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- W2159968205 abstract "Bone sialoprotein (BSP) is an anionic phosphoprotein expressed in mineralizing connective tissues that binds to hydroxyapatite and nucleates its formation in vitro. Two polyglutamic acid regions (poly [E]) are believed to participate in these activities. The aim of this study was to evaluate the contribution of these acidic regions to the binding of prokaryote recombinant BSP (prBSP E ) within an actual in vivo environment. Full-length prBSP E and prBSP E in which the poly [E] domains were replaced by polyalanine (prBSP A ) were tagged with dinitrophenol (DNP). Tagged preparations comprised intact molecules and some fragmented forms. They were infused through a surgically created hole in the bone of rat hemimandibles and detected using immunogold labeling with anti-DNP antibodies. prBSP E -DNP was consistently immunodetected along exposed mineralized bone surfaces and osteocyte canaliculi at the surgical site. Few gold particles were observed on these surfaces when prBSP A -DNP was infused. Quantitative analyses showed significant differences in labeling between prBSP E -DNP (5.04 ± 0.73 particles/μm 2 ) and prBSP A -DNP (1.37 ± 0.35 particles/μm 2 ). These results indicate that poly [E] domains influence binding of prBSP E to surfaces presenting a mixture of mineral and proteins bathed by tissue fluids and suggest that they may similarly mediate the interaction of native BSP in the bone environment." @default.
- W2159968205 created "2016-06-24" @default.
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- W2159968205 date "2006-08-09" @default.
- W2159968205 modified "2023-10-13" @default.
- W2159968205 title "In Vivo Functional Analysis of Polyglutamic Acid Domains in Recombinant Bone Sialoprotein" @default.
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- W2159968205 doi "https://doi.org/10.1369/jhc.6a7046.2006" @default.
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