Enzyme compartmentalization during biphasic enamel matrix processing.
Connect Tissue Res
; 39(1-3): 89-99; discussion 141-9, 1998.
Article
em En
| MEDLINE
| ID: mdl-11062991
ABSTRACT
Processing of enamel matrix proteins is essentially biphasic. Secretory stage metalloprotease activity generates a discrete, presumably functional, spectrum of molecules which may also undergo dephosphorylation. Maturation stage serine proteases almost completely destroy the matrix. The present aim was to examine the tissue compartmentalization of these enzyme activities in relation to their possible function. A sequential extraction using synthetic enamel fluid, phosphate buffer and SDS was used to identify enzymes free in the enamel fluid, crystal bound or aggregated with the bulk matrix respectively. Results indicated that the metallo-proteases and alkaline phosphatase were free in the secretory stage enamel fluid while the serine proteases appeared to be largely bound to the maturation stage crystals. The mobility of the metallo-proteases and alkaline phosphatase would ensure efficient initial processing of secretory matrix, while the largely mineral bound serine proteases would ensure retention of protease activity despite massive destruction and protein removal.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Metaloendopeptidases
/
Processamento de Proteína Pós-Traducional
/
Proteínas do Esmalte Dentário
Limite:
Animals
Idioma:
En
Revista:
Connect Tissue Res
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Reino Unido