Congenital disorder of glycosylation-Ia (CDG-Ia, also known as PMM2-CDG) is caused by mutations in the gene that encodes phosphomannomutase 2 (PMM2, EC 5.4.2.8) leading to a multisystemic disease with severe psychomotor and mental retardation. In a hypomorphic Pmm2 mouse model, we were able to overcome embryonic lethality by feeding mannose to pregnant dams. The results underline the essential role of glycosylation in embryonic development and may open new treatment options for this disease.

Modification of glycoproteins by the attachment of fucose residues is widely distributed in nature. The importance of fucosylation has recently been underlined by identification of the monogenetic inherited human disease "congenital disorder of glycosylation IIc," also termed "leukocyte adhesion deficiency II." Due to defective Golgi GDP-fucose transporter (SLC35C1) activity, patients show a hypofucosylation of glycoproteins and present clinically with mental and growth retardation, persistent leukocytosis, and severe infections. To investigate effects induced by the loss of fucosylated structures in different organs, we generated a mouse model for the disease by inactivating the Golgi GDP-transporter gene (Slc35c1). Lectin binding studies revealed a tremendous reduction of fucosylated glycoconjugates in tissues and isolated cells from Slc35c1 ؊/؊ mice. Fucose treatment of cells from different organs led to partial normalization of the fucosylation state of glycoproteins, thereby indicating an alternative GDP-fucose transport mechanism. Slc35c1-deficient mice presented with severe growth retardation, elevated postnatal mortality rate, dilatation of lung alveoles, and hypocellular lymph nodes. In vitro and in vivo leukocyte adhesion and rolling assays revealed a severe impairment of P-, E-, and L-selectin ligand function. The diversity of these phenotypic aspects demonstrates the broad general impact of fucosylation in the mammalian organism.The covalent attachment of oligosaccharide moieties to newly synthesized proteins comprises one of the most frequent but also complex forms of co-and posttranslational protein modifications, which has been found in nearly all living organisms (1). Glycan structures affect the physicochemical properties and the function of proteins in a variety of biological processes, including folding, solubility, sorting, proteolytic stability, and receptor-ligand interactions. In mammalian organisms, the biosynthesis of the oligosaccharide chains requires a broad spectrum of glycosyltransferases, glycosidases, transport proteins, and 13 different monosaccharides (2-4).Due to its variability of binding types (␣-1,2-, ␣-1,3-, ␣-1,4-, and ␣-1,6-fucosylation have been described), the monosaccharide fucose plays an important role in the microheterogeneity of oligosaccharide structures (5). Fucose residues are predominantly linked to peripheral parts of N-, O-, and lipid-linked oligosaccharides, thereby building cap structures, which have been observed in many surface-localized and secreted proteins,

The aim of this exploratory research is to capture spatial evolution patterns in the Bucharest metropolitan area using sets of single polarised synthetic aperture radar (SAR) satellite data and multi-temporal radar interferometry. Three sets of SAR data acquired during the years 1992–2010 from ERS-1/-2 and ENVISAT, and 2011–2014 from TerraSAR-X satellites were used in conjunction with the Small Baseline Subset (SBAS) and persistent scatterers (PS) high-resolution multi-temporal interferometry (InSAR) techniques to provide maps of line-of-sight displacements. The satellite-based remote sensing results were combined with results derived from classical methodologies (i.e., diachronic cartography) and field research to study possible trends in developments over former clay pits, landfill excavation sites, and industrial parks. The ground displacement trend patterns were analysed using several linear and nonlinear models, and techniques. Trends based on the estimated ground displacement are characterised by long-term memory, indicated by low noise Hurst exponents, which in the long-term form interesting attractors. We hypothesize these attractors to be tectonic stress fields generated by transpressional movements.

Congenital disorders of glycosylation (CDG) comprise a clinically and biochemically heterogeneous group of monogenetic-inherited, multisystemic diseases that affect the biosynthesis of N- and/or O-glycans linked to glycoconjugates. Recently, we identified the first patient with a defect in the cytosolic-orientated GDP-mannose:Man(3-4) GlcNAc(2)-PP-dolichol alpha-1,2-mannosyltransferase (ALG11), who presented an accumulation of shortened dolichol-linked oligosaccharides leading to CDG-Ip (ALG11-CDG). Here we describe an improved metabolic labeling method that allowed the identification of three new CDG-Ip cases that were missed so far in routine diagnostics. Although all CDG-Ip patients carry different mutations in the ALG11 gene, they share a variety of clinical syndromes like an unremarkable prenatal period followed by developmental delay, psychomotor, and mental retardation, strabismus convergens and seizures occurring in the first year of life.