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Molecular and Cellular Biology, September 2005, p. 7828-7838, Vol. 25, No. 17
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.17.7828-7838.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Abnormalities Caused by Carbohydrate Alterations in Iß6-N-Acetylglucosaminyltransferase-Deficient Mice

Department of Biochemistry,¹ Division of Disease Models, Center for Neurological Disease and Cancer,² Department of Ophthalmology, Nagoya University Graduate School of Medicine, Nagoya 466-8550,³ Center for Animal Resources and Development, Kumamoto University, Kumamoto 866-0811,⁴ Department of Health Science, Faculty of Psychological and Physical Sciences, Aichi Gakuin University, Aichi 470-0195, Japan⁵

Received 2 March 2005/ Returned for modification 16 April 2005/ Accepted 8 June 2005

Iß6-N-acetylglucosaminyltransferase (IGnT) catalyzes the branching of poly-N-acetyllactosamine carbohydrate chains. In both humans and mice, three spliced forms of IGnT have been identified, and a common exon is present in all of them. We generated mice deficient in the common exon to understand the physiological function of poly-N-acetyllactosamine branching. IGnT activity was abolished in the stomach, kidney, bone marrow, and cerebellum of the deficient mice, while a low level of the activity persisted in the small intestine. Immunohistochemical analysis confirmed the loss of I antigen from the lung, stomach, and kidney. The deficient mice had reduced spontaneous locomotive activity. The number of peripheral blood lymphocytes was also reduced and renal function decreased in the deficient mice. Furthermore, in aged mice, vacuolization occurred in the kidney, and epidermoid cysts were frequently formed. However, cataracts did not develop earlier in the deficient mice. Decreased levels of lysosomal proteins, LAMP-2 and synaptotagmin VII, were found in the kidney of the deficient mice and correlated with renal abnormalities.

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