title: Influence of spermine on intestinal maturation of the glycoprotein glycosylation process in neonatal rats.
abstract: Previous work has shown an inverse evolution of the rat intestinal glycoprotein sialylation that decreases from birth to weaning and of fucosylation that increases markedly after weaning during postnatal development. At weaning time, an increase in the intestinal level of polyamines (and especially that of spermine) was observed, owing partly to the higher level of spermine found in solid food given to rats at this period in comparison with the level found in milk. To study the role of this polyamine as a possible maturation factor of the glycoprotein glycosylation, suckling rats were treated for 4 days with spermine administered orally. This treatment allowed us to mimic the spermine increase that was observed naturally in rat small intestine after weaning because, in intestines of spermine-treated suckling rats, spermine was the only polyamine to be increased and was at a level similar to that of weaned rats. Spermine treatment did not induce appreciable changes in sialyltransferase activity or in sialylation of the brush-border-membrane glycoproteins. On the contrary, this treatment induced a rise in an alpha-1, 2-fucosyltransferase activity that was regulated at the transcriptional level, but not by its inhibitor (fuctinin), and no change in the availability of substrate (GDP-fucose). As a consequence of the increase in alpha-1,2-fucosyltransferase level and of the decrease in alpha-l-fucosidase level after treatment with spermine, several alpha-1,2-fucoproteins, naturally found in brush border membranes after weaning time, appeared precociously in these membranes after the treatment of the immature suckling rats. These results indicate that spermine is a maturation factor for the fucosylation of intestinal brush-border-membrane glycoproteins but not for their sialylation, and that this polyamine might be implicated in the increased fucosylation naturally occurring at weaning time during postnatal development.
authors.affiliation: Unité INSERM U189 - SDI CNRS, Département de Biochimie, Faculté de Médecine Lyon-Sud, BP 12, 69600 Oullins, France.
authors.forename: S
authors.initials: S
authors.lastname: Greco
authors.forename: I
authors.initials: I
authors.lastname: Hugueny
authors.forename: P
authors.initials: P
authors.lastname: George
authors.forename: P
authors.initials: P
authors.lastname: Perrin
authors.forename: P
authors.initials: P
authors.lastname: Louisot
authors.forename: M C
authors.initials: MC
authors.lastname: Biol
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D000833:Animals, Suckling; D005647:Fucosyltransferases / Q000235:genetics / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation / Q000187:drug effects; D007421:Intestine, Small / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism*; D008297:Male; D008871:Microvilli / Q000187:drug effects / Q000378:metabolism; D011073:Polyamines / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D012799:Sialyltransferases / Q000378:metabolism; D013096:Spermine / Q000494:pharmacology*
chemical_list: D006023:Glycoproteins; D011073:Polyamines; D012333:RNA, Messenger; D013096:Spermine; D005647:Fucosyltransferases; D012799:Sialyltransferases