OBJECTIVE: Small integrin-binding ligand N-linked glycoproteins (SIBLINGs) are expressed in dentin and believed to control dentinogenesis. Five members of SIBLING family include bone sialoprotein (BSP), osteopontin (OPN), matrix extracellular phosphoglycoprotein (MEPE), dentin matrix protein 1 (DMP1) and dentin sialophosphoprotein (DSPP). These genes are clustered on chromosome 4q in humans and share similar biological features. DSPP and DMP1 are processed into given structural/functional fragments in rat and porcine. It still remains unclear whether these evidences occur in mouse and other SIBLING members are also processed into given fragments from their parent precursors. The aim of this study was to identify expression and processing of the five proteins in two mouse odontoblastic cell lines. DESIGN: Two mouse odontoblastic cells were used to study expression and processing of the five SIBLING proteins by immunohistochemistry and Western blot analyses. RESULTS: Immunohistochemistry study showed that all of the five SIBLING members were expressed within the cytoplasm and cellular processes in the mouse odontoblastic cell lines. Expression levels of DMP1 and DSPP were higher in differentiated mouse odontoblasts than undifferentiated mouse odontoblasts. Immunolabelling signal of DSP and MEPE was also detected within the nucleus in the two cell lines. Western blot assay indicated that all five members were processed into at least two fragments in these cells. CONCLUSIONS: These results suggest that different processed products and expression levels of the SIBLING proteins may play distinct biological functions in tooth development and mineralisation.
OBJECTIVE: Small integrin-binding ligand N-linked glycoproteins (SIBLINGs) are expressed in dentin and believed to control dentinogenesis. Five members of SIBLING family include bone sialoprotein (BSP), osteopontin (OPN), matrix extracellular phosphoglycoprotein (MEPE), dentin matrix protein 1 (DMP1) and dentin sialophosphoprotein (DSPP). These genes are clustered on chromosome 4q in humans and share similar biological features. DSPP and DMP1 are processed into given structural/functional fragments in rat and porcine. It still remains unclear whether these evidences occur in mouse and other SIBLING members are also processed into given fragments from their parent precursors. The aim of this study was to identify expression and processing of the five proteins in two mouse odontoblastic cell lines. DESIGN: Two mouse odontoblastic cells were used to study expression and processing of the five SIBLING proteins by immunohistochemistry and Western blot analyses. RESULTS: Immunohistochemistry study showed that all of the five SIBLING members were expressed within the cytoplasm and cellular processes in the mouse odontoblastic cell lines. Expression levels of DMP1 and DSPP were higher in differentiated mouse odontoblasts than undifferentiated mouse odontoblasts. Immunolabelling signal of DSP and MEPE was also detected within the nucleus in the two cell lines. Western blot assay indicated that all five members were processed into at least two fragments in these cells. CONCLUSIONS: These results suggest that different processed products and expression levels of the SIBLING proteins may play distinct biological functions in tooth development and mineralisation.
Authors: Michael L Paine; Wen Luo; Hong-Jun Wang; Pablo Bringas; Amanda Y W Ngan; Vetea G Miklus; Dan-Hong Zhu; Mary MacDougall; Shane N White; Malcolm L Snead Journal: J Biol Chem Date: 2005-07-13 Impact factor: 5.157
Authors: Bettina Lorenz-Depiereux; Murat Bastepe; Anna Benet-Pagès; Mustapha Amyere; Janine Wagenstaller; Ursula Müller-Barth; Klaus Badenhoop; Stephanie M Kaiser; Roger S Rittmaster; Alan H Shlossberg; José L Olivares; César Loris; Feliciano J Ramos; Francis Glorieux; Miikka Vikkula; Harald Jüppner; Tim M Strom Journal: Nat Genet Date: 2006-10-08 Impact factor: 38.330
Authors: C Mesgouez; M Oboeuf; N Mauro; P Colon; M MacDougall; P Machtou; J M Sautier; A Berdal Journal: Int Endod J Date: 2006-06 Impact factor: 5.264