Document Detail


From cytoskeleton to polarity and chemoreception in the gut epithelium.
MedLine Citation:
PMID:  9928371     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The membrane surface of polarized epithelial cells can be separated in apical and basolateral domains that differ in molecular composition and function. Components of the cytoskeleton obviously play an important role in both generation and maintenance of epithelial polarity. The microtubular system is uniformly aligned in enterocytes and pancreatic acinar cells with the minus ends of the microtubules located apically and the plus ends basally. Drug-induced disassembly of microtubules results in mistargeting of pancreatic zymogen granules and of apical but not basolateral membrane proteins of enterocytes. Association of zymogen granules with the minus end motor protein, cytoplasmic dynein, and components of its receptor, dynactin, indicates that microtubules are important for vectorial delivery of apical but not basolateral post-Golgi vesicles. The lateral membrane domain of the gut epithelium is scaffolded by a spectrin-based membrane cytoskeleton consisting basically of actin, spectrin, and ankyrin. Ankyrin binds to different integral membrane proteins, such as the sodium pump in glandular and kidney epithelial cells or to the anion exchanger (AE2) of gastric parietal cells, thereby probably playing a critical role in maintenance and/or generation of the polarized distribution of these basolateral membrane proteins. Scattered epithelial cells sharing apical cytoskeletal features of gustatory receptor cells were identified as brush cells (tufted cells). These cells are rich in nitric oxide synthase and contain in their apical brush border the gustatory trimeric G-protein, alpha-gustducin, indicating that brush cells are involved in chemoreceptive signaling.
Authors:
D Höfer; T Jöns; J Kraemer; D Drenckhahn
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Annals of the New York Academy of Sciences     Volume:  859     ISSN:  0077-8923     ISO Abbreviation:  Ann. N. Y. Acad. Sci.     Publication Date:  1998 Nov 
Date Detail:
Created Date:  1999-02-24     Completed Date:  1999-02-24     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  7506858     Medline TA:  Ann N Y Acad Sci     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  75-84     Citation Subset:  IM    
Affiliation:
Institute of Anatomy, University of Würzburg, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Membrane / physiology
Cell Polarity*
Chemoreceptor Cells / physiology*
Cytoskeleton / physiology*
Epithelial Cells / physiology*
Gastric Mucosa / physiology*
Golgi Apparatus / physiology
Humans
Intestinal Mucosa / physiology*
Microtubules / physiology
Microvilli / physiology

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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