Porcine dentin sialoprotein glycosylation and glycosaminoglycan attachments |
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Authors: | Yasuo Yamakoshi Takatoshi Nagano Jan CC Hu Fumiko Yamakoshi James P Simmer |
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Affiliation: | (1) Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, 1210 Eisenhower Place, 48108 Ann Arbor, MI, USA;(2) Department of Periodontics and Endodontics, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, 230-8501 Tsurumi-ku, Yokohama, Japan |
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Abstract: | Background Dentin sialophosphoprotein (Dspp) is a multidomain, secreted protein that is critical for the formation of tooth dentin. Mutations in DSPP cause inherited dentin defects categorized as dentin dysplasia type II and dentinogenesis imperfecta type II and type III. Dentin sialoprotein (Dsp), the N-terminal domain of dentin sialophosphoprotein (Dspp), is a highly glycosylated proteoglycan, but little is known about the number, character, and attachment sites of its carbohydrate moieties. |
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