title: Extensive glycosylation changes revealed by lectin histochemistry in morphologically normal prenatal tissues of the mouse mutant undulated (un/un).
abstract: Recently we observed that in human embryos and fetuses with a variety of malformations, not only malformed tissues, but also several non-malformed tissues displayed alterations in the glycosylation pattern. It was the aim of this work to investigate this more or less inexplicable phenomenon under experimental conditions. To this end, we studied a well known mouse model, the mouse mutant undulated, which has an exactly defined genetic defect (substitution in the pax-1 gene) leading to a localized malformation in the vertebral column. The glycosylation pattern was studied using lectin histochemistry. Distribution of binding sites for the lectins RCA I, Con A, SNA, SBA, PNA, LTA and WGA was studied during the organogenesis stages (i.e., days 11-18). It was striking that in mutants, changes in the glycosylation pattern were found not only in the malformed organ (i.e., vertebral anlage), but also in other embryonic tissues, which showed normal morphology. This suggests that the altered glycosylation seems to be a part of genetically determined phenomena throughout the entire organism. Our results show that a defect in a gene with a very restricted expression can cause universal changes in the glycosylation pattern during development.
authors.affiliation: Department of Histology, University of Goettingen, D-37075 Goettingen, Federal Republic of Germany. fquonda@gwdg.de
authors.forename: F
authors.initials: F
authors.lastname: Quondamatteo
authors.forename: J
authors.initials: J
authors.lastname: Zieger
authors.forename: W
authors.initials: W
authors.lastname: Götz
authors.forename: N
authors.initials: N
authors.lastname: Miosge
authors.forename: R
authors.initials: R
authors.lastname: Herken
mesh_terms: D000818:Animals; D002831:Choroid Plexus / Q000196:embryology / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics*; D004805:Ependyma / Q000196:embryology / Q000378:metabolism; D005333:Fetus / Q000737:chemistry / Q000378:metabolism; D006031:Glycosylation; D006197:Hair / Q000196:embryology / Q000378:metabolism; D006651:Histocytochemistry; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000196:embryology; D037102:Lectins; D008099:Liver / Q000196:embryology / Q000378:metabolism; D051379:Mice; D008817:Mice, Mutant Strains; D009055:Mouth / Q000196:embryology / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009672:Notochord / Q000196:embryology / Q000378:metabolism*; D051761:Paired Box Transcription Factors; D010641:Phenotype; D012137:Respiratory System / Q000196:embryology / Q000378:metabolism; D013131:Spine / Q000002:abnormalities* / Q000196:embryology / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics*
chemical_list: D004268:DNA-Binding Proteins; D037102:Lectins; D009419:Nerve Tissue Proteins; D051761:Paired Box Transcription Factors; D014157:Transcription Factors; C070835:PAX1 transcription factor