Literature DB >> 8088431

Developmental regulation of beta-galactoside alpha 2,6-sialyltransferase in small intestine epithelium.

A Vertino-Bell1, J Ren, J D Black, J T Lau.   

Abstract

A striking biochemical alteration to the epithelium of the small intestine upon weaning is the loss of microvillar sialic acids. Antibody and cDNA probes to the beta-galactoside alpha 2,6-sialyltransferase (SiaT-1, EC 2.4.99.1) were used to characterize the expression of this sialyltransferase in the small intestine of suckling rats. SiaT-1 mRNA and protein in the intestinal epithelium are rapidly lost upon weaning, in agreement with the loss of mucosal sialic acids and general sialyltransferase activity. Developmental repression of SiaT-1 is manifested in a proximal to distal gradient; SiaT-1 mRNA and protein are lost first from the duodenum and persist the longest in the ileum. We have previously documented that SiaT-1 gene expression can be transcriptionally initiated from a number of distinct tissue-specific promoter regions. Here, by criteria of mRNA mobility on agarose gels, primer extension analysis, and differential Northern hybridization, we show that the promoter previously considered to be liver-specific is operative in SiaT-1 expression in the small intestine of suckling animals. Comparison of this SiaT-1 promoter region with promoter regions of other genes exhibiting dual intestine-hepatic tissue specificity revealed a number of striking sequence similarities. Regulatory implications and consequences of small intestinal SiaT-1 expression in suckling but not in weaned animals are discussed.

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Year:  1994        PMID: 8088431     DOI: 10.1006/dbio.1994.1240

Source DB:  PubMed          Journal:  Dev Biol        ISSN: 0012-1606            Impact factor:   3.582


  10 in total

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3.  Differentiation -dependent expression of human beta-galactoside alpha 2,6-sialyltransferase mRNA in colon carcinoma CaCo-2 cells.

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4.  Murine hepatic beta-galactoside alpha 2,6-sialyltransferase gene expression involves usage of a novel upstream exon region.

Authors:  Y P Hu; M Dalziel; J T Lau
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Review 5.  The sialyl-alpha2,6-lactosaminyl-structure: biosynthesis and functional role.

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6.  Influence of spermine on intestinal maturation of the glycoprotein glycosylation process in neonatal rats.

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7.  Altered granulopoietic profile and exaggerated acute neutrophilic inflammation in mice with targeted deficiency in the sialyltransferase ST6Gal I.

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8.  Bacterial colonization and TH17 immunity are shaped by intestinal sialylation in neonatal mice.

Authors:  Eric E Irons; Eduardo Cortes Gomez; Valerie L Andersen; Joseph T Y Lau
Journal:  Glycobiology       Date:  2022-04-21       Impact factor: 5.954

9.  Disruption of hepatocyte Sialylation drives a T cell-dependent pro-inflammatory immune tone.

Authors:  Douglas M Oswald; Julie Y Zhou; Mark B Jones; Brian A Cobb
Journal:  Glycoconj J       Date:  2020-03-28       Impact factor: 2.916

10.  Differential expression of sialic acid on porcine organs during the maturation process.

Authors:  V Vallejo; J Reyes-Leyva; J Hernández; H Ramírez; P Delannoy; E Zenteno
Journal:  Comp Biochem Physiol B Biochem Mol Biol       Date:  2000-07       Impact factor: 2.231

  10 in total

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