Alternative mitochondrial respiratory chains from two crustaceans: Artemia franciscana nauplii and the white shrimp, Litopenaeus vannamei
Por:
Rodriguez-Armenta C., Uribe-Carvajal S., Rosas-Lemus M., Chiquete-Felix N., Huerta-Ocampo J.A., Muhlia-Almazan A.
Publicada:
1 abr 2018
Resumen:
Mitochondrial ATP is synthesized by coupling between the electron
transport chain and complex V. In contrast, physiological uncoupling of
these processes allows mitochondria to consume oxygen at high rates
without ATP synthesis. Such uncoupling mechanisms prevent reactive
oxygen species overproduction. One of these mechanisms are the
alternative redox enzymes from the mitochondrial respiratory chain,
which may help cells to maintain homeostasis under stress independently
of ATP synthesis. To date, no reports have been published on alternative
redox enzymes in crustaceans mitochondria. Specific inhibitors were used
to identify alternative redox enzymes in mitochondria isolated from
Artemia franciscana nauplii, and the white shrimp, Litopenaeus vannamei.
We report the presence of two alternative redox enzymes in the
respiratory chain of A. franciscana nauplii, whose isolated mitochondria
used glycerol-3-phosphate as a substrate, suggesting the existence of a
glycerol-3-phosphate dehydrogenase. In addition, cyanide and
octyl-gallate were necessary to fully inhibit this species'
mitochondrial oxygen consumption, suggesting an alternative oxidase is
present. The in-gel activity analysis confirmed that additional
mitochondrial redox proteins exist in A. franciscana. A mitochondrial
glycerol-3-phosphate dehydrogenase oxidase was identified by protein
sequencing as part of a branched respiratory chain, and an alternative
oxidase was also identified in this species by western blot. These
results indicate different adaptive mechanisms from artemia to face
environmental challenges related to the changing levels of oxygen
concentration in seawater through their life cycles. No alternative
redox enzymes were found in shrimp mitochondria, further efforts will
determine the existence of an uncoupling mechanism such as uncoupling
proteins.
Filiaciones:
Bioenergetics and Molecular Genetics Laboratory, Centro de Investigacion en Alimentacion y Desarrollo (CIAD), A. C. Carretera a Ejido La Victoria Km 0.6, PO Box. 1735, Hermosillo, Sonora, Mexico
Department of Molecular Genetics, Instituto de Fisiologia Celular, Universidad Nacional Autonoma de Mexico, Ciudad Universitaria, Box. 70-242, Mexico City, Mexico
Illinois Institute of Technology, Chicago, IL, United States
Protein Biochemistry Laboratory, CONACYT-Centro de Investigacion en Alimentacion y Desarrollo (CIAD), A. C. Carretera a Ejido La Victoria Km 0.6, PO Box. 1735, Hermosillo, Sonora, Mexico
Bioenergetics and Molecular Genetics Laboratory, Centro de Investigacion en Alimentacion y Desarrollo (CIAD), A. C. Carretera a Ejido La Victoria Km 0.6, PO Box. 1735, Hermosillo, Sonora 83000, Mexico
Protein Biochemistry Laboratory, CONACYT-Centro de Investigacion en Alimentacion y Desarrollo (CIAD), A. C. Carretera a Ejido La Victoria Km 0.6, PO Box. 1735, Hermosillo, Sonora 83000, Mexico
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