Advanced Search

Journal Navigation

Journal Home

Subscriptions

Archive

Contact Us

Table of Contents

CiteULike is a free service for managing and discovering scholarly references - click here to get started.

Sign In to gain access to subscriptions and/or personal tools.
Critical Reviews in Oral Biology & Medicine
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Add to Saved Citations
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Request Reprints
Right arrow Add to My Marked Citations
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Right arrow Citing Articles via Scopus
Google Scholar
Right arrow Articles by Prakobphol, A.
Right arrow Articles by Fisher, S. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?
4(3):325-333 (1993)     Crit Rev Oral Biol Med
© 1993 SAGE Publications

The High-Molecular-Weight Human Mucin Is the Primary Salivary Carrier of ABH, Lea, and Leb Blood Group Antigens

Akraporn Prakobphol

Division of Oral Biology, School of Dentistry, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143, Department of Pharmaceutical Chemistry, School of Pharmacy, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143, Departments of Psychiatry, Anatomy, and Obstetrics, Gynecology, and Reproductive Sciences, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143

Hakon Leffler

Division of Oral Biology, School of Dentistry, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143, Department of Pharmaceutical Chemistry, School of Pharmacy, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143, Departments of Psychiatry, Anatomy, and Obstetrics, Gynecology, and Reproductive Sciences, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143

Susan J. Fisher

Division of Oral Biology, School of Dentistry, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143, Department of Pharmaceutical Chemistry, School of Pharmacy, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143, Departments of Psychiatry, Anatomy, and Obstetrics, Gynecology, and Reproductive Sciences, School of Medicine, Box 0512 HSW 604, University of California, San Francisco, CA 94143

Because many bacteria interact with the carbohydrate portions of receptor molecules, factors controlling glycosylation probably influence the ability of salivary components to mediate bacterial adherence/clearance. Important sources of diversity in glycosylation are the ABO, secretor, and Lewis genes, which code for glycosyltransferases that add specific sugar sequences to the termini of carbohydrate chains of glycolipids and glycoproteins. We identified, by Western blotting, salivary glycoproteins carrying the ABH and Le a or Leb antigens. Samples of whole, unstimulated saliva were obtained from 19 subjects whose blood group was determined by agglutination of red blood cells with specific antisera. After centrifugation, the samples were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotted onto nitrocellulose. Glycoproteins carrying blood group antigens were identified by staining the blot with monoclonal antisera specific for the A, B, H, Lea, or Leb antigens. The most intensely staining component from all the samples migrated at the same position as the high-molecular-weight mucin. Saliva samples from the nonsecretors contained only the Lea antigen. Samples from the secretors contained one or more of the ABH antigens and, variably, the Leb antigen. In all cases, the salivary blood group antigens corresponded to those found on the red blood cells of the same subject. The functional consequences of the expression of blood group antigens on the high-molecular-weight mucin are not known, but their presence could modulate the adherence of certain oral microorganisms that interact preferentially with this molecule.

Key Words: saliva • mucin • carbohydrate • blood group antigens • bacterial receptors.

Critical Reviews in Oral Biology & Medicine, Vol. 4, No. 3, 325-333 (1993)
DOI: 10.1177/10454411930040031001


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


This article has been cited by other articles:


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


Home page
GlycobiologyHome page
K. A. Thomsson, B. L. Schulz, N. H. Packer, and N. G. Karlsson
MUC5B glycosylation in human saliva reflects blood group and secretor status
Glycobiology, August 1, 2005; 15(8): 791 - 804.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
K. A. Thomsson, A. Prakobphol, H. Leffler, M. S. Reddy, M. J. Levine, S. J. Fisher, and G. C. Hansson
The salivary mucin MG1 (MUC5B) carries a repertoire of unique oligosaccharides that is large and diverse
Glycobiology, January 1, 2002; 12(1): 1 - 14.
[Abstract] [Full Text] [PDF]


Home page
JDRHome page
P.A. Nielsen, U. Mandel, M.H. Therkildsen, and H. Clausen
Differential Expression of Human High-molecular-weight Salivary Mucin (MG1) and Low-molecular-weight Salivary Mucin (MG2)
Journal of Dental Research, November 1, 1996; 75(11): 1820 - 1826.
[Abstract] [PDF]


Home page
JDRHome page
A. Prakobphol, C.A. Burdsal, and S.J. Fisher
Quantifying the Strength of Bacterial Adhesive Interactions with Salivary Glycoproteins
Journal of Dental Research, May 1, 1995; 74(5): 1212 - 1218.
[Abstract] [PDF]


Home page
CROBMHome page
J.D. Rudney
Does Variability in Salivary Protein Concentrations Influence Oral Microbial Ecology and Oral Health?
Critical Reviews in Oral Biology & Medicine, January 1, 1995; 6(4): 343 - 367.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Prakobphol, F. Xu, V. M. Hoang, T. Larsson, J. Bergstrom, I. Johansson, L. Frangsmyr, U. Holmskov, H. Leffler, C. Nilsson, et al.
Salivary Agglutinin, Which Binds Streptococcus mutans and Helicobacter pylori, Is the Lung Scavenger Receptor Cysteine-rich Protein gp-340
J. Biol. Chem., December 15, 2000; 275(51): 39860 - 39866.
[Abstract] [Full Text] [PDF]