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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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1437-4315
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Volume 388, Issue 12

Issues

Salivary agglutinin/glycoprotein-340/DMBT1: a single molecule with variable composition and with different functions in infection, inflammation and cancer

Antoon J.M. Ligtenberg
  • 1Department of Oral Biochemistry, Academic Centre for Dentistry, Free University and University of Amsterdam, van de Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Enno C.I. Veerman
  • 2Department of Oral Biochemistry, Academic Centre for Dentistry, Free University and University of Amsterdam, van de Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Arie V. Nieuw Amerongen
  • 3Department of Oral Biochemistry, Academic Centre for Dentistry, Free University and University of Amsterdam, van de Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jan Mollenhauer
  • 4Division of Molecular Genome Analysis, German Cancer Research Centre (DKFZ), Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2007-11-16 | DOI: https://doi.org/10.1515/BC.2007.158

Abstract

Salivary agglutinin (SAG), lung glycoprotein-340 (gp-340) and Deleted in Malignant Brain Tumours 1 (DMBT1) are three names for identical proteins encoded by the dmbt1 gene. DMBT1/SAG/gp-340 belongs to the scavenger receptor cysteine-rich (SRCR) superfamily of proteins, a superfamily of secreted or membrane-bound proteins with SRCR domains that are highly conserved down to sponges, the most ancient metazoa. On the one hand, DMBT1 may represent an innate defence factor acting as a pattern recognition molecule. It interacts with a broad range of pathogens, including cariogenic streptococci and Helicobacter pylori, influenza viruses and HIV, but also with mucosal defence proteins, such as IgA, surfactant proteins and MUC5B. Stimulation of alveolar macrophage migration, suppression of neutrophil oxidative burst and activation of the complement cascade point further to an important role in the regulation of inflammatory responses. On the other hand, DMBT1 has been demonstrated to play a role in epithelial and stem cell differentiation. Inactivation of the gene coding for this protein may lead to disturbed differentiation, possibly resulting in tumour formation. These data strongly point to a role for DMBT1 as a molecule linking innate immune processes with regenerative processes.

Keywords: innate immunity; mucosal defence; saliva; tumour suppression

About the article

Corresponding author


Published Online: 2007-11-16

Published in Print: 2007-12-01


Citation Information: Biological Chemistry, Volume 388, Issue 12, Pages 1275–1289, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.158.

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