Quantitative cytochemistry of lysosomal structures in rat incisor maturation enamel organ.
Trimetaphosphatase was used as a lysosomal marker in the ruffle-ended maturation ameloblasts and associated papillary cells. Morphometric analysis was carried out of the percentage area of these cells (density) occupied by the various enzyme-reactive lysosomal structures. The density of total TMPase-positive lysosomal structures, tubular lysosomes and multivesicular bodies in ruffle-ended ameloblasts were all significantly greater (p less than or equal to 0.05) in early than in late maturation enamel formation. In papillary cells the same was true of tubular lysosomes, whereas the greater density of enzyme-positive total structures in early maturation was not statistically significant when compared to late maturation. These findings demonstrate a corresponding pattern between enamel-organ lysosomal activity and the period of early enamel maturation when most enamel protein is lost. They support the likely involvement by ruffle-ended ameloblasts and papillary cells in absorption and degradation of exogenous enamel proteins.
Salama
A H
AH
Department of Oral Biology, Faculty of Oral and Dental Medicine, Cairo University, Orman, Ghiza, Egypt.
Bailey
R L
RL
Eisenmann
D R
DR
Zaki
A E
AE
D017766:Acid Anhydride Hydrolases; D000565:Ameloblasts / Q000166:cytology; D000566:Amelogenesis; D000818:Animals; D004658:Enamel Organ / Q000166:cytology*; D006651:Histocytochemistry; D007180:Incisor; D008247:Lysosomes / Q000201:enzymology / Q000648:ultrastructure*; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis; D051381:Rats; D011919:Rats, Inbred Strains
D010744:Phosphoric Monoester Hydrolases; D017766:Acid Anhydride Hydrolases; C022768:trimetaphosphatase