The developing enamel matrix contains mostly amelogenins, which are hydrophobic proline-rich proteins. During amelogenesis, the amelogenins are presumably hydrolysed and removed from the enamel. Recently a number of metalloproteinases that may be important in amelogenesis have been identified in zymograms of the developing enamel matrix. In the present study an antibody specific for the matrix metalloproteinase collagenase activator protein (CAP) was characterized and used to identify this metalloproteinase in enamel. Immunoblotting showed that the CAP proteinase was present in the enamel matrix. Immunohistochemistry confirmed that the proteinase is localized in the enamel matrix, most specifically along the dentino-enamel junction. Purified CAP was found to hydrolyse amelogenin protein. Possible functions of the proteinase in the enamel matrix are discussed.
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December 1989
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Research Article|
December 15 1989
The presence and possible functions of the matrix metalloproteinase collagenase activator protein in developing enamel matrix
P K DenBesten;
P K DenBesten
*Department of Biochemistry, Forsyth Dental Center, 140 Fenway, Boston, MA 02115.
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L M Heffernan;
L M Heffernan
*Department of Biochemistry, Forsyth Dental Center, 140 Fenway, Boston, MA 02115.
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B V Treadwell;
B V Treadwell
†Orthopaedic Research Laboratories, Massachusetts General Hospital, Boston, MA 02114, U.S.A.
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B J Awbrey
B J Awbrey
†Orthopaedic Research Laboratories, Massachusetts General Hospital, Boston, MA 02114, U.S.A.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1989 London: The Biochemical Society
1989
Biochem J (1989) 264 (3): 917–920.
Citation
P K DenBesten, L M Heffernan, B V Treadwell, B J Awbrey; The presence and possible functions of the matrix metalloproteinase collagenase activator protein in developing enamel matrix. Biochem J 15 December 1989; 264 (3): 917–920. doi: https://doi.org/10.1042/bj2640917
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