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Journal of Cell Science, Vol 92, Issue 2 197-203, Copyright © 1989 by Company of Biologists


JOURNAL ARTICLES

The secretory vesicle in living Paramecium is acidic

GR Busch and BH Satir
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461.

In Paramecium, secretory proteins are packaged within membrane-bounded vesicles in a condensed form. This form expands when the proteins are released. We have now determined that a proton gradient is present in the secretory vesicles of living Paramecium. Acridine Orange, used as an in vivo indicator of acidic compartments, stained the secretory vesicles in both wild-type and mutant cells. Addition of the two agents that dissipate proton gradients (protonophores), namely, 2,4-dinitrophenol (DNP) and carbonylcyanide m-chlorophenylhydrazone (CCCP), eliminated this staining. Washed cells re-established their intravesicular acidity. Effects of sodium azide on vesicular acidity suggest that proton transport in these vesicles involves an ATP-dependent mechanism.


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S. J. Shih and D. L. Nelson
Proteolytic processing of secretory proteins in Paramecium: immunological and biochemical characterization of the precursors of trichocyst matrix proteins
J. Cell Sci., October 1, 1992; 103(2): 349 - 361.
[Abstract] [PDF]




© The Company of Biologists Ltd 1989