Linked Life Data

9719031

Source:http://linkedlifedata.com/resource/pubmed/id/9719031

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1998-8-27
pubmed:abstractText
The formation of dental enamel is a precisely regulated and dynamic developmental process. The forming enamel starts as a soft, protein-rich tissue and ends as a hard tissue that is over 95% mineral by weight. Intact amelogenin and its proteolytic cleavage products are the most abundant proteins present within the developing enamel. Proteinases are also present within the enamel matrix and are thought to help regulate enamel development and to expedite the removal of proteins prior to enamel maturation. Recently, a novel matrix metalloproteinase named enamelysin was cloned from the porcine enamel organ. Enamelysin transcripts have previously been observed in the enamel organ and dental papillae of the developing tooth. Here, we show that the sources of the enamelysin transcripts are the ameloblasts of the enamel organ and the odontoblasts of the dental papilla. Furthermore, we show that enamelysin is present within the forming enamel and that it is transported in secretory vesicles prior to its secretion from the ameloblasts. We also characterize the ability of recombinant enamelysin (rMMP-20) to degrade amelogenin under conditions of various pHs and calcium ion concentrations. Enamelysin displayed the greatest activity at neutral pH (7.2) and high calcium ion concentration (10 mM). During the initial stages of enamel formation, the enamel matrix maintains a neutral pH of between 7.0 and 7.4. Thus, enamelysin may play a role in enamel and dentin formation by cleaving proteins that are also present during these initial developmental stages.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-0345
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1580-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9719031-Ameloblasts, pubmed-meshheading:9719031-Amelogenesis, pubmed-meshheading:9719031-Amelogenin, pubmed-meshheading:9719031-Animals, pubmed-meshheading:9719031-Blotting, Western, pubmed-meshheading:9719031-Calcium, pubmed-meshheading:9719031-Dental Enamel Proteins, pubmed-meshheading:9719031-Dental Papilla, pubmed-meshheading:9719031-Dentinogenesis, pubmed-meshheading:9719031-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:9719031-Enamel Organ, pubmed-meshheading:9719031-Hydrogen-Ion Concentration, pubmed-meshheading:9719031-Hydrolysis, pubmed-meshheading:9719031-Immunohistochemistry, pubmed-meshheading:9719031-In Situ Hybridization, pubmed-meshheading:9719031-Matrix Metalloproteinase 20, pubmed-meshheading:9719031-Matrix Metalloproteinases, pubmed-meshheading:9719031-Metalloendopeptidases, pubmed-meshheading:9719031-Mice, pubmed-meshheading:9719031-Odontoblasts, pubmed-meshheading:9719031-RNA, Messenger, pubmed-meshheading:9719031-Recombinant Proteins, pubmed-meshheading:9719031-Swine
pubmed:year
1998
pubmed:articleTitle
Enamelysin (matrix metalloproteinase-20): localization in the developing tooth and effects of pH and calcium on amelogenin hydrolysis.
pubmed:affiliation
Department of Biochemistry, School of Dental Medicine, Tsurumi University, Yokohama, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't