Calcium binding of enamel proteins and their derivatives with emphasis on the calcium-binding domain of porcine sheathlin

被引:57
作者
Yamakoshi, Y
Tanabe, T
Oida, S
Hu, CC
Simmer, JP
Fukae, M
机构
[1] Tsurumi Univ, Sch Dent Med, Dept Biochem, Tsurumi Ku, Yokohama, Kanagawa 2308501, Japan
[2] Univ Texas, Hlth Sci Ctr, Dept Pediat Dent, San Antonio, TX 78229 USA
关键词
amelogenesis; calcium-binding proteins; enamel; sheathlin; sulphated; O-linked oligosaccharide;
D O I
10.1016/S0003-9969(01)00070-X
中图分类号
R78 [口腔科学];
学科分类号
1003 ;
摘要
Dental enamel is believed to form by the transfer of ions froth solution, primarily calcium, phosphate, hydroxyl and carbonate, to the surface of solid-state mineral. Such precipitation phenomena can be controlled by regulating the degree of saturation of the solution with respect to the potential solid phases that can form. The concentration of free calcium is the factor that most affects the degree of saturation for calcium hydroxyapatite, and its buffering by calcium-binding proteins has been proposed as the mechanism that determines the enamel mineral structure. In this study, Stains-all staining was used to identify and isolate calcium-binding proteins from the enamel matrix, and determine their structures and association constants for calcium. Proteolytic cleavage fragments derived from the C-terminus of sheathlin, having apparent molecular weights of 13, 15, 27 and 29 kDa, were characterized by amino-terminal protein sequencing, amino acid analysis, and sugar, phosphate and sulphate determinations. Sheathlin C-terminal cleavage products were shown to have no N-linked glycosylations or phosphorylated amino acids, but Pro(350) was hydroxylated, and there was one sulphated O-linked glycosylation at Thr(386), containing galactose and N-acetylgalactosamine. The calcium-binding association constants for enamel proteins ranged from a high of 1.2 x 10(4) M-1 to a low of 4.4 x 10(1) M-1. The relative strengths of binding in order of decreasing affinity were: 13 and 15 kDa calcium-binding domain of sheathlin > 27 and 29 kDa calcium-binding proteins > 32 kDa enamelin > 89 kDa enamelin > 6.5 kDa, 25 kDa, 23 kDa, 20 kDa, 13 kDa, 5.3 kDa amelogenins. It is concluded that if enamel proteins have similar calcium-binding properties in vivo as have been measured in vitro, they would tend to buffer the free calcium ion concentration in enamel fluid. (C) 2001 Published by Elsevier Science Ltd.
引用
收藏
页码:1005 / 1014
页数:10
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