Fucose, placental evolution and the glycocode.
A family of 13 fucosyltransferase genes has evolved to catalyze the addition of fucose in various linkage positions to nascent glycoproteins. Null mutations in mice are unearthing unsuspected functions for glycoprotein fucosylation that affect embryo implantation and growth of the conceptus. Furthermore, as we show here, histological studies demonstrate that a variety of fucosylated structures are found within the glycan-rich interface between trophectoderm and uterine epithelium. We suggest that conservation or change in fucosyltransferase gene expression over evolutionary time has played a role in determining the stability of the maternal-fetal interface and therefore in shaping reproductive compatibility and, in turn, speciation.
Maternal and Fetal Health Research Centre, Manchester Academic Health Sciences Centre, University of Manchester, St Mary's Hospital, Oxford Road, Manchester M13 9WL, UK. john.aplin@manchester.ac.uk
John D
JD
Aplin
Carolyn J P
CJ
Jones
D000818:Animals; D010064:Embryo Implantation; D004622:Embryo, Mammalian / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D019143:Evolution, Molecular; D005260:Female; D005643:Fucose / Q000378:metabolism*; D005647:Fucosyltransferases / Q000235:genetics* / Q000378:metabolism; D006031:Glycosylation; D010920:Placenta / Q000166:cytology / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D011247:Pregnancy
D005643:Fucose; D005647:Fucosyltransferases