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Murine Ortholog of the Novel Glycosyltransferase, B3GTL: Primary Structure, Characterization of the Gene and Transcripts, and Expression in Tissues.

Authors :
Heinonen, Taisto Y. K.
Pelto-Huikko, Markku
Pasternack, Leena
Mäki, Markku
Kainulainen, Heikki
Source :
DNA & Cell Biology. Aug2006, Vol. 25 Issue 8, p465-474. 10p. 1 Chart.
Publication Year :
2006

Abstract

Glycosylation of proteins and lipids is important in cellular communication and maintenance of tissues. B3GTL (β3-glycosyltransferase-like) is a novel glycosyltransferase that is found in multicellular animals ranging from mammals to insects and nematodes. The aim of this work was to identify and characterize the B3GTL gene in the mouse and to study its expression in various tissues. The murine gene codes for a protein which shares 84% amino acid sequence identity with its human ortholog, and contains all the primary structural features that characterize B3GTL proteins. The murine and human B3GTL genes share an identical exon/intron organization, and both genes utilize multiple polyadenylation signals. Their promoter regions show extensive conservation, implying that the two genes also share regulatory similarities. This notion was reinforced by Northern hybridization analysis of mouse tissues, which showed the tissue distribution of B3GTL mRNA to be similar to that previously found in human tissues, with the heart, kidney, and brain being major sites of expression in both species. The localization of B3GTL mRNA was studied by in situ hybridization in an extensive collection of mouse tissues, of which the granular cells of the olfactory bulb and the epithelium of the seminal vesicle displayed particularly strong signals. Together, these analyses indicate that the B3GTL mRNA is subject to strong tissue-specific and developmental regulation. The findings reported here make possible the design of a B3GTL "knock-out" mouse, provide a framework for analyzing the regulation of the gene, and provide an extensive catalog of tissues in which this novel protein acts. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10445498
Volume :
25
Issue :
8
Database :
Academic Search Index
Journal :
DNA & Cell Biology
Publication Type :
Academic Journal
Accession number :
21945123
Full Text :
https://doi.org/10.1089/dna.2006.25.465