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J. Biol. Chem., Vol. 275, Issue 29, 22284-22292, July 21, 2000
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From the Enamel biomineralization is a complex process
that involves interactions between extracellular matrix proteins. To
identify proteins interacting with tuftelin, a potential nucleator of
enamel crystallites, the yeast two-hybrid system was applied to a mouse tooth expression library and a
tuftelin-interacting protein (TIP) was isolated for further characterization. Polyclonal antibodies were
prepared against two recombinant variants of this protein. Both
antibodies identified a major protein product in tooth organs at 39 kDa, and this protein has been called TIP39. Northern analysis showed
TIP39 messenger RNA in multiple organs, a pattern similar to that of
tuftelin messenger RNA. In situ hybridization of mandibles of 1-day-old mice detected TIP39 RNA in secretory ameloblasts and
odontoblasts. Immunolocalization of TIP39 and tuftelin in cultured
ameloblast-like cells showed that these two proteins colocalize. Within
the developing tooth organ, TIP39 and tuftelin immunolocalized to the
apical pole of secretory ameloblasts (Tomes' processes) and to the
newly secreted extracellular enamel matrix. TIP39 amino acid sequence
appears to be highly conserved with similarities to proteins in species
as diverse as yeast and primates. Available sequence data and the
findings reported here suggest a role for TIP39 in the secretory
pathway of extracellular proteins.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF156852.
A Tuftelin-interacting Protein (TIP39) Localizes to the Apical
Secretory Pole of Mouse Ameloblasts*
,§,,
, and
Center for Craniofacial Molecular Biology,
University of Southern California School of Dentistry,
Los Angeles, California 90033-1004, the ¶ Department of
Pharmaceutical Sciences, University of Southern California School of
Pharmacy, Los Angeles, California 90033, and the Institute of
Oral Pathology, Faculty of Dentistry, University of Oslo, P. O. Box 1109 Blindern, N-0317 Oslo, Norway
*
This work was supported by NIDCR Grants DE06988, DE07211,
DE11704, and DE13045 from the National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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