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AJP - Gastrointestinal and Liver Physiology, Vol 269, Issue 5 613-G627, Copyright © 1995 by American Physiological Society
ARTICLES |
B. J. Van Klinken, J. Dekker, H. A. Buller and A. W. Einerhand
Academic Medical Center, Amsterdam, The Netherlands.
The cloning of mucin cDNAs brought about by the application of molecular biology and molecular analyses constitutes a major step in understanding mucin structure and function. Here two classes of mucins are described: epithelium-associated and endothelium/leukocyte-associated mucins, which have thus far been described separately in the literature. The epithelial mucins are generally believed to play a role in cytoprotection. The endothelial and leukocyte class of mucins are adhesion molecules involved in lymphocyte homing and lymphocyte activation or are part of the adhesion cascade that plays a role in the initiation of inflammation. Mucins in general contain many threonine and serine residues, which are extensively O-glycosylated. Due to this profound glycosylation, mucins have a filamentous conformation. By virtue of their extended filamentous, and often negatively charged, structure, mucins can act as a barrier protecting the cell. However, when an opposing cell has specific receptors for mucins, adhesion can override the barrier function. Therefore, mucins may be powerful two-edged swords: they are both protective and adhesive.
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