Skip to main content
SpringerLink
Log in

Effect of palmitoylcarnitine on mitochondrial activities

  • Published:
Planta Aims and scope Submit manuscript

Abstract

Mitochondria from pea (Pisum sativum L.) cotyledons and potato (Solanum tuberosum L.) tubers exhibited a palmitoyl carnitine-dependent, KCN-sensitive stimulation of the oxygen uptake measured in the presence of 0.2mmol·−1 malate (sparker malate), provided a certain concentration range of palmitoylcarnitine was observed. Above this concentration range, which was dependent on the bovine serum albumin (BSA) concentration of the reaction mixture, the mitochondrial oxygen uptake was inhibited by palmitoylcarnitine. Palmitoylcarnitine (racemate) and palmitoyl-l-carnitine were equally effective in stimulating/inhibiting mitochondrial oxygen uptake in the presence of sparker malate. The mitochondrial membrane potential generated in the presence of sparker malate was partially dissipated by palmitoyl-lcarnitine concentrations stimulating the mitochondrial oxygen uptake. The formation of acid-soluble radioactivity in reaction mixtures provided with [1-14C]palmitoyll-carnitine was considerably lower than that expected minimally if the palmitoyl-l-carnitine-stimulated oxygen uptake resulted from palmitoyl-l-carnitine oxidation sparked by malate. Palmitoylcarnitine concentrations resulting in stimulation of the mitochondrial oxygen uptake in the presence of sparker malate also led to a stimulation of succinate-cytochrome c reductase activity, as well as to an increase in the measurable activities of mitochondrial matrix enzymes, indicating loss of both mitochondrial integrity and mitochondrial enzyme latency in the presence of palmitoylcarnitine. Correspondingly, malate-dependent NADH formation was stimulated by palmitoylcarnitine. Neither NAD reduction nor oxygen uptake were observed when the mitochondria were provided with palmitoylcarnitine only. The oxygen uptake due to glycine oxidation by mitochondria from green sunflower (Helianthus annuus L.) cotyledons was affected by palmitoylcarnitine in a similar manner to the oxygen uptake of pea cotyledon and potato tuber mitochondria in the presence of sparker malate. The results lead to the conclusion that the palmitoylcarnitine-dependent stimulation of mitochondrial oxygen uptake observed in the presence of sparker malate results substantially from an enhanced malate oxidation due to the detergent effect of palmitoylcarnitine on the mitochondrial membranes, rather than from palmitoylcarnitine β-oxidation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

BSA:

bovine serum albumin

CCCP:

carbonylcyanide m-chlorophyenylhydrazone

References

  • Betsche, T., Eising, R. (1989) CO2-fixation, glycolate formation, and enzyme activities of photorespiration and photosynthesis during greening of sunflower cotyledons. J. Exp. Bot. 40, 1037–1043

    Google Scholar 

  • Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254

    Article  CAS  PubMed  Google Scholar 

  • Cooper, T.G., Beevers, H. (1969) β-Oxidation in glyoxysomes from castor bean endosperm. J. Biol. Chem. 244, 3514–3520

    Google Scholar 

  • Day, D.A., Neuburger, M., Douce, R. (1984) Activation of NAD-linked malic enzyme in intact plant mitochondria by exogenous coenzyme A. Arch. Biochem. Biophys. 231, 233–242

    Google Scholar 

  • Douce, R. (1985) Mitochondria in higher plants. Structure, function and biogenesis. Academic Press, Orlando

    Google Scholar 

  • Douce, R., Christensen, E.L., Bonner, W.D. (1972) Preparation of intact plant mitochondria. Biochim. Biophys. Acta 275, 148–160

    Google Scholar 

  • Edwards, G.E., Gardeström, P. (1987) Isolation of mitochondria from leaves of C3, C4, and crassulacean acid metabolism plants. Methods Enzymol. 148, 421–433

    Google Scholar 

  • Estabrook, R.W. (1967) Mitochondrial respiratory control and the polarographic measurement of ADP: O ratios. Methods Enzymol. 10, 41–47

    Google Scholar 

  • Gerbling, H., Gerhardt, B. (1987) Activation of fatty acids by non-glyoxysomal peroxisomes. Planta 171, 386–392

    Google Scholar 

  • Gerbling, H., Gerhardt, B. (1988) Carnitine acyltransferase activity of mitochondria from mung-bean hypocotyls. Planta 174, 90–93

    Google Scholar 

  • Gerhardt, B. (1983) Localization of β-oxidation enzymes in peroxisomes isolated from non-fatty plant tissues. Planta 159, 238–246

    Google Scholar 

  • Gerhardt, B. (1987) Peroxisomes and fatty acid degradation. Methods Enzymol. 148, 516–525

    Google Scholar 

  • Gerhardt, B. (1992) Fatty acid degradation in plants. Progr. Lipid Res. 31, 417–446

    Google Scholar 

  • Miernyk, J.A., Trelease, R.N. (1981) Control of enzyme activities in cotton cotyledons during maturation and germination. IV. β- Oxidation. Plant Physiol. 67, 341–346

    Google Scholar 

  • Moore, A.L., Bonner, W.D., Jr. (1982) Measurements of membrane potentials in plant mitochondria with the safranine method. Plant Physiol. 70, 1271–1276

    Google Scholar 

  • Neuburger, M., Journet, E.P., Bligny, R., Carde, J.P., Douce, R. (1982) Purification of plant mitochondria by isopycnic centrifugation in density gradients of Percoll. Arch. Biochem. Biophys. 217, 312–323

    Google Scholar 

  • Neuburger, M., Day, D.A., Douce, R. (1984) Transport of coenzyme A in plant mitochondria. Arch. Biochem. Biophys. 229, 253–258

    Google Scholar 

  • Pourfarzam, M., Bartlett, K. (1993) Skeletal muscle mitochondrial β-oxidation of dicarboxylates. Biochim. Biophys. Acta 1141, 81–89

    Google Scholar 

  • Thomas, D.R., Wood, C. (1986) The two β-oxidation sites in pea cotyledons. Carnitine palmitoyltransferase: Location and function in pea mitochondria. Planta 168, 261–266

    Google Scholar 

  • Thomas, D.R., Wood, C., Masterson, C. (1988) Long-chain acyl- CoA synthetase, carnitine and β-oxidation in the pea-seed mitochondria. Planta 173, 263–266

    Google Scholar 

  • Wedding, R.T. (1989) Malic enzymes of higher plants. Plant Physiol. 90, 367–371

    Google Scholar 

  • Wiskich, J.T., Bryce, J.H., Day, D.A., Dry, J.B. (1990) Evidence for metabolic domains within the matrix compartment of pea leaf mitochondria. Plant Physiol. 93, 611–616

    Google Scholar 

  • Wood, C., Noh Hj Jalil, M., McLaren, J., Yong, B.C.S., Ariffin, A., McNeil, P.M., Burgess, N., Thomas, D.R. (1984) Carnitine longchain acyltransferase and oxidation of palmitate, palmitoyl coenzyme A and palmitoylcarnitine by pea mitochondria preparations. Planta 161, 255–260

    Google Scholar 

  • Wood, C., Burgess, N., Thomas, D.R. (1986) The dual location of β-oxidation enzymes in germinating pea cotyledons. Planta 167, 54–57

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut für Botanik, Universität Münster, Schloßgarten 3, D-48149, Münster, Germany

    B. Gerhardt, K. Fischer & U. Maier

Authors
  1. B. Gerhardt
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. K. Fischer
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. U. Maier
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

The work was supported by the Deutsche Forschungsgemeinschaft.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gerhardt, B., Fischer, K. & Maier, U. Effect of palmitoylcarnitine on mitochondrial activities. Planta 196, 720–726 (1995). https://doi.org/10.1007/BF00197337

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00197337

Key words

Search

Navigation