IN VITRO EFFECTS OF CEMENTUM PROTEIN 1 (CEMP1) ON CALCIUM PHOSPHATE CRYSTAL FORMATION AND ITS ROLE DURING THE MINERALIZA
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IN VITRO EFFECTS OF CEMENTUM PROTEIN 1 (CEMP1) ON CALCIUM PHOSPHATE CRYSTAL FORMATION AND ITS ROLE DURING THE MINERALIZATION PROCESS. Enrique Romo-Arévalo1, Eduardo Villarreal-Ramírez1, Juan L. Chávez-Pacheco1, Cristina PiñaBarba2, M. Aguilar-Franco3 and Higinio Arzate1 1 Laboratorio de Biología de Periodontal y Tejidos Mineralizados, Facultad de Odontología, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510 2 Instituto de Investigación en Materiales, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510. 3 Instituto de Física, Universidad Nacional Autónoma de México, Coyoacán, México D.F., 04510.
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. INTRODUCTION Cementum is a thin mineralized connective tissue that facilitates the attachment of the periodontal ligament (PDL) to the tooth. The composition and structural features of cementum resembles bone. However, cementum is avascular, lacks innervation and does not undergo remodeling under normal conditions. The biological processes that regulate cementogenesis and normal cementum metabolism remain unclear to date. Recent evidence indicates that cementum formation is critical for appropriate maturation of the periodontium [1]. Recently we have isolated and characterized a human cementum protein which we named Cementum Protein 1 (CEMP1), (GenBank Accession No. NP_001041677; HGNC: ID 32553) [2]. This gene product
is expressed on the cementoid layer, cementoblastic cell layer, by cementocytes and progenitor cells located near the blood vessels in the periodontal ligament, [2,3,4,5]. This protein promotes cell attachment and cell differentiation [6,7]. Additionally, CEMP1 seems to regulate the deposition rate, composition, and morphology of hydroxyapatite crystals formed by human cementoblast cells [7]. Since CEMP1 is synt
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