Heterogeneous distribution of glucose-6-phosphate dehydrogenase in lingual epithelium.
Lingual epithelium undergoes oxidative stress and apoptosis with consequent renewal of superficial keratinized cells by proliferation and differentation of the stem cells of the basal germinative layer. In 3 distinct areas of lingual epithelium of rat and rabbit, the anterior third, central third and posterior third, we determined the activity of hexose monophosphate shunt enzymes and antioxidant enzymes, which are essential for support of cell proliferation and differentation. Enzymatic assays of the epithelium showed that glucose-6-phosphate dehydrogenase (G6PD) activity was highest in the anterior third, whereas activity of glutathione peroxidase, 6-phosphogluconate dehydrogenase, glutathione reductase, superoxide dismutase and catalase was similar over all areas. Histochemical localization of activity and immunohistochemical localization of protein of G6PD showed that all types of papillae had a similar G6PD content; moreover, the presence of different G6PD isoforms in the 3 areas was excluded by electrophoretic analysis. We conclude that the higher G6PD activity in the anterior part of the epithelium is due only to the anatomical organization of the epithelial surface of this area, in which many filiform and fungiform papillae are arranged in a compact manner, which corresponds with a higher number of proliferating and differentiating cells. These processes need products of G6PD activity. This study indicates that G6PD is a good marker for the number of differentiating cells in tongue epithelium.
Ninfali
P
P
Istituto di Chimica Biologica G. Fornaini, University of Urbino, Italy. p.ninfali@bib.uniurb.it
Aluigi
G
G
Capellacci
S
S
Biagiotti
E
E
D000818:Animals; D017209:Apoptosis; D002374:Catalase / Q000096:biosynthesis; D002454:Cell Differentiation; D002455:Cell Division; D003771:Dental Papilla / Q000378:metabolism; D004848:Epithelium / Q000378:metabolism*; D005954:Glucosephosphate Dehydrogenase / Q000096:biosynthesis* / Q000737:chemistry; D005980:Glutathione Reductase / Q000096:biosynthesis; D007150:Immunohistochemistry; D008297:Male; D008953:Models, Anatomic; D018384:Oxidative Stress; D010734:Phosphogluconate Dehydrogenase / Q000096:biosynthesis; D020033:Protein Isoforms; D011817:Rabbits; D051381:Rats; D017207:Rats, Sprague-Dawley; D013053:Spectrophotometry; D013482:Superoxide Dismutase / Q000096:biosynthesis; D014018:Tissue Distribution; D014059:Tongue / Q000378:metabolism*
D020033:Protein Isoforms; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D002374:Catalase; D013482:Superoxide Dismutase; D005980:Glutathione Reductase