Posttranslational Amelogenin Processing and Changes in Matrix Assembly during Enamel Development.
Posttranslational Amelogenin Processing and Changes in Matrix Assembly during Enamel Development.
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DOI：
10.3389/fphys.2017.00790
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发表时间：
2017
影响因子：
4
通讯作者：
Diekwisch TGH
中科院分区：
文献类型：
--
作者：
Pandya M;Lin T;Li L;Allen MJ;Jin T;Luan X;Diekwisch TGH
The extracellular tooth enamel matrix is a unique, protein-rich environment that provides the structural basis for the growth of long and parallel oriented enamel crystals. Here we have conducted a series of in vivo and in vitro studies to characterize the changes in matrix shape and organization that take place during the transition from ameloblast intravesicular matrices to extracellular subunit compartments and pericrystalline sheath proteins, and correlated these changes with stages of amelogenin matrix protein posttranslational processing. Our transmission electron microscopic studies revealed a 2.5-fold difference in matrix subunit compartment dimensions between secretory vesicle and extracellular enamel protein matrix as well as conformational changes in matrix structure between vesicles, stippled materials, and pericrystalline matrix. Enamel crystal growth in organ culture demonstrated granular mineral deposits associated with the enamel matrix framework, dot-like mineral deposits along elongating initial enamel crystallites, and dramatic changes in enamel matrix configuration following the onset of enamel crystal formation. Atomic force micrographs provided evidence for the presence of both linear and hexagonal/ring-shaped full-length recombinant amelogenin protein assemblies on mica surfaces, while nickel-staining of the N-terminal amelogenin N92 His-tag revealed 20 nm diameter oval and globular amelogenin assemblies in N92 amelogenin matrices. Western blot analysis comparing loosely bound and mineral-associated protein fractions of developing porcine enamel organs, superficial and deep enamel layers demonstrated (i) a single, full-length amelogenin band in the enamel organ followed by 3 kDa cleavage upon entry into the enamel layer, (ii) a close association of 8–16 kDa C-terminal amelogenin cleavage products with the growing enamel apatite crystal surface, and (iii) a remaining pool of N-terminal amelogenin fragments loosely retained between the crystalline phases of the deep enamel layer. Together, our data establish a temporo-spatial correlation between amelogenin protein processing and the changes in enamel matrix configuration that take place during the transition from intracellular vesicle compartments to extracellular matrix assemblies and the formation of protein coats along elongating apatite crystal surfaces. In conclusion, our study suggests that enzymatic cleavage of the amelogenin enamel matrix protein plays a key role in the patterning of the organic matrix framework as it affects enamel apatite crystal growth and habit.
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DOI：
10.1002/anie.201100181
发表时间：
2011-08-08
期刊：
Angewandte Chemie (International ed. in English)
影响因子：
--
作者：
Friddle RW;Battle K;Trubetskoy V;Tao J;Salter EA;Moradian-Oldak J;De Yoreo JJ;Wierzbicki A
通讯作者：
Wierzbicki A
影响因子：
4.6
作者：
Carneiro KM;Zhai H;Zhu L;Horst JA;Sitlin M;Nguyen M;Wagner M;Simpliciano C;Milder M;Chen CL;Ashby P;Bonde J;Li W;Habelitz S
通讯作者：
Habelitz S
影响因子：
3
作者：
Beniash, Elia;Metzler, Rebecca A.;Lam, Raymond S. K.;Gilbert, P. U. P. A.
通讯作者：
Gilbert, P. U. P. A.
影响因子：
3.6
作者：
DIEKWISCH, TGH;BERMAN, BJ;SLAVKIN, HC
通讯作者：
SLAVKIN, HC
影响因子：
4.8
作者：
Bromley, Keith M.;Kiss, Andrew S.;Moradian-Oldak, Janet
通讯作者：
Moradian-Oldak, Janet