| Assembly and processing of an engineered amelogenin proteolytic product (rP148). | |
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MedLine Citation:
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PMID: 16674664 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The purpose of this study was to express, characterize, and investigate the self-assembly of a recombinant porcine amelogenin lacking the hydrophilic 24 C-terminal amino acids (rP148). To gain further insight into the function of amelogenin processing during enamel mineralization, this protein was also used as a substrate to examine the action of matrix metalloproteinase-20 (MMP-20). The assembly properties of rP148 were monitored by dynamic light scattering (DLS). In general, rP148 molecules assemble into monomers, dimers, oligomers, and some nanosphere-like particles. Depending on the solution conditions, large aggregates were also observed. Matrix metalloproteinase-20 cleaved the rP148 molecule at a few sites, creating a number of different products, including the tyrosine-rich amelogenin polypeptide (TRAP). Our data suggest that although rP148 self-assembles into small particles, its assembly properties are different from those of the full-length rP172, indicating that the C-terminal 24 amino acids play a critical role in nanosphere assembly. We further demonstrate that MMP-20 digests rP148 in a manner that generates a similar proteolytic pattern, as would be expected to occur in vivo. |
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Authors:
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Zhi Sun; Mohammad M Ahsan; Hongjun Wang; Chang Du; Christopher Abbott; Janet Moradian-Oldak |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural |
Journal Detail:
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Title: European journal of oral sciences Volume: 114 Suppl 1 ISSN: 0909-8836 ISO Abbreviation: Eur. J. Oral Sci. Publication Date: 2006 May |
Date Detail:
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Created Date: 2006-05-05 Completed Date: 2006-07-28 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 9504563 Medline TA: Eur J Oral Sci Country: Denmark |
Other Details:
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Languages: eng Pagination: 59-63; discussion 93-5, 379-80 Citation Subset: D; IM |
Affiliation:
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Center for Craniofacial Molecular Biology, University of Southern California, Los Angeles, CA 90033, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amelogenin Amino Acids / genetics, metabolism Animals Dental Enamel / metabolism Dental Enamel Proteins / genetics*, metabolism, ultrastructure Light / diagnostic use Matrix Metalloproteinase 20 Matrix Metalloproteinases / metabolism Protein Engineering* Recombinant Proteins Scattering, Radiation Swine Tooth Calcification / genetics Tyrosine / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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DE-13414/DE/NIDCR NIH HHS; DE-15332/DE/NIDCR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amelogenin; 0/Amino Acids; 0/Dental Enamel Proteins; 0/Recombinant Proteins; 0/tyrosine-rich amelogenin polypeptide; 55520-40-6/Tyrosine; EC 3.4.24.-/Matrix Metalloproteinase 20; EC 3.4.24.-/Matrix Metalloproteinases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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