Purification, characterization, and biosynthesis of bovine enamelins. Calcif.
Secretory-stage ameloblasts are responsible for many important processes necessary for enamel formation, including: alternative mRNA splicing, translation and secretion of enamel proteins (amelogenin, ameloblastin, enamelin, MMP-20), selective reabsorption and degradation of cleavage products, establishment and regulation of the influx of calcium and phosphate ions, and maintenance of extracellular pH and ionic strength (Simmer & Fincham, 1995; Fincham et al., 1999).
The process of amelogenesis is a complex and regulated by ameloblasts that requires secretion of certain matrix proteins that includes amelogenins, amelins, enamelins
and tuftelins and the previously formed dentine.3 Literature survey revealed that amelogenesis has three phases that are pre- secretory, secretory, and maturation.3
The matrix proteins are a heterogeneous group which are generally separated into amelogenins (major component) and enamelins. Enamelins have been suggested to function as nucleation sites for the hydroxyapatite crystals, while amelogenins are thought to regulate the rate, size and pattern of hydroxyapatite crystal growth.
(10.) Fukae M, Tanabe T, Uchida T, Yamakoshi Y and Shimizu M Enamelins in the newly formed bovine enamel.
Recently a gene encoding a second amleoblast specific protein, Enamelin has been mapped to the AIH2 critical region within 15kb of AMBN.
The enamelin gene, ENAM, has been mapped with different techniques to the same region on chromosome 4q as AIH2 and AMBN, suggesting that this region could contain a cluster of genes encoding enamel proteins.