Characterization of recombinant human cementum protein 1 (hrCEMP1): primary role in biomineralization.
Cementum protein 1 (CEMP1) has been recently cloned, and in vitro experiments have shown functions as regulator of cementoblast behavior and inducer of differentiation of non-osteogenic cells toward a cementoblastic/osteoblastic phenotype. In this study, we have produced a full-length human recombinant CEMP1 protein in a human gingival fibroblast cell line. The purified protein (hrCEMP1) has a M(r) 50,000. Characterization of hrCEMP1 indicates that its secondary structure is mainly composed of beta-sheet (55%), where random coil and alpha helix conformations correspond to 35% and 10%, respectively. It was found that hrCEMP1 is N-glycosylated, phosphorylated and possesses strong affinity for hydroxyapatite. Even more important, our results show that hrCEMP1 plays a role during the biomineralization process by promoting octacalcium phosphate (OCP) crystal nucleation. These features make CEMP1 a very good candidate for biotechnological applications in order to achieve cementum and/or bone regeneration.
Villarreal-Ramírez
Eduardo
E
Laboratorio de Biología Periodontal y Tejidos Mineralizados, Facultad de Odontología, UNAM, México DF, Mexico.
Moreno
Abel
A
Mas-Oliva
Jaime
J
Chávez-Pacheco
Juan Luis
JL
Narayanan
A Sampath
AS
Gil-Chavarría
Ivet
I
Zeichner-David
Margarita
M
Arzate
Higinio
H
D002113:Calcification, Physiologic; D017886:Durapatite / Q000737:chemistry; D005347:Fibroblasts / Q000378:metabolism; D005881:Gingiva / Q000166:cytology / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics
C510886:CEMP1 protein, human; D011506:Proteins; D011994:Recombinant Proteins; D017886:Durapatite