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Immunoreaction against antifukutin antibody is found in all the retinal layers, with stronger intensity in the inner segments of photoreceptors and in the outer plexiform layer [36]. In our immunostaining on formalin-fixed, paraffin-embedded human retina, all the layers are stained, but more intense in the outer and inner nuclear layer (Figure 5). This may due to the difference of tissue preparation like fixation. As for subcellular localization of fukutin, in retinal cells, it is mainly localized in the endoplasmic reticulum rather than the Golgi apparatus and in the nucleus in vivo [36]. Similar localization is observed in carcinoma cell lines [48]. These observations are contradict to the general consideration that fukutin is localized in the Golgi apparatus on cultured cells transfected with fukutin [3]. Further examinations are needed to explain the difference and clarify the localization of fukutin in vivo. If fukutin is truly localized in the endoplasmic reticulum and nucleus, this might suggest further unknown functions of fukutin, regardless of the

Expression of fukutin in normal human retina. Fukutin is expressed in both retinal neurons and Müller cells (A–C). On fluorescent immunohistochemistry (A), fukutin is visualized in red (DAPI: blue). On Photoshopaided double immunohistochemistry, green color indicates the elements positive for both fukutin and GFAP. IPL: inner plexiform layer, INL: inner nuclear layer, OPL: outer plexiform layer, ONL: outer nuclear layer.

Among severe forms of α-dystroglycanopathy like WWS, MEB, and FCMD, apparent CNS and ocular lesions are accompanied. Pathology of ocular lesions shares some characteristics common with that of CNS lesions. In this chapter, representative pathological findings of the eye of FCMD are presented, mainly focusing on the retinal dysplasia, and its pathogenesis is discussed with the review

The authors wish to thank Ms. Noriko Sakayori, Mr. Fumiaki Muramatsu, Mr. Hideyuki Takeiri, Mr. Shuichi Iwasaki, and Mr. Mizuho Karita for their excellent

relation to the glycosylation of α-DG.

4. Conclusions

Figure 5.

Muscular Dystrophies

of literatures.

Acknowledgements

technical assistance.

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Tomoko Yamamoto1,2\*, Yoichiro Kato2 and Noriyuki Shibata1,2

1 Department of Surgical Pathology, Tokyo Women's Medical University Hospital, Shinjuku-ku, Tokyo, Japan

2 Department of Pathology, Tokyo Women's Medical University, Shinjuku-ku, Tokyo, Japan

\*Address all correspondence to: yamamoto.tomoko@twmu.ac.jp

© 2018 The Author(s). Licensee IntechOpen. This chapter is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/ by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
