Literature DB >> 12489201

Enamelin compartmentalization in developing porcine enamel.

S J Brookes1, S P Lyngstadaas, C Robinson, R C Shore, S R Wood, J Kirkham.   

Abstract

The tissue compartmentalization of enamelin-processing products has been investigated in developing pig enamel using a sequential extraction procedure. Only trace amounts of enamelin-processing products were detected in simulated enamel fluid extracts, suggesting that enamelins are not solubilized in the matrix to any great extent. Subsequent phosphate buffer extraction desorbed and extracted several enamelin-processing products that were presumably bound to the mineral phase. A 35-kD processing product dominated the phosphate extract, suggesting that enamelin processing leads to an accumulation of this mineral-bound molecule. Dissociative extraction with urea subsequently extracted the remainder of the enamelin-processing products present. This material was presumably present in the tissue in an aggregated insoluble state. Several enamelin-processing products were only extracted by specific extraction procedures, suggesting that different enamelin-processing products are differentially compartmentalized. This may indicate that specific enamelin-processing products have different functions. In contrast to amelogenins, which are processed in the deeper tissue to generate products having a low affinity for the mineral, enamelin processing appears to produce products (those enamelins desorbed by phosphate buffer) that have a high affinity for the mineral. These products, appearing in the deeper enamel layers, may serve to influence crystal growth kinetics in the absence of any mineral-binding amelogenins.

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Year:  2002        PMID: 12489201     DOI: 10.1080/03008200290000862

Source DB:  PubMed          Journal:  Connect Tissue Res        ISSN: 0300-8207            Impact factor:   3.417


  6 in total

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4.  Is the 32-kDa fragment the functional enamelin unit in all species?

Authors:  Steven J Brookes; Nicola J Kingswell; Martin J Barron; Michael J Dixon; Jennifer Kirkham
Journal:  Eur J Oral Sci       Date:  2011-12       Impact factor: 2.612

5.  Amelogenesis imperfecta caused by N-terminal enamelin point mutations in mice and men is driven by endoplasmic reticulum stress.

Authors:  Steven J Brookes; Martin J Barron; Claire E L Smith; James A Poulter; Alan J Mighell; Chris F Inglehearn; Catriona J Brown; Helen Rodd; Jennifer Kirkham; Michael J Dixon
Journal:  Hum Mol Genet       Date:  2017-05-15       Impact factor: 6.150

6.  A mutation in the mouse Amelx tri-tyrosyl domain results in impaired secretion of amelogenin and phenocopies human X-linked amelogenesis imperfecta.

Authors:  Martin J Barron; Steven J Brookes; Jennifer Kirkham; Roger C Shore; Charlotte Hunt; Aleksandr Mironov; Nicola J Kingswell; Joanne Maycock; C Adrian Shuttleworth; Michael J Dixon
Journal:  Hum Mol Genet       Date:  2010-01-12       Impact factor: 6.150

  6 in total

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