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Uptake of Exogenous Coenzyme Q by Caenorhabditis elegans
Author(s) -
Lunceford Adam L.,
Saiki Ryoichi,
Wong Tarra,
Furukawa Satoru,
Larsen Pamela L.,
Clarke Catherine F.
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a1346
Coenzyme Q (Q) functions as a component of the electron transport chain and as a lipid‐soluble antioxidant. Q can be synthesized de novo in the mitochondria or it can be derived from the diet. Both endogenous and exogenous forms of Q localize to the plasma and organellar membranes in cultured human cells. The current study investigates the ability of C. elegans to uptake Q from the surrounding medium and to transport it to the mitochondria. clk‐1 mutants fed a Q‐less diet arrest at the L2 larval stage and are sterile when grown from eggs. If the clk‐1 worms are allowed to develop to the dauer stage on a Q‐replete diet and are then allowed to recover on the Q‐less diet, they become sterile adults. A water‐soluble formulation of Q made by AQUANOVA® is able to rescue the clk‐1 growth arrest and sterility phenotypes of a Q‐less diet for both the worms developing from eggs and those developing from dauer larvae. However, the same formulation fails to rescue the Q‐less Escherichia coli for growth on succinate. A higher concentration of the AQUANOVA® Q is required to rescue clk‐1 mutants carrying the more severe allele than to rescue those carrying a point mutation. Quantification of Q present in lipid extracts from these animals shows that a significant amount of Q is present in the crude mitochondrial fraction. Future work will investigate the effect of this exogenous Q on the function of the aerobic electron transport complexes. This work was supported by NIA Grant AG19777 and by the Ellison Medical Foundation.