Decreased brain levels of Lupus La protein and increased U5 small ribonucleoprotein-specific 40 kDa protein in fetal Down syndrome.
RNA-binding proteins have important role in the post-transcriptional regulation of gene expression. They are involved in events such as mRNA processing, transport, stability and translation. Studies in different species indicate that mutants with defect in RNA-binding proteins are defective in cell growth and differentiation. Expression of various RNA-binding proteins in prenatal life was analyzed by the highly sensitive two-dimensional electrophoresis coupled to matrix-assisted laser desorption ionization mass spectroscopy. No apparent change was obtained in levels of heterogeneous nuclear ribonucleoproteins (A3, C1-C2, L and M), nucleolin, polyadenylate binding protein-1, nuclear factor associated with double stranded RNA-2 and RNA-binding motif protein-4 between control and Down syndrome fetuses. By contrast, U5 small nuclear ribonucleoprotein-specific 40 kDa protein (p < 0.05) and Lupus La protein (p < 0.01) were significantly elevated and reduced, respectively in fetal DS. As a conclusion we can say U5 small nuclear ribonucleoprotein-specific 40 kDa protein appears to play important role in spliceosome assembly and disassembly, whereas La protein is involved in small nuclear riboncleoprotein complex biogenesis and transfer RNA maturation. Aberrant expression of these proteins points to the fact that dysregulation of the splicing and translation processes is apparent early in prenatal life, and may contribute to the defective growth and differentiation in Down syndrome.
Gulesserian
T
T
Department of Pediatrics, Division of Neonatology, University of Vienna, Währinger Gürtel 18-20, A-1090, Vienna, Austria.
Engidawork
E
E
Fountoulakis
M
M
Lubec
G
G
D037881:Aborted Fetus / Q000737:chemistry*; D001324:Autoantigens; D002540:Cerebral Cortex / Q000737:chemistry*; D030562:Databases, Protein; D004314:Down Syndrome / Q000196:embryology / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D034481:Heterogeneous-Nuclear Ribonucleoprotein Group A-B / Q000032:analysis; D034482:Heterogeneous-Nuclear Ribonucleoprotein Group C / Q000032:analysis; D034761:Heterogeneous-Nuclear Ribonucleoprotein Group M / Q000032:analysis; D034664:Heterogeneous-Nuclear Ribonucleoprotein L / Q000032:analysis; D006801:Humans; D006868:Hydrolysis; D007091:Image Processing, Computer-Assisted; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008297:Male; D008970:Molecular Weight; D050779:Nuclear Factor 90 Proteins; D010448:Peptide Initiation Factors / Q000032:analysis; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000032:analysis; D011247:Pregnancy; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification; D016601:RNA-Binding Proteins / Q000032:analysis; D017415:Ribonucleoprotein, U5 Small Nuclear / Q000032:analysis*; D012261:Ribonucleoproteins / Q000032:analysis*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014357:Trypsin / Q000378:metabolism; D000097585:SS-B Antigen; D000097796:Nucleolin
D001324:Autoantigens; D034481:Heterogeneous-Nuclear Ribonucleoprotein Group A-B; D034482:Heterogeneous-Nuclear Ribonucleoprotein Group C; D034761:Heterogeneous-Nuclear Ribonucleoprotein Group M; D034664:Heterogeneous-Nuclear Ribonucleoprotein L; D050779:Nuclear Factor 90 Proteins; D010448:Peptide Initiation Factors; D010750:Phosphoproteins; D011506:Proteins; D016601:RNA-Binding Proteins; D017415:Ribonucleoprotein, U5 Small Nuclear; D012261:Ribonucleoproteins; D014357:Trypsin; D000097585:SS-B Antigen; D000097796:Nucleolin; C429643:ILF3 protein, human; C111580:PAIP1 protein, human; C473692:RBM4 protein, human