Subunit compartments of secretory stage enamel matrix. Academic Article

abstract

• Three quarters of the micro-environment of early secretory stage enamel consist of protein and water. The physical arrangement of this enamel matrix is closely related to enamel crystal growth and habit. In the present study, structural components of developing enamel were analyzed using atomic force microscopy, transmission electron microscopy, immuno-ultracryotomy, and electron diffraction. Atomic force images revealed spherical subunits measuring between 108 nm and 124 nm in diameter. Transmission electron micrographs indicated that developing crystals were surrounded by an electron dense coat which may be rich in proteins. Transmission electron micrographs and electron diffraction studies supported a concept in which initial enamel crystals consist of amorphous calcium phosphate and later fuse to hydroxyapatite. Cryo-immuno electron microscopy demonstrated homogeneous distribution of amelogenin epitopes within the entire enamel matrix. The current study suggests an intricate role of protein aggregation phenomena involved in initial enamel crystal growth and habit.

authors

• Diekwisch, Thomas

published proceedings

• Connect Tissue Res

author list (cited authors)

• Diekwisch, T. G.

citation count

• 35

complete list of authors

• Diekwisch, TG

publication date

• January 1998

publisher

• Taylor & Francis  Publisher

published in

• Connective Tissue Research  Journal

keywords

• Animals
• Cryoelectron Microscopy
• Crystallization
• Dental Enamel
• Mice
• Microscopy, Atomic Force
• Microscopy, Electron
• Microscopy, Immunoelectron
• Organometallic Compounds
• Palladium
• Staining And Labeling

Digital Object Identifier (DOI)

• 10.3109/03008209809017026

start page

• 101

end page

• 111

volume

• 38

issue

• 1-4

URL

• http://dx.doi.org/10.3109/03008209809017026