OBJECTIVE -The Registry for Type 1 Diabetes Mellitus in Italy (RIDI) Study Group was established to coordinate the registries of type 1 diabetes in Italy. This report is based on 3,606 children younger than 15 years diagnosed with type 1 diabetes and prospectively registered during 1990 -1999 by nine centers, covering Ͼ35% of the Italian population.RESEARCH DESIGN AND METHODS -Registries were pooled in four geographic macro-areas: north, central, south, and insular. The completeness of registration was assessed by the capture-recapture method. Poisson regression analysis was used to evaluate temporal trend in incidence.RESULTS -Large variations in incidence were confirmed not only between Sardegna and the mainland but also among peninsular areas. In Sardegna, there was an excess of boys (the boy-to-girl incidence ratio was 1.4). The overall incidence showed average increases of 3.6% (P Ͻ 0.001) and 3.7% (P Ͻ 0.001) per year in peninsular Italy and in Sardegna, respectively. Significant increases in incidence rates were found in boys aged 10 -14 years (6.7%, 95% CI 0.5-13.3) and in girls aged 5-9 years (6.6%, 0.5-13.1) living in the southern area. The incidence rate also increased in boys aged 10 -14 years (5.0%, 0.3-10) and in girls aged 0 -4 years (4.9%, 0.8 -9.1) living in Sardegna.CONCLUSIONS -Italy is a country with large geographical variations in incidence rates of type 1 diabetes. However, the rates are evenly increasing both in the mainland and Sardegna, suggesting that similar environmental factors are operating over populations that have different genetic backgrounds.

Carbohydrate recognition in water by biomimetic receptors is an attractive, but very challenging goal. Despite advances achieved in glucose recognition, little or no success has been obtained in the recognition of other saccharidic epitopes of paramount importance in biological processes. Herein, the unprecedented recognition of fucose in water by an artificial receptor that shows affinities closely comparable to those of several lectins is reported. The receptor has been constructed by assembling a hydrogen-bonding element (carbazole), a hydrophobic aromatic moiety (anthracene), and a water-solubilising function (phosphonate) into a macrocyclic structure to provide the appropriate binding geometry. The described receptor binds fucose with sub-millimolar affinity in water at physiological pH; this shows that enthalpic binding can be ascribed to hydrogen bonding to saccharidic hydroxy groups and to CH-π interactions between the sugar backbone and aromatic moieties. Experimental NOE contacts coupled to conformational search calculations return a picture of a binding site in which fucose assumes a staggered orientation reminiscent of that shown by fucose when bound to the Ralstonia solanacearum lectin (RSL).

Blood 3HB evaluation is a better indicator of metabolic control compared to urine KB detection and is useful to predict the time required for blood KB clearing. Further studies are needed to assess its use in the early detection and management of DKA.

Protein glycosylation is the most complex post‐translational modification process. More than 50 % of human cells proteins are glycosylated, whereas bacteria such as E. coli do not have this modification machinery. Indeed, the carbohydrate residues in natural proteins affect their folding, immunogenicity, and stability toward proteases, besides controlling biological properties and activities. It is therefore important to introduce such structural modification in bioengineered proteins lacking the presence of carbohydrate residues. This is not trivial as it requires reagents and conditions compatible with the protein's stability and reactivity. This work reports on the introduction of lactose moieties in two natural proteins, namely ubiquitin (Ub) and l‐asparaginase II (ANSII). The synthetic route employed is based on the sulfur(VI) fluoride exchange (SuFEx) coupling of a lactose tethered arylfluorosulfate (Lact‐Ar‐OSO2F) with the ϵ‐NH2 group of lysine residues of the proteins. This metal‐free click SuFEx reaction relies on the properties of the fluorosulfate employed, which is easily prepared in multigram scale from available precursors and reacts chemoselectively with the ϵ‐NH2 group of lysine residues under mild conditions. Thus, iterative couplings of Lact‐Ar‐OSO2F to Ub and ANSII, afforded multiple glycosylations of these proteins so that up to three and four Lact‐Ar‐OSO2 groups were introduced in Ub and ANSII, respectively, via the formation of a sulfamoyl (OSO2‐NH) linkage.