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 References
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 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 Curtenaz, S.
Right arrow Articles by Peck, R. K.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Curtenaz, S.
Right arrow Articles by Peck, R. K.

Journal of Cell Science, Vol 103, Issue 4 1117-1125, Copyright © 1992 by Company of Biologists

JOURNAL ARTICLES

A monoclonal antibody study of protein distribution in the membrane skeleton of the ciliate Pseudomicrothorax

S Curtenaz and RK Peck

The membrane skeleton, or epiplasm, of the ciliated protozoon Pseudomicrothorax dubius is a chemically and structurally complex layer. It is responsible for the cell shape and the positioning of some cortical organelles. One may expect that its possible morphogenetic role can be achieved only via a regional differentiation of the protein distribution in the epiplasm. We have tried to demonstrate such differentiation by preparing an epiplasm extract, which consists predominantly of concanavalin A (ConA)-positive glycoproteins. This fraction, either untreated or deglycosylated, was used to raise monoclonal antibodies (mAbs), whose specificity was tested on western blots of either untreated or deglycosylated epiplasm. The recognized polypeptides were then localized in situ by fluorescence and electron microscopic immunocytochemistry. Six mAbs are presented here. Four of them are directed against ConA-positive glycoproteins and show a localization of the latter on the outer surface of the epiplasm. The two others are directed against other epiplasmic polypeptides: one is specific for a common epitope shared by most of the epiplasmic proteins, but not by the glycoproteins, and labels the entire membrane skeleton, whereas the other recognizes three minor polypeptides, which seem localized to the inner part of the epiplasm.


This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
I Huttenlauch, R. Peck, U Plessmann, K Weber, and R Stick
Characterisation of two articulins, the major epiplasmic proteins comprising the membrane skeleton of the ciliate Pseudomicrothorax
J. Cell Sci., June 8, 2000; 111(14): 1909 - 1919.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
I Huttenlauch, R. Peck, and R Stick
Articulins and epiplasmins: two distinct classes of cytoskeletal proteins of the membrane skeleton in protists
J. Cell Sci., January 11, 1998; 111(22): 3367 - 3378.
[Abstract] [PDF]


© The Company of Biologists Ltd 1992