Insulin sensitivity was evaluated SRT2104 by an insulin sensitivity index derived from OGTT (IS(OGTT)), whereas insulin secretion was calculated as a ratio of the total
area under the insulin curve to the total area under the glucose curve (AUC(ins/glu)). Beta cell function in relation to insulin sensitivity (i.e. disposition index) was derived from the product of insulin sensitivity and insulin secretion (i.e. AUC(ins/glu) x IS(OGTT)). In women diagnosed with GDM (n=57), the disposition index was significantly lower than that in those without GDM, irrespective of obesity. The disposition index in women with GDM was significantly correlated with levels of fasting and mean preprandial capillary glucose and HbA1c before initiating insulin therapy (r = -0.45, -0.38, -0.49, respectively). Furthermore, there was a significant correlation
between the disposition selleck chemicals index and total insulin dosage to achieve glycemic goal (r = -0.41). In conclusion, we demonstrated beta cell dysfunction in Japanese women with GDM irrespective of obesity. The level of beta cell dysfunction in GDM was associated with the severity of glucose intolerance and total insulin dosage required. These findings underpin clinical significance of beta cell dysfunction in GDM.”
“Metallothioneins (MTs) are ubiquitous cysteine-rich proteins with a high affinity for divalent metal ions such as Zn-II, Cu-I and Cd-II that are involved in metal ion homeostasis and detoxification, as well as protection against reactive oxygen species. Here we show the NMR solution structure
of the beta(E)-domain of the early cysteine-labeled protein (E-c-1) from find more wheat (beta(E)-E-c-1), which represents the first three-dimensional structure of a plant MT. The beta(E)-domain comprises the 51 C-terminal residues of E-c-1 and exhibits a distinctive unprecedented structure with two separate metal-biricling centers, a mononuclear Zn-II binding site constituted by two cysteine and two highly conserved histidine residues as found in certain zinc-finger motifs, and a cluster formed by three Zn-II ions coordinated by nine Cys residues that resembles the cluster in the beta-domain of vertebrate MTs. Cys-metal ion connectivities were determined by exhaustive structure calculations for all 7560 possible configurations of the three-metal cluster. Backbone dynamics investigated by N-15 relaxation experiments support the results of the structure determination in that beta(E)-E-c-1 is a rigidly folded polypeptide. To further investigate the influence of metal ion binding on the stability of the structure, we replaced Zn-II with Cd-II ions and examined the effects of metal ion release on incubation with a metal. ion chelator. (C) 2009 Elsevier Ltd. All rights reserved.