High-level expression and characterization of a glycosylated human cementum protein 1 with lectin activity.

Autor: Romo-Arévalo E; Facultad de Odontología, Laboratorio de Biología Periodontal, Universidad Nacional Autónoma de México, Mexico City, Mexico., Arzate H; Facultad de Odontología, Laboratorio de Biología Periodontal, Universidad Nacional Autónoma de México, Mexico City, Mexico., Montoya-Ayala G; Facultad de Odontología, Laboratorio de Biología Periodontal, Universidad Nacional Autónoma de México, Mexico City, Mexico., Rodríguez-Romero A; Instituto de Química, Universidad Nacional Autónoma de México, Mexico City, Mexico.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2016 Jan; Vol. 590 (1), pp. 129-38. Date of Electronic Publication: 2016 Jan 11.
DOI: 10.1002/1873-3468.12032
Abstrakt: This work aims to contribute to the knowledge of human cementum protein 1 (CEMP1), its conformational characteristics and influence during the biomineralization process. The results revealed that hrCEMP1 expressed in Pichia pastoris is a 2.4% glycosylated, thermostable protein which possesses a molecular mass of 28,770 Da. The circular dichroism spectrum indicated a secondary structure content of 28.6% of alpha-helix, 9.9% of beta-sheet and 61.5% of random-coil forms. Biological activity assays demonstrated that hrCEMP1 nucleates and regulates hydroxyapatite crystal growth. Hereby, it is demonstrated for the first time that CEMP1 has a (C-type) lectin-like activity and specifically recognizes mannopyranoside. The information produced by this biochemical and structural characterization may contribute to understand more fully the biological functions of CEMP1.
(© 2015 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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