Fate of annular gap junctions in the papillary cells of the enamel organ in the rat incisor.
To investigate the mechanisms whereby annular gap junctions in the papillary cells of the enamel organ are degraded intracellularly, continuously growing rat incisors were examined by electron microscopy of routine thin sections as well as for the cytochemical localization of inorganic trimetaphosphatase activity. Routine thin-section analysis revealed small flat or undulated gap junctions, hemi-annular gap junctions between an invaginated cell process and a cell body, and fully internalized cytoplasmic annular gap junctions. Both hemi-annular and annular gap junctions usually contain various organelles and/or inclusions, such as mitochondria, endoplasmic reticulum, ribosomes, vesicles, and lysosomes in the cytoplasm confined by the junctional membranes. Annular gap junctions are sometimes fused with vesicular or tubulovesicular structures. Cytochemistry of inorganic trimetaphosphatase activity revealed an intense enzymatic reaction within a system of tubular structures and round or oval dense bodies. Both structures are believed to correspond to primary lysosomes. A part of the Golgi apparatus also shows a weak reaction. Although hemi-annular gap junctions never show enzymatic reaction, annular gap junctions sometimes contain reaction products throughout their interior cytoplasm and inclusions. Fusion of annular gap-junctional membranes with reaction-positive tubular structures is also observed. In one instance, revealed in serial sections, an annular gap junction was encircled entirely by a reaction-positive structure. These results suggest that cytoplasmic annular gap junctions are formed by endocytosis of hemi-annular gap junctional membranes from the cell surface and then degraded intracellularly by lysosomal enzymes.
D017766:Acid Anhydride Hydrolases; D000818:Animals; D003593:Cytoplasm / Q000648:ultrastructure; D004658:Enamel Organ / Q000201:enzymology / Q000648:ultrastructure*; D006651:Histocytochemistry; D007180:Incisor / Q000648:ultrastructure*; D007365:Intercellular Junctions / Q000648:ultrastructure*; D008247:Lysosomes / Q000648:ultrastructure; D008854:Microscopy, Electron; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D014083:Tooth Germ / Q000648:ultrastructure*
D010744:Phosphoric Monoester Hydrolases; D017766:Acid Anhydride Hydrolases; C022768:trimetaphosphatase