Perinatal protein deprivation impacts nuclear O-GalNAc glycosylation in rat pup cells

GARAY, YOHANA C; GUTIERREZ, MARÍA C; LARDONE, RICARDO D; IRAZOQUI, FERNANDO J; PERONDI, MARÍA C; FERRERO, FRANCO A; CUADRA, GABRIEL R; CEJAS, ROMINA B; PARODI, PEDRO; VALDOMERO, ANALIA

Congreso; Reunión Conjunta SAIB-SAMIGE; 2021

Sociedad Argentina de Investigación Bioquímica y Biología Molecular (SAIB) | Asociación Civil de Microbiología General (SAMIGE)

Post-translational modifications are key factors in the modulation of nuclear protein function controlling cell physiology and individual health. We study the influence of early under-nutrition on the nuclear O-GalNAc glycosylation of rat pup cells. Pregnant rats were fed with well-nourished and protein deprived diets, and after weaning at 30 days, pups were studied. Perinatal protein deficit exerted a direct consequence on offspring development, reducing the progeny weight. In different offspring tissues, we analyzed for the presence in nucleus of all the factors involved in the beginning of O-GalNAc glycan biosynthesis: the substrate donor (UDP-GalNAc), the enzyme activity (ppGalNAc-T) and the glycosylation product (O- GalNAc glycans). Here we observed that UDP-GalNAc levels available in cytoplasm and nucleus were not affected in cells from liver, cerebral cortex, cerebellum and hippocampus. However, perinatal protein deficiency affected the total activity of ppGalNAc-T localized in liver nucleus, thus reducing the ?writing? ppGalNAc-T activity of nuclear O-GalNAc glycans. In addition, liver nucleoplasm of protein-deprived pups reported a significant reduction in expression of nuclear O-GalNAc glycan level. Our results suggest that limited availability of essential amino acids during early life stages (gestation and lactation) can modulate nuclear O-GalNAc glycosylation, which might ultimately regulate nuclear protein functions.