M A Torres-Quintana

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Post-translational modification of enamel proteins is regulated by casein kinases (CK) and results in binding sites for calcium ions that subsequently play a key role during the initial stages of mineralization. Phosphorylation may also influence the secretion and extracellular organization of enamel proteins. Previous studies indicated that inositol(More)
Immunohistochemical studies using a polyclonal antibody, raised against the recombinant form of dentin matrix protein 1 (DMP1), show that DMP1 was detected mainly in odontoblasts in cultured mouse embryonic tooth germs. However, in restricted areas, DMP1 staining was also observed in secretory ameloblasts, in the stratum intermedium and stellate reticulum,(More)
To study the effects of impaired protein phosphorylation on dentine formation and mineralization, inositol hexasulphate, an intracellular type I and type II casein kinase inhibitor, was used in an in vitro organotypic culture system. Mandibular first molar tooth germs were dissected from 18-day-old mouse embryos and cultured for 11 days with and without(More)
Lanthanum nitrate was either perfused intravascularly or segments of mouse tooth were immersed in a fixative solution containing the tracer. The tracer deposits were examined in young (8-day-old) and older (8-week-old) mouse incisors and molars, demineralized or undemineralized. Lanthanum passed the distal junctional complex of odontoblasts and appeared in(More)
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