• Corpus ID: 33631003

Carnitine transport in rat heart slices: I. The action of thiol reagents on the acetylcarnitine/carnitine exchange.

  title={Carnitine transport in rat heart slices: I. The action of thiol reagents on the acetylcarnitine/carnitine exchange.},
  author={Lodovico Sartorelli and M. Ciman and Noris Siliprandi},
  journal={The Italian journal of biochemistry},
  volume={34 4},
Rat heart slices show a permeability barrier that can be crossed by carnitine but not by sucrose and inulin. The integrity of thiol groups of heart cell membrane is essential for the uptake of carnitine. N-ethylmaleimide inhibits the transport into heart slices which is insensitive to Mersalyl. On the contrary both N-ethylmaleimide and Mersalyl inhibit acetyl carnitine/carnitine exchange. The amount of thiol groups titrated by the above reagents are related to the extent of exchange inhibition. 

Myocardial carnitine transport.

It is demonstrated that in heart slices carnitine-deoxycarnitine exchange, occurring in a close one to one ratio, is (i) insensitive to both glycolysis and oxidative phosphorylation inhibitors and (ii) sensitive to thiol reagents, such as NEM and Mersalyl.

Carnitine transport in volume-overloaded rat hearts

Carnitine concentration in tissue is generally related to mitochondrial volume-density and ability to oxidize fatty acids. The highest tissue carnitine has been detected in ventricular myocardium

OCTN2 is associated with carnitine transport capacity of rat skeletal muscles

It is tested the hypothesis that OCTN2 is expressed at higher levels in oxidative muscles than in other muscles, and that the carnitine uptake capacity of skeletal muscles depends on the amount of OCTn2.

Carnitine: metabolism and clinical chemistry.

Characterization of L-carnitine transport into rat skeletal muscle plasma membrane vesicles.

Transport of L-carnitine into skeletal muscle was investigated using rat sarcolemmal membrane vesicles and found the existence of more than one carnitine carrier in skeletal muscle suggests potential-dependent transport.

Transport and Function of Carnitine: Relevance to Carnitine‐Deficient Diseases

  • N. Siliprandi
  • Biology, Medicine
    Annals of the New York Academy of Sciences
  • 1986
This is the best known primary carnitine deficiency, first described by Engel and Angelhi* and so far recognized in about 30 patients. It is characterized by a pronounced weakness of muscles, coupled

Carnitine and carnitine esters in mitochondrial metabolism and function

Carnitine exerts a role in any CoA-dependent process and the modulation of the ratio between free CoA (CoASH) and esterified CoA can be seen as the main task accomplished by carnitine.

Carnitine and Mitochondrial Dysfunction

Since ATP is not cell permeant, a decrease in its content cannot be restored by extracellular sources. Thus, in every cell ATP consumption has to be matched by comparable rates of ATP production. By

Effect of exogenous carnitine on carnitine homeostasis in the rat.

Supplemental carnitine and exercise.

  • E. Brass
  • Biology, Medicine
    The American journal of clinical nutrition
  • 2000
Clinical trials integrating physiologic, biochemical, and pharmacologic assessments are needed to definitively clarify any effects of carnitine on exercise performance in healthy persons.