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

作者：Romo Arevalo Enrique^*; Arzate Higinio; Montoya Ayala Gonzalo; Rodriguez Romero Adela

来源：FEBS LETTERS, 2016, 590(1): 129-138.

DOI：10.1002/1873-3468.12032

• biomineralization
• cementum protein 1
• C-type lectin-like protein
• hydroxyapatite
• periodontum
• root cementum

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.

• 出版日期2016-1