Abstract
The enzyme alpha 1,3‐galactosyltransferase (α1,3‐GT), which catalyzes synthesis of terminal α‐galactosyl epitopes (Gal α1,3Gal β1‐4GlcNAc‐R), is produced in non‐primate mammals, prosimians and new‐world monkeys, but not in old‐world monkeys, apes and humans. We cloned and sequenced a cDNA that contains the coding sequence of the feline α1,3‐GT gene. Flow cytometric analysis demonstrated that the α‐galactosyl epitope was expressed on the surface of a human cell line transduced with an expression vector containing this cDNA, and this α‐galactosyl epitope expression subsided by α‐galactosidase treatment. The open reading frame of the feline α1,3‐GT cDNA is 1,113 base pairs in length and encodes 371 amino acids. The nucleotide sequence and its deduced amino acid sequence of the feline α1,3‐GT gene are 88–90% and 85–87%, respectively, similar to the reported sequences of the bovine, porcine, marmoset and cebus monkey α1,3‐GT genes, while they are 88% and 82–83%, respectively, similar to those of the orangutan and human α1,3‐GT pseudogenes, and 81% and 77%, respectively, similar to the murine α1,3‐GT gene. Thus, the α1,3‐GT genes and pseudogenes of mammals are highly similar. Ratios of non‐synonymous nucleotide changes among the primate pseudogenes as well as the primate genes are still higher than the ratios of non‐primates, suggesting that the primate α1,3‐GT genes tend to be divergent. J. Exp. Zool.(Mol. Dev. Evol.) 306B, 2006. © 2005 Wiley‐Liss, Inc.