Dipeptidyl-peptidase II and cathepsin B activities in amelogenesis of the rat incisor

Smid, JR, Young, WG and Monsour, PA (2001) Dipeptidyl-peptidase II and cathepsin B activities in amelogenesis of the rat incisor. European Journal of Oral Sciences, 109 4: 260-266. doi:10.1034/j.1600-0722.2001.00025.x


Author Smid, JR
Young, WG
Monsour, PA
Title Dipeptidyl-peptidase II and cathepsin B activities in amelogenesis of the rat incisor
Journal name European Journal of Oral Sciences   Check publisher's open access policy
ISSN 0909-8836
Publication date 2001
Sub-type Article (original research)
DOI 10.1034/j.1600-0722.2001.00025.x
Volume 109
Issue 4
Start page 260
End page 266
Total pages 7
Editor Anders Linde
Place of publication Denmark
Publisher Munksgaard Int Publishers Ltd
Collection year 2001
Language eng
Subject C1
320899 Dentistry not elsewhere classified
730112 Oro-dental and disorders
Abstract A body of published evidence suggests that a significant portion of enamel matrix protein synthesized by ameloblasts localises in the lysosomal-endosomal organelles of these enamel organ cells. Little is known regarding the lysosomal proteolytic activities during amelogenesis. The aims of this study were to detect and measure the activities of lysosomal peptidases cathepsin B (E.C. 3.4.22.1) and dipeptidyl-peptidase II (E.C. 3.4.14.2) in the enamel organ of the rat incisor and to ascertain whether rat enamel matrix proteins are degraded by these peptidases in vitro. Whole enamel organs were dissected from rat mandibular incisors. Enamel protein was also collected from the rat teeth. Analysis indicated that the rat incisor enamel organs contained specific activities of both dipeptidyl-peptidase II and cathepsin B at levels comparable with those of kidney which is rich in both these lysosomal peptidases. Gel electrophoresis and immunoblotting demonstrated that both cathepsin B and dipeptidyl-peptidase II were able to substantially degrade the rat enamel proteins in vitro. Based on these observations, we propose that lysosomal proteases have roles in amelogenesis in the intracellular degradation of amelogenins.
Keyword Dentistry, Oral Surgery & Medicine
Cathepsin B
Dipeptidyl-peptidases
Enamel Organ
Incisor
Sodium-fluoride
Enamel Proteins
Ameloblasts
Degradation
Lysosomes
Secretion
Pathways
Tissues
Suramin
Serum
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Dentistry Publications
 
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Created: Tue, 14 Aug 2007, 15:19:12 EST