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J Biol Chem, Vol. 274, Issue 4, 2464-2471, January 22, 1999
From the Center for Craniofacial Molecular Biology, School of
Dentistry, University of Southern California,
Los Angeles, California 90033
Ameloblasts secrete amelogenins on the
pre-existing enamel matrix glycoproteins at the dentine-enamel
junction. The hypothesis that amelogenins may interact with enamel
matrix glycoproteins is tested by hemagglutination of purified, native
(porcine) and recombinant murine amelogenins (rM179 and rM166) and
hemagglutination inhibition with sugars. Amelogenin agglutination of
murine erythrocytes was specifically inhibited by
N-acetylglucosamine (GlcNAc), chitobiose, and chitotetraose
and by ovalbumin with terminal GlcNAc. The GlcNAc affinity was
confirmed by dosimetric binding of rM179 with
[14C]GlcNAc, specific binding in relation to varying
concentrations of GlcNAc, Scatchard plot analysis and competitive
inhibition with cold GlcNAc. The hemagglutination activity and
[14C]GlcNAc affinity were retained by the
NH2-terminal tyrosine-rich amelogenin peptide (TRAP) but
not by the leucine-rich amelogenin peptide, LRAP (a polypeptide sharing
33 amino acid residues of TRAP), or by the C-terminal 13 residue
polypeptide of amelogenin (rM179). Since TRAP but not the 33-residue
sequence of the TRAP shared by LRAP bound to [14C]GlcNAc,
we inferred that the GlcNAc binding motif was located in the 13-residue
tyrosyl C-terminal domain of TRAP (PYPSYGYEPMGGW), which was absent
from LRAP. [14C]GlcNAc did indeed bind to this
"amelogenin tyrosyl motif peptide" but not when the tyrosyl
residues were substituted with phenylalanine or when the third
proline was replaced by threonine. Significantly, this latter
modification mimics a point mutation identified in a case of human
X-linked amelogenesis imperfecta. The amelogenin tyrosyl
motif peptide sequence showed a similarity to the secondary GlcNAc-binding site of wheat germ agglutinin.
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