HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 22, 20293-20302, May 30, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/22/20293    most recent M211184200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ravindranath, R. M. H. Articles by Vaitheesvaran, B. Search for Related Content PubMed PubMed Citation Articles by Ravindranath, R. M. H. Articles by Vaitheesvaran, B. Social Bookmarking                      What's this?

Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth^*

Rajeswari M. H. Ravindranath , Rajam M. Basilrose, Sr., Naren H. Ravindranath and Bhavapriya Vaitheesvaran

From the Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, Los Angeles, California 90033-1004

The enamel protein amelogenin binds to GlcNAc (Ravindranath, R. M. H., Moradian-Oldak, R., and Fincham, A.G. (1999) J. Biol. Chem. 274, 2464–2471) and to the GlcNAc-mimicking peptide (GMp) (Ravindranath, R. M. H., Tam, W., Nguyen, P., and Fincham, A. G. (2000) J. Biol. Chem. 275, 39654–39661). The GMp motif in the N-terminal region of the cytokeratin 14 of ameloblasts binds to trityrosyl motif peptide (ATMP) of amelogenin (Ravindranath, R. M. H., Tam, W., Bringas, P., Santos, V., and Fincham, A. G. (2001) J. Biol. Chem. 276, 36586 – 36597). K14 (Type I) pairs with K5 (Type II) in basal epithelial cells; GlcNAc-acylated K5 is identified in ameloblasts. Dosimetric analysis showed the binding affinity of amelogenin to K5 and to GlcNAc-acylated-positive control, ovalbumin. The specific binding of [³H]ATMP with K5 or ovalbumin was confirmed by Scatchard analysis. [³H]ATMP failed to bind to K5 after removal of GlcNAc. Blocking K5 with ATMP abrogates the K5-amelogenin interaction. K5 failed to bind to ATMP when the third proline was substituted with threonine, as in some cases of human X-linked amelogenesis imperfecta or when tyrosyl residues were substituted with phenylalanine. Confocal laser scan microscopic observations on ameloblasts during postnatal (PN) growth of the teeth showed that the K5-amelogenin complex migrated from the cytoplasm to the periphery (on PN day 1) and accumulated at the apical region on day 3. Secretion of amelogenin commences from day 1. K5, similar to K14, may play a role of chaperone during secretion of amelogenin. Upon secretion of amelogenin, K5 pairs with K14. Pairing of K5 and K14 commences on day 3 and ends on day 9. The pairing of K5 and K14 marks the end of secretion of amelogenin.

Received for publication, October 31, 2002 , and in revised form, March 24, 2003.

^* This work was supported by NIDR, National Institutes of Health Grant DE-03660 (to R. M. H. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 323-442-3171; Fax: 323-442-2981; E-mail: rravindr{at}usc.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Hatakeyama, D. Philp, Y. Hatakeyama, N. Haruyama, L. Shum, M.A. Aragon, Z. Yuan, C.W. Gibson, T. Sreenath, H.K. Kleinman, et al. Amelogenin-mediated Regulation of Osteoclastogenesis, and Periodontal Cell Proliferation and Migration J. Dent. Res., February 1, 2006; 85(2): 144 - 149. [Abstract] [Full Text] [PDF]