NDLI: Porcine beta1,4-galactosyltransferase-I sequence and expression.

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Year: 2009 Volume: 44 Issue: Supplementary 2

Year: 2009 Volume: 44 Issue: 1

Year: 2008 Volume: 43

Year: 2007 Volume: 42

Porcine beta1,4-galactosyltransferase-I sequence and expression.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Landers, E. A. Burkin, H. R. Bleck, G. T. Howell-Skalla, L. Miller, D. J.
Description	Country affiliation: United States Author Affiliation: Landers EA ( Department of Animal Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.)
Abstract	Beta1,4-galactosyltransferase-I (B4GALT1), one of seven beta1,4-galactosyltransferases, is an enzyme commonly found in the trans-Golgi complex that adds galactose to oligosaccharides. In the three mammals studied to date, the B4GALT1 gene directs production of B4GALT1 protein using either of two transcription start sites. The product of the smaller transcript serves the traditional biosynthetic role in the Golgi. This form also complexes with alpha-lactalbumin, a mammary-specific protein, to form lactose synthase. In addition to a biosynthetic role, the protein translated from the longer transcript appears on the plasma membranes of some cells where it serves as a signalling receptor in cell-matrix interactions such as sperm-egg binding. The objective of this study was to sequence the protein-coding region of porcine B4GALT1 and examine the sequence for relationships to the bovine, human, murine and chicken B4GALT1 genes. The sequence for the 1203 base pair protein-coding region of porcine B4GALT1 was obtained. Analysis of the deduced protein sequences revealed that the transmembrane region displayed the highest identity between the four mammals. The catalytic domain was 84-88% identical between the porcine sequence and those of the bovine, human and mouse. The porcine protein had the lowest overall homology to the chicken amino acid sequence, 58% identity. Conservation of both transcription start sites in the porcine gene supports the existence of two isoforms. When compared to the other mammalian B4GALT1 genes, the porcine coding sequence contained a single threonine codon inserted into the region encoding the cytoplasmic domain. Two putative phosphorylation sites in the mouse cytoplasmic domain were conserved in the porcine sequence. Northern blots revealed a widely expressed 4.4 kb transcript that was more abundant in the mammary gland during lactation. These results are important for studies of the function of this unusual and important glycosyltransferase during glycoprotein biosynthesis, lactation and fertilization.
File Format	HTM / HTML
ISSN	09366768
Issue Number	2
Volume Number	44
e-ISSN	14390531
Journal	Reproduction in Domestic Animals
Language	English
Publisher	Wiley
Publisher Date	2009-04-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Reproductive Medicine Discipline Veterinary Medicine Discipline Zoology Galactosyltransferases Chemistry Genetics Swine Amino Acid Sequence Animals Blotting, Northern Cattle Dna, Complementary Humans Isoenzymes Mammary Glands, Animal Enzymology Mice Molecular Sequence Data Reverse Transcriptase Polymerase Chain Reaction Sequence Alignment Sequence Analysis, Dna Veterinary Comparative Study Journal Article
Content Type	Text
Resource Type	Article
Subject	Animal Science and Zoology Endocrinology Biotechnology

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