Journal of Histochemistry and Cytochemistry Priciples for Free Access to Science
  Search:   
    >> Advanced Search

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
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
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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ellinger, A.
Right arrow Articles by Pavelka, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ellinger, A.
Right arrow Articles by Pavelka, M.
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  
What's this?

Subdomains of the rough endoplasmic reticulum in colon goblet cells of the rat: lectin-cytochemical characterization

A Ellinger and M Pavelka

Institute of Micromorphology and Electronmicroscopy, University of Vienna, Austria.

Using lectin binding, we characterized subdomains of the rough endoplasmic reticulum (rER) in goblet cells of the rat colon. In this cell type, special rER regions can be differentiated on the basis of their content of low electron density and dilated cisternal spaces in conventional transmission electron microscopic preparations. The fine fibrillar content of these cisternal regions demonstrated high-affinity binding with lectins from wheat germ, Helix pomatia, Griffonia simplicifolia I-A4 and -B4, and Ricinus communis I, although not with the sialic acid-specific Limax flavus lectin and the fucose-binding Ulex europaeus I lectin. Sugar-inhibitory experiments indicated that glycoconjugates packed within these regions bound the lectins with higher affinity than molecules present in the Golgi apparatus and secretory granules. Furthermore, the lectin binding patterns of the rER subdomains differed from those of the Golgi apparatus and mucin granules: the terminal sugar residues sialic acid and fucose were demonstrable in the Golgi apparatus and mucin granules and were absent from the rER, while galactose-recognizing lectins bound intensely at these rER regions, weakly to Golgi elements, and were almost absent from mucin granules.

Volume 40, Issue 7, pp. 919-930, 07/01/1992
Copyright © 1992 by The Histochemical Society


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    What's this?


This article has been cited by other articles:


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
J. A. Valentijn, L. van Weeren, A. Ultee, and A. J. Koster
Novel localization of Rab3D in rat intestinal goblet cells and Brunner's gland acinar cells suggests a role in early Golgi trafficking
Am J Physiol Gastrointest Liver Physiol, July 1, 2007; 293(1): G165 - G177.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
D. R. Klopfenstein, J. Klumperman, A. Lustig, R. A. Kammerer, V. Oorschot, and H.-P. Hauri
Subdomain-specific Localization of CLIMP-63 (p63) in the Endoplasmic Reticulum Is Mediated by Its Luminal {alpha}-Helical Segment
J. Cell Biol., June 11, 2001; 153(6): 1287 - 1300.
[Abstract] [Full Text] [PDF]



Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1992