Abstract
Strepsirrhines are members of a primate suborder that has a distinctive set of features associated with the development of the dentition. Amelogenin (AMEL), the better known of the enamel matrix proteins, forms 90% of the secreted organic matrix during amelogenesis. Although AMEL has been sequenced in numerous mammalian lineages, the only reported strepsirrhine AMEL sequences are those of the ring-tailed lemur and galago, which contain a set of additional proline-rich tandem repeats absent in all other primates species analyzed to date, but present in some non-primate mammals. Here, we first determined that these repeats are present in AMEL from three additional lemur species and thus are likely to be widespread throughout this group. To evaluate the functional relevance of these repeats in strepsirrhines, we engineered a mutated murine amelogenin sequence containing a similar proline-rich sequence to that of Lemur catta. In the monomeric form, the MQP insertions had no influence on the secondary structure or refolding properties, whereas in the assembled form, the insertions increased the hydrodynamic radii. We speculate that increased AMEL nanosphere size may influence enamel formation in strepsirrhine primates.
Highlights
Strepsirrhines are members of a suborder of primates that include lorises, galagos, and lemurs
Some differences were noted between the AMELX and AMELY derived lemur amelogenin sequences (Figure 3)
The structural disorder/order in the recombinant mouse and chimeric amelogenin was examined using the mean net charge versus mean hydrophobicity plot that allows the binary classification of proteins [25]
Summary
Strepsirrhines are members of a suborder of primates that include lorises, galagos, and lemurs They are characterized by anatomical features relevant to the dentition, such as the presence of a tooth comb and a distinct dental formula and morphology different to most other primate suborders, tarsiiformes and anthropoidea [1]. Once the tooth follicle has advanced to the bell stage, epithelial cells from the inner enamel epithelium start to elongate and polarize. Soon after, these cells (ameloblasts) express enamel matrix proteins (EMPs) that regulate the development of enamel microstructure by forming an extracellular scaffold that guides mineral growth [6]
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