Abstract
Lipopolysaccharide (LPS) of a number of gram-negative bacteria affected mitochondrial respiration and phosphorylation when it was preincubated with the mitochondrial suspension. The structural part responsible for this activity of LPS is the lipid moiety (lipid A), because the lipid A prepared from either the LPS of Escherichia coli or the endotoxic glycolipid of a heptose-less mutant (R595) of Salmonella minnesota affected mitochondrial oxidative phosphorylation as did LPS, whereas the polysaccharide moiety was inactive. Preincubation of the mitochondrial suspension with lipid A resulted in (i) inhibition of respiration and accompanying phosphorylation in the presence of either succinate or a number of reduced nicotinamide adenine dinucleotide-linked substrates, (ii) decrease of respiratory control, (iii) inhibition of the transfer of electrons at coupling site II without decrease of efficiency of phosphorylation, and the uncoupling at coupling site III, and (iv) stimulation of adenosine triphosphatase and the inhibition of 2,4-dinitrophenol-induced adenosine triphosphatase.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BRADLEY L. B., JACOB M., JACOBS E. E., SANADI D. R. Uncoupling of oxidative phosphorylation by cadmium ion. J Biol Chem. 1956 Nov;223(1):147–156. [PubMed] [Google Scholar]
- Gmeiner J., Lüderitz O., Westphal O. Biochemical studies on lipopolysaccharides of Salmonella R mutants. 6. Investigations on the structure of the lipid A component. Eur J Biochem. 1969 Jan;7(3):370–379. doi: 10.1111/j.1432-1033.1969.tb19618.x. [DOI] [PubMed] [Google Scholar]
- Harris R. A., Harris D. L., Green D. E. Effect of Bordetella endotoxin upon mitochondrial respiration and energized processes. Arch Biochem Biophys. 1968 Oct;128(1):219–230. doi: 10.1016/0003-9861(68)90025-8. [DOI] [PubMed] [Google Scholar]
- Kasai N. Chemical studies on the lipid component of endotoxin, with special emphasis on its relation to biological activities. Ann N Y Acad Sci. 1966 Jun 30;133(2):486–507. doi: 10.1111/j.1749-6632.1966.tb52385.x. [DOI] [PubMed] [Google Scholar]
- Kato M., Asselineau J. Chemical structure and biochemical activity of cord factor analogs. 6,6'-Dimycoloyl sucrose and methyl 6-mycoloyl- -D-glucoside. Eur J Biochem. 1971 Oct 14;22(3):364–370. doi: 10.1111/j.1432-1033.1971.tb01553.x. [DOI] [PubMed] [Google Scholar]
- Kato M. Site II-specific inhibition of mitochondria oxidative phosphorylation by trehalose-6,6'-dimycolate (cord factor) of Mycobacterium tuberculosis. Arch Biochem Biophys. 1970 Oct;140(2):379–390. doi: 10.1016/0003-9861(70)90079-2. [DOI] [PubMed] [Google Scholar]
- Kato M. Site of action of the cord factor of Corynebacterium diphtheriae in mitochondria. J Bacteriol. 1971 Sep;107(3):746–752. doi: 10.1128/jb.107.3.746-752.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kato M. Studies of a biochemical lesion in experimental tuberculosis in mice. 8. Effect of derivatives and chemical analogues of cord factor on structure and function of mouse liver mitochondria. Am Rev Respir Dis. 1968 Oct;98(4):668–676. doi: 10.1164/arrd.1968.98.4.668. [DOI] [PubMed] [Google Scholar]
- Kato M. Studies of a biochemical lesion in experimental tuberculosis in mice. VII. Structural and functional damage in mouse liver mitochondria under the toxic action of cord factor. Am Rev Respir Dis. 1968 Aug;98(2):260–269. doi: 10.1164/arrd.1968.98.2.260. [DOI] [PubMed] [Google Scholar]
- Kim Y. B., Watson D. W. Biologically active endotoxins from Salmonella mutants deficient in O- and R-polysaccharides and heptose. J Bacteriol. 1967 Nov;94(5):1320–1326. doi: 10.1128/jb.94.5.1320-1326.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LARDY H. A., WELLMAN H. Oxidative phosphorylations; rôle of inorganic phosphate and acceptor systems in control of metabolic rates. J Biol Chem. 1952 Mar;195(1):215–224. [PubMed] [Google Scholar]
- Lüderitz O., Galanos C., Risse H. J., Ruschmann E., Schlecht S., Schmidt G., Schulte-Holthausen H., Wheat R., Westphal O., Schlosshardt J. Structural relationship of Salmonella O and R antigens. Ann N Y Acad Sci. 1966 Jun 30;133(2):349–374. doi: 10.1111/j.1749-6632.1966.tb52376.x. [DOI] [PubMed] [Google Scholar]
- NOLL H., BLOCH H., ASSELINEAU J., LEDERER E. The chemical structure of the cord factor of Mycobacterium tuberculosis. Biochim Biophys Acta. 1956 May;20(2):299–309. doi: 10.1016/0006-3002(56)90289-x. [DOI] [PubMed] [Google Scholar]
- Senn M., Ioneda T., Pudles J., Lederer E. Spectrométrie de masse de glycolipides. I. Structure du "cord factor" de Corynebacterium diphtheriae. Eur J Biochem. 1967 May;1(3):353–356. doi: 10.1111/j.1432-1033.1967.tb00081.x. [DOI] [PubMed] [Google Scholar]