Abstract Aim: It has been suggested that the decline in menarcheal age is associated with the increase of obesity prevalence. Objective: To examine the association between age at menarche and adiposity development from age 7 to 15 years. Subjects: A cohort of 109 schoolgirls from Viana do Castelo (Northern Portugal). Methods: Anthropometric measurements (height, weight, and triceps and subscapular skinfold thicknesses) were longitudinally obtained at 7, 8, 9, and 15 years. Waist circumference and self-reported age at menarche were obtained at age 15. Obesity was defined by the cut-off value of 30% body fat. Ages of 13 years were classified as early menarche (EM), average menarche (AM) and late menarche (LM), respectively. Results: Median menarcheal age was 12.0 years (range, 8–15 years), with 26.6% of girls classified as EM. Compared with their LM peers, EM girls were always fatter (p=0.001) and had higher waist circumference at age 15 (p=0.009). All variables showed significant negative associations with age at menarche, except subscapular to triceps skinfold ratio at all ages and height at age 15. At both ages 9 and 15 years, LM girls had the lowest prevalence of obesity (4.5% and 9.1%, respectively). The 8-year incidence of obesity in EM girls was 24.1%, while that in the AM plus LM group was 13.8% (p=0.005). Conclusion: EM seems to be a risk factor for the development of obesity during adolescence. However, this vulnerability may start to be programmed before menarche as girls with precocious menarche were already fatter than their late-maturing peers at age 7 years.

Candida albicansaccumulates large amounts of the polyols glycerol andd-arabitol when the cells are exposed to physiological conditions relevant to stress and virulence in animals. Intracellular concentrations of glycerol are determined by rates of glycerol production and catabolism and of glycerol uptake and efflux through the plasma membrane. We and others have studied glycerol production inC. albicans, but glycerol uptake byC. albicanshas not been studied. In the present study, we found that [14C]glycerol uptake byC. albicansSC5314 was (i) accumulative; (ii) dependent on proton-motive force; (iii) unaffected by carbon source; and (iv) unaffected by large molar excesses ofd-arabitol or other polyols. The respectiveKmandVmaxvalues were 2.1 mM and 460 μmol h−1(g dry wt)−1in glucose medium and 2.6 mM and 268 μmol h−1(g dry wt)−1in glycerol medium. To identify theC. albicansglycerol uptake protein(s), we cloned theC. albicanshomologues of theSaccharomyces cerevisiaegenesGUP1andSTL1, both of which are known to be involved in glycerol transport. When multicopy plasmids encodingC. albicans STL1,C. albicans STL2andC. albicans GUP1were introduced into the correspondingS. cerevisiaenull mutants, the transformants all acquired the ability to grow on minimal glycerol medium; however, onlyS. cerevisiae stl1null mutants transformed withC. albicans STL1actively took up extracellular [14C]glycerol. When both chromosomal alleles ofC. albicans STL1were deleted fromC. albicansBWP17, the resultingstl1null mutants grew poorly on minimal glycerol medium, and their ability to transport [14C]glycerol into the cell was markedly reduced. In contrast, deletion of both chromosomal alleles ofC. albicans STL2or ofC. albicans GUP1had no significant effects on [14C]glycerol uptake or the ability to grow on minimal glycerol medium. Northern blot analysis indicated thatC. albicans STL1was expressed in both glucose and glycerol media, conditions under which we detected wild-type active glycerol uptake. Furthermore,STL1was highly expressed in salt-stressed cells; however, thestl1null mutant was no more sensitive to salt stress than wild-type controls. We also detected high levels ofSTL2expression in glycerol-grown cells, even though deletion of this gene did not influence glycerol uptake activity in glycerol-grown cells. We conclude from the results above that a plasma-membrane H+symporter encoded byC. albicans STL1actively transports glycerol intoC. albicanscells.

Glycerol and other polyols are used as osmoprotectants by many organisms. Several yeasts and other fungi can take up glycerol by proton symport. To identify genes involved in active glycerol uptake in Saccharomyces cerevisiae we screened a deletion mutant collection comprising 321 genes encoding proteins with 6 or more predicted transmembrane domains for impaired growth on glycerol medium. Deletion of STL1, which encodes a member of the sugar transporter family, eliminates active glycerol transport. Stl1p is present in the plasma membrane in S. cerevisiae during conditions where glycerol symport is functional. Both the Stl1 protein and the active glycerol transport are subject to glucose-induced inactivation, following identical patterns. Furthermore, the Stl1 protein and the glycerol symporter activity are strongly but transiently induced when cells are subjected to osmotic shock. STL1 was heterologously expressed in Schizosaccharomyces pombe, a yeast that does not contain its own active glycerol transport system. In S. pombe, STL1 conferred the ability to take up glycerol against a concentration gradient in a proton motive force-dependent manner. We conclude that the glycerol proton symporter in S. cerevisiae is encoded by STL1.

Previous studies evidenced in Saccharomyces cerevisiae the activity of a H+/glycerol symport, derepressed by growth on non‐fermentable carbon sources, later associated with GUP1 and GUP2 genes. It was also demonstrated that only the combined deletion of GUP1, GUP2 together with GUT1 (glycerol kinase) abolished active transport in ethanol‐induced cells. In this work, we show that a glycerol H+/symport, with identical characteristics to the previously described, was found in gup1gup2gut1 grown under salt‐stress, particularly high in cells collected during diauxic‐shift. These results suggest different roles for Gup1/2p than glycerol transport. The gene encoding for glycerol active uptake is thus yet unknown.