The role of smooth-ended ameloblasts in enamel protein degradation in the rat incisor pigmentation.
Rats were perfused with glutaraldehyde. The lower incisors were dissected free. Mid-sagittal slice was cut through the entire incisor, demineralized. The pigmentation zone was isolated and further sliced into cross sections. These sections were incubated for CMPase. CMPase reaction product were associated with the lateral cell membrane of subclass II and Subclass III. This localization confirm the role of extracellular space of SAs as a route of enamel proteins during maturation.
Salama
A H
AH
Oral Biology Department, Faculty of Oral and Dental Medicine, Cairo University.
George
A A
AA
Ali
M A
MA
D000565:Ameloblasts / Q000201:enzymology* / Q000648:ultrastructure; D000818:Animals; D015415:Biomarkers; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D003746:Dental Enamel Proteins / Q000378:metabolism*; D007180:Incisor / Q000201:enzymology* / Q000648:ultrastructure; D008247:Lysosomes / Q000201:enzymology / Q000648:ultrastructure; D008854:Microscopy, Electron; D009708:Nucleotidases / Q000378:metabolism; D010858:Pigmentation / Q000502:physiology; D051381:Rats; D017207:Rats, Sprague-Dawley
D015415:Biomarkers; D003746:Dental Enamel Proteins; D009708:Nucleotidases; C025221:cytidine-5'-monophosphatase