caa a22 4500 463185315 CHVBK 20180406164851.0 cr unu---uuuuu 170326e20070101xx s 000 0 eng 10.1007/s00726-006-0325-y doi (NATIONALLICENCE)springer-10.1007/s00726-006-0325-y Manifold decrease of sialic acid synthase in fetal Down syndrome brain [Elektronische Daten] [T. Gulesserian, E. Engidawork, M. Fountoulakis, G. Lubec] Summary.: Background: Down syndrome (DS, trisomy 21) is the most common genetic cause of mental retardation. A large series of biochemical defects have been observed in fetal and adult DS brain that help in unraveling the molecular mechanisms underlying mental retardation. Aims: As sialylation of glycoconjugates plays an important role in brain development, this study aimed to look at the sialic acid metabolism by measuring sialic acid synthase (SAS; N-acetylneuraminate synthase) in early second trimester fetal control and DS brain. Results: In this regard, protein profiling was performed by two-dimensional gel electrophoresis coupled to matrix-assisted laser desorption/ionization mass-spectrometry followed by database search and subsequent quantification of spot using specific software. SAS, the enzyme catalyzing synthesis of N-acetyl-neuraminic acid (syn: sialic acid) was represented as a single spot and found to be significantly and manifold reduced (P < 0.01) in cortex of fetuses with DS (control vs. DS, 0.052 ± 0.025 vs. 0.012 ± 0.006). Conclusion: The intriguing finding of the manifold decrease of SAS in DS fetal cerebral cortex as early as in the second trimester of pregnancy may help to explain the brain deficit observed in DS. Decreased SAS may well lead to altered sialic acid metabolism, required for brain development and, more specifically, for sialylation of key brain proteins, including neuronal cell adhesion molecule and myelin associated glycoprotein. Springer-Verlag, 2006 Keywords: Sialic acid synthase - Sialic acid - Two-dimensional gel electrophoresis - Down syndrome - Fetal brain nationallicence Gulesserian T. Department of Pediatrics, Medical University of Vienna, Vienna, Austria aut Engidawork E. Department of Pediatrics, Medical University of Vienna, Vienna, Austria aut Fountoulakis M. F. Hoffmann-La Roche Ltd., Pharmaceutical Research, Genomics Technologies, Basel, Switzerland aut Lubec G. Department of Pediatrics, Medical University of Vienna, Vienna, Austria aut Amino Acids Springer-Verlag 32/1(2007-01-01), 141-144 0939-4451 32:1<141 2007 32 726 https://doi.org/10.1007/s00726-006-0325-y text/html Onlinezugriff via DOI 1 brief-communication jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0325-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Gulesserian T. Department of Pediatrics, Medical University of Vienna, Vienna, Austria aut NATIONALLICENCE 700 1- Engidawork E. Department of Pediatrics, Medical University of Vienna, Vienna, Austria aut NATIONALLICENCE 700 1- Fountoulakis M. F. Hoffmann-La Roche Ltd., Pharmaceutical Research, Genomics Technologies, Basel, Switzerland aut NATIONALLICENCE 700 1- Lubec G. Department of Pediatrics, Medical University of Vienna, Vienna, Austria aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 32/1(2007-01-01), 141-144 0939-4451 32:1<141 2007 32 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer