Posttranslational regulation of glucose-6-phosphate dehydrogenase activity in tongue epithelium.
Expression of glucose-6-phosphate dehydrogenase (G6PD) activity is high in tongue epithelium, but its exact function is still unknown. It may be related either to the high proliferation rate of this tissue or to protection against oxidative stress. To elucidate its exact role, we localized quantitatively G6PD activity, protein and mRNA using image analysis in tongue epithelium of rat and rabbit, two species with different diets. Distribution patterns of G6PD activity were largely similar in rat and rabbit but the activities were twofold lower in rabbit. Activity was two to three times higher in upper cell layers of epithelium than in basal cell layers, whereas basal layers, where proliferation takes place, contained twice as much G6PD protein and 40% more mRNA than upper layers. Our findings show that G6PD is synthetized mainly in basal cell layers of tongue epithelium and that it is posttranslationally activated when cells move to upper layers. Therefore, we conclude that the major function of G6PD activity in tongue epithelium is the formation of NADPH for protection against oxidative stress and that diet affects enzyme expression in this tissue.
Biagiotti
E
E
Academic Medical Center, University of Amsterdam, Department of Cell Biology and Histology, Amsterdam, The Netherlands.
Bosch
K S
KS
Ninfali
P
P
Frederiks
W M
WM
Van Noorden
C J
CJ
D000818:Animals; D005954:Glucosephosphate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D006651:Histocytochemistry; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D008297:Male; D009061:Mouth Mucosa / Q000378:metabolism*; D018809:Proliferating Cell Nuclear Antigen / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D017208:Rats, Wistar; D014059:Tongue / Q000378:metabolism*
D018809:Proliferating Cell Nuclear Antigen; D012333:RNA, Messenger; D005954:Glucosephosphate Dehydrogenase