CROBM CROBM & JDR Merger
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bradway, S. D.
Right arrow Articles by Levine, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bradway, S. D.
Right arrow Articles by Levine, M. J.

Critical Reviews in Oral Biology & Medicine, Vol 4, 293-299, Copyright © 1993 by International & American Associations for Dental Research


ARTICLES

Do proline-rich proteins modulate a transglutaminase catalyzed mechanism of candidal adhesion?

S. D. Bradway and M. J. Levine
Department of Periodontology, OSU College of Dentistry, Columbus 43210.

Previously, we reported that a membrane-bound epithelial enzyme, transglutaminase (TGase), catalyzes the covalent cross-linking of acidic proline-rich proteins (APRPs) to surface proteins of buccal epithelial cells (BECs). The purpose of this study was twofold: (1) to provide evidence that TGase stabilizes C. albicans adhesion by covalently cross-linking C. albicans and BEC surface proteins and (2) to implicate PRPs in the modulation of this adhesive mechanism. The reactivity of candidal cell wall proteins with TGase was assessed in two separate experiments. Initially, following incubation with native BECs, the cross-linking of iodinated candidal cell wall proteins into high-molecular-weight complexes, as shown by SDS-PAGE/autoradiography, was inhibited by the TGase inhibitor iodoacetamide. Additionally, [14C]putrescine in the presence of purified TGase, but not [14C]putrescine alone, was shown by SDS-PAGE/fluorography to be cross-linked into surface proteins of both morphogenetic forms (blastospore > hyphal forms) of C. albicans. In adherence assays, a component of both blastospore and hyphal form Candida/BEC adherence was shown to be resistant to detachment by heating adherent cells in 1% SDS at 100 degrees C. However, pretreatment of BECs with iodoacetamide decreased SDS resistant adherence of both forms of C. albicans by approximately 75%. When incubated with [125I]APRPs and purified TGase, both morphogenetic forms of C. albicans bound dramatically more APRP than controls without TGase. [125I]APRP binding in experimental, but not control, samples was resistant to repeated extraction (48 h) with 4% SDS/10% beta-mercaptoethanol at 65 degrees C, suggesting that [125I]APRPs were cross-linked to the Candida surface.(ABSTRACT TRUNCATED AT 250 WORDS)


This article has been cited by other articles:


Home page
J. Dent. Res.Home page
E.J. Helmerhorst and F.G. Oppenheim
Saliva: a Dynamic Proteome
J. Dent. Res., August 1, 2007; 86(8): 680 - 693.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
J. F. Staab, S. D. Bradway, P. L. Fidel, and P. Sundstrom
Adhesive and Mammalian Transglutaminase Substrate Properties of Candida albicans Hwp1
Science, March 5, 1999; 283(5407): 1535 - 1538.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
J. F. Staab, C. A. Ferrer, and P. Sundstrom
Developmental Expression of a Tandemly Repeated, Proline- and Glutamine-rich Amino Acid Motif on Hyphal Surfaces of Candida albicans
J. Biol. Chem., March 15, 1996; 271(11): 6298 - 6305.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
IADR Journals Advances in Dental Research ®
Journal of Dental Research ® Critical Reviews (1990-2004)
Copyright © 1993 Institutional Access Guidelines