Mice lacking [alpha]1,3-fucosyltransferase IX demonstrate disappearance of Lewis x structure in brain and increased anxiety-like behaviors

• Published in: Glycobiology (Oxford) Vol. 17; no. 1; p. 1
• Main Authors: Kudo, Takashi, Fujii, Takashi, Ikegami, Shiro, Inokuchi, Kaoru, Takayama, Yuko, Ikehara, Yuzuru, Nishihara, Shoko, Togayachi, Akira, Takahashi, Satoru, Tachibana, Kouichi, Yuasa, Shigeki, Narimatsu, Hisashi
• Format: Journal Article
• Language: English
• Published: Oxford Oxford Publishing Limited (England) 01.01.2007
• ISSN: 0959-6658; 1460-2423

The 3-fucosyl-N-acetyllactosamine [Lewis x (Lex), CD15, SSEA-1] carbohydrate structure is expressed on several glycolipids, glycoproteins, and proteoglycans of the nervous system and has been implicated in cell-cell recognition, neurite outgrowth, and neuronal migration during development. To characterize the functional role of Lex carbohydrate structure in vivo, we have generated mutant mice that lack α1,3-fucosyltransferase IX (Fut9-/-). Fut9-/- mice were unable to synthesize the Lex structure carried on glycoproteins and glycolipids in embryonic and adult brain. However, no obvious pathological differences between wild-type and Fut9-/- mice were found in brain. In behavioral tests, Fut9-/- mice exhibited increased anxiety-like responses in dark-light preference and in elevated plus maze tests. Immunohistochemical analysis showed that the number of calbindin-positive neurons was decreased in the basolateral amygdala in Fut9-/- mice. These observations indicated that the carbohydrates synthesized by Fut9 play critical roles in functional regulations of interneurons in the amygdalar subdivisions and suggested a role for the Lex structure in some aspects of emotional behavior in mice.