Abstract
Cytochalasin-B, one of a series of structurally related metabolites obtained from the moldHelminthosporium dematioideum, has been shown to alter several partial reaction parameters associated with mitochondrial oxidative phosphorylation. State-3 (active) respiratory rates, respiratory control ratios and overall ATPase activity were all inhibited by cytochalasin-B at concentrations between 0.2 and 1.0 mM. However, the efficiency of coupled oxidative phosphorylation, evaluated by the ADP/O ratio, was not significantly affected. Therefore, the metabolite does not appear to act at enzymic loci directly affiliated with the coupling mechanism of oxidative phosphorylation. The mode of action of cytochalasin-B may be conceived as restricting diffusion by means of macromolecular conformational changes occurring within the mitochondrial membranes. Electron micrographs of paired, 10 min mitochondrial incubations, in the presence and absence of 1.0 mM cytochalasin-B, clearly display a structural alteration within these organelles, such that upon the binding of cytochalasin-B the matrix area decreases and the inner membrane cristae develop condensed, tubular distortions.
Similar content being viewed by others
References
S. B. Carter,Endeavour,31 (1972) 77–82.
S. B. Carter,Nature,213 (1967) 261–264.
B. S. Spooner and N. K. Wessells,Proc. Natl. Acad. Sci. USA,66 (1970) 360–364.
H. Holtzer and J. Sanger,Dev. Biol.,27 (1972) 444–446.
T. E. Schroeder,Biol. Bull.,137 (1969) 443.
R. F. Kletzien, et al.,J. Biol. Chem.,247 (1972) 2964–2966.
B. S. Spooner, et al.J. Cell Biol.,49 (1971) 595.
N. K. Wessells, et al.,Science,171 (1971) 135–143.
R. D. Estensen and P. Plagemann,Proc. Natl. Acad. Sci. USA,69 (1972) 1430–1434.
R. F. Kletzien and J. F. Perdue,J. Biol. Chem.,248 (1973) 711–719.
R. D. Estensen,Proc. Soc. Exp. Biol. Med.,136 (1971) 1256–1260.
P. Plagemann and R. D. Estensen,J. Cell Biol.,55 (1972) 179–185.
W. J. Rutter, et al,Ann. Rev. Biochem.,42 (1973) 635–637.
P. S. Coleman,Biochim. Biophys. Acta,305 (1973) 179–184.
B. Chance and G. R. Williams,Adv. Enzymol.,17 (1956) 65–134.
C. H. Fiske and Y. SubbaRow,J. Biol. Chem.,66 (1925) 375–400.
E. C. Slater in “Regulation of Metabolic Processes in Mitochondria” (J. M. Tager, S. Papa, E. Quagliariello and E. C. Slater, eds.) Elsevier, Amsterdam and London. (1966) 166–179.
K. Van Dam and A. J. Meyer,Ann. Rev. Biochem. 40 (1971) 115–160.
C. P. Lee and L. Ernster,Eur. J. Biochem.,3 (1968) 391–400.
A. F. Miranda, et al.,J. Cell. Biol.,61 (1974) 481–500.
P. S. Coleman and N. S. Hermina, manuscript in preparation.
M. Klingenberg, et al., in FEBS Symposium, Vol. 17, “Mitochondria; Structure and Function”, L. Ernster and Z. Drahota, eds., Academic Press, London and New York. (1969) 59–77.
B. Scherer and M. Klingenberg,Biochemistry,13 (1973) 161–170
Author information
Authors and Affiliations
Additional information
These investigations were supported, in part, by a grant from The American Cancer Society, #IN-14-0.
Rights and permissions
About this article
Cite this article
Coleman, P.S., Hermina, N.S. The effects of cytochalasin-B on the membranes of enzymatically active mitochondria. J Bioenerg Biomembr 6, 193–204 (1974). https://doi.org/10.1007/BF01520861
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01520861