Distinct Regulation of Brain Mitochondrial Carrier Protein-1 and Uncoupling Protein-2 Genes in the Rat Brain during Cold Exposure and Aging

2000 ◽  
Vol 278 (3) ◽  
pp. 691-697 ◽  
Author(s):  
Takafumi Mizuno ◽  
Tomoko Miura-Suzuki ◽  
Hitoshi Yamashita ◽  
Nozomu Mori
Keyword(s):  
Rat Brain ◽  
Cold Exposure ◽  
Uncoupling Protein ◽  
Uncoupling Protein 2 ◽  
Carrier Protein ◽  
Mitochondrial Carrier ◽  
Mitochondrial Carrier Protein

scholarly journals Not all mitochondrial carrier proteins support permeability transition pore formation: no involvement of uncoupling protein 1

2009 ◽  
Vol 30 (3) ◽  
pp. 187-192 ◽  
Author(s):  
Paul G. Crichton ◽  
Nadeene Parker ◽  
Antonio J. Vidal-Puig ◽  
Martin D. Brand
Keyword(s):  
Cyclosporin A ◽  
Pore Formation ◽  
Uncoupling Protein ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Protein Family ◽  
Carrier Protein ◽  
Uncoupling Protein 1 ◽  
Mitochondrial Carrier ◽  
Mitochondrial Carrier Protein

The mPTP (mitochondrial permeability transition pore) is a non-specific channel that is formed in the mitochondrial inner membrane in response to several stimuli, including elevated levels of matrix calcium. The pore is proposed to be composed of the ANT (adenine nucleotide translocase), voltage-dependent anion channel and cyclophilin D. Knockout studies, however, have demonstrated that ANT is not essential for permeability transition, which has led to the proposal that other members of the mitochondrial carrier protein family may be able to play a similar function to ANT in pore formation. To investigate this possibility, we have studied the permeability transition properties of BAT (brown adipose tissue) mitochondria in which levels of the mitochondrial carrier protein, UCP1 (uncoupling protein 1), can exceed those of ANT. Using an improved spectroscopic assay, we have quantified mPTP formation in de-energized mitochondria from wild-type and Ucp1KO (Ucp1-knockout) mice and assessed the dependence of pore formation on UCP1. When correctly normalized for differences in mitochondrial morphology, we find that calcium-induced mPTP activity is the same in both types of mitochondria, with similar sensitivity to GDP (~50% inhibited), although the portion sensitive to cyclosporin A is higher in mitochondria lacking UCP1 (~80% inhibited, compared with ~60% in mitochondria containing UCP1). We conclude that UCP1 is not a component of the cyclosporin A-sensitive mPTP in BAT and that playing a role in mPTP formation is not a general characteristic of the mitochondrial carrier protein family but is, more likely, restricted to specific members including ANT.

scholarly journals Role of YHM1, encoding a mitochondrial carrier protein, in iron distribution of yeast

2004 ◽  
Vol 378 (2) ◽  
pp. 599-607 ◽  
Author(s):  
Emmanuel LESUISSE ◽  
Elise R. LYVER ◽  
Simon A. B. KNIGHT ◽  
Andrew DANCIS
Keyword(s):  
Protein Family ◽  
Carrier Protein ◽  
Ferric Reductase ◽  
Mitochondrial Carrier ◽  
Mitochondrial Dna Damage ◽  
Cellular Iron ◽  
Mitochondrial Transporter ◽  
Large Protein Family ◽  
Mitochondrial Carrier Protein ◽  
Mitochondrial Carrier Proteins

Mitochondrial carrier proteins are a large protein family, consisting of 35 members in Saccharomyces cerevisiae. Members of this protein family have been shown to transport varied substrates from cytoplasm to mitochondria or mitochondria to cytoplasm, although many family members do not have assigned substrates. We speculated whether one or more of these transporters will play a role in iron metabolism. Haploid yeast strains each deleted for a single mitochondrial carrier protein were analysed for alterations in iron homoeostasis. The strain deleted for YHM1 was characterized by increased and misregulated surface ferric reductase and high-affinity ferrous transport activities. Siderophore uptake from different sources was also increased, and these effects were dependent on the AFT1 iron sensor regulator. Mutants of YHM1 converted into rho°, consistent with secondary mitochondrial DNA damage from mitochondrial iron accumulation. In fact, in the Δyhm1 mutant, iron was found to accumulate in mitochondria. The accumulated iron showed decreased availability for haem synthesis, measured in isolated mitochondria using endogenously available metals and added porphyrins. The phenotypes of Δyhm1 mutants indicate a role for this mitochondrial transporter in cellular iron homoeostasis.

scholarly journals Correction: Legionella pneumophila Secretes a Mitochondrial Carrier Protein during Infection

2012 ◽  
Vol 8 (1) ◽  
Author(s):  
Pavel Dolezal ◽  
Margareta Aili ◽  
Janette Tong ◽  
Jhih-Hang Jiang ◽  
Carlo M. T. Marobbio ◽  
...  
Keyword(s):  
Legionella Pneumophila ◽  
Carrier Protein ◽  
Mitochondrial Carrier ◽  
Mitochondrial Carrier Protein
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