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

FEBS Letters
Enrique Romo-ArévaloAdela Rodríguez-Romero

Abstract

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.

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Citations

Aug 17, 2018·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Rodrigo CorreaHiginio Arzate
Aug 15, 2019·Journal of Peptide Science : an Official Publication of the European Peptide Society·Gonzalo MontoyaHiginio Arzate

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