spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

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 Email this article to a friend
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 Google Scholar
Google Scholar
Right arrow Articles by Rosen, S. D.
Right arrow Articles by Grabel, L. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rosen, S. D.
Right arrow Articles by Grabel, L. B.

Journal of Cell Science, Vol 51, Issue 1 279-294, Copyright © 1981 by Company of Biologists

JOURNAL ARTICLES

Specific rosette formation between fibroblasts and erythrocytes

SD Rosen, MS Singer, CG Glabe and LB Grabel

Fibroblast cells (BHK-21, Swiss 3T3, SV403T3, L929) will form rosettes by binding to erythrocytes of specific types. The specificity of binding varies with the cell line. Monolayer cultures of spread baby hamster kidney (BHK) cells also bind erythrocytes with the same specificity exhibited by suspended cells. Our studies have concentrated on rosette formation between trypsinzed-ox (TOx) erythrocytes and BHK cells. Extensive protease treatment of the BHK cells reduces their ability to bind TOx erythrocytes in a dose- and time-dependent manner, suggesting the involvement of protein in the binding site. Simple saccharides, and glycopeptide isolated from ox erythrocyte ghosts, do not inhibit rosetting. However, neutral glycosphinogolipids from ox erythrocyte ghosts inhibit BHK-TOx rosetting, whereas neutral glycosphingolipids from non-rosetting rabbit erythrocytes have no effect on rosetting. Furthermore, incorporation of ox glycolipids into guinea-pig erythrocytes causes these non-rosetting erythrocytes to adhere to BHK cells. These experiments suggest that specific glycolipids of the ox erythrocyte act as receptors for binding sites on the cell surface of BHK cells. These cell-specific binding sites may play a role in cell-surface events involving carbohydrate recognition.




© The Company of Biologists Ltd 1981