assays of calcium phosphate crystal growth were realized by means of capillary counterdiffusion system. Our results demonstrated that hrCEMP1 promotes octacalcium phosphate crystal nucleation and possesses high affinity for hydroxyapatite. We infer that hrCEMP1 plays a key role during the regeneration of mineralized tissues.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1244: Symposium 9 – Biomaterials , 2009 , 5
Copyright
Copyright © Materials Research Society 2009

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References

REFERENCES

[1] Bosshardt, D.D., Zalzal, S., McKee, M.D., Nanci, A., Anat. Rec 250, 13 (1998)Google Scholar
[2] Alvarez-Perez, M.A., Narayanan, S., Zeichner-David, M., Carmona-Rodríguez, B., Arzate, H., Bone 38, 409 (2006).Google Scholar
[3] Narayanan, A.S., Page, R.C., J. Biol. Chem. 251, 5464 (1976).Google Scholar
[4] Zeichner-David, M., Oishi, K., González, E., Su, Z., Zakartchenko, V., Chen, L.S., Arzate, H., Bringas, P., Dev. Dyn 228, 651 (2003).Google Scholar
[5] Arzate, H., Jiménez-García, L.F., Alvarez-Pérez, M.A., Landa, A., Bar-Kana, I., Pitaru, S., J. Dent. Res 81, 541 (2002).Google Scholar
[6] Arzate, H., Chimal-Monroy, J., Hernández-Lagunas, L., Díaz de León, L., J. Periodont. Res. 31, 144 (1996).Google Scholar
[7] Alvarez Pérez, M.A., Pitaru, S., AlvarezFregoso, O., Reyes Gasga, J., Arzate, H., J. Struct. Biol 143, 1 (2003).Google Scholar
[8] Carmona-Rodríguez, B., Alvarez-Pérez, M. A., Narayanan, A. S., Zeichner-David, M., Reyes-Gasga, J., Molina-Guarneros, J., García-Hernández, A., Suárez-Franco, J., Gil Chavarría, I., Villarreal-Ramírez, E., Arzate, H., Biochem. Biophys. Res. Comm. 358, 763 (2007).Google Scholar
[9] Silverman, L., Boskey, A.L., Calcif Tissue Int. 75, 494 (2004).Google Scholar
[10] Tye, C.E., Rattray, K.R., Warner, K.J., Gordon, J.A.R., Sodek, J., Hunter, G.K., Goldberg, H.A., J. Biol Chem. 278, 7949 (2003).Google Scholar
[11] Garcia-Ruiz, J.M., Methods Enzymol. 368, 130 (2003).Google Scholar
[12] Kuivaniemi, H., Tromp, G, Prockop, DJ. Hum Mutat 9, 300 (1997).Google Scholar
[13] Shen G., G, Orthod Craniofac Res 8, 11 (2005).Google Scholar
[14] Hjerten, S., Levin, O., Tiselius, A., Arch. Biochem. Biophys 65, 132 (1956)‥Google Scholar