Transport of proteins across mitochondrial membranes

Neupert, Walter

doi:10.1007/bf00180036

Cited by 18 publications

(5 citation statements)

References 70 publications

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“…BMCP1 was found in mitochondria but not cytosol in pure neuronal cultures, as well as neurons in mixed astrocyte–neuronal co‐cultures. Only the 36‐kDa BMCP1 protein band was present in mitochondria, indicating that BMCP1 does not undergo cleavage by the mitochondrial processing peptidase (MPP), which removes N‐terminal targeting sequences from proteins after import into mitochondria (Neupert 1994). Immunostaining of cortical neurons with both BMCP1 and cytochrome c also confirmed that BMCP1 co‐localized with mitochondrial cytochrome c (Fig.…”

Section: Resultsmentioning

confidence: 99%

BMCP1: a mitochondrial uncoupling protein in neurons which regulates mitochondrial function and oxidant production

Kim-Han

Reichert

Quick

et al. 2001

Journal of Neurochemistry

102

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Outside the nervous system, members of the mitochondrial uncoupling protein (UCP) family have been proposed to contribute to control of body temperature and energy metabolism, and regulation of mitochondrial production of reactive oxygen species (ROS). However, the function of brain mitochondrial carrier protein 1 (BMCP1), which is highly expressed in brain, remains to be determined. To study BMCP1 expression and function in the nervous system, a high-af®nity antibody to BMCP1 was generated and used to analyze tissue expression of BMCP1 protein in mouse. BMCP1 protein was highly expressed in heart and kidney, but not liver or lung. In the nervous system, BMCP1 was present in cortex, basal ganglia, substantia nigra, cerebellum, and spinal cord. Both BMCP1 mRNA and protein expression was almost exclusively neuronal. To study the effect of BMCP1 expression on mitochondrial function, neuronal (GT1-1) cell lines with stable overexpression of BMCP1 were generated. Transfected cells had higher State 4 respiration and lower mitochondrial membrane potential (c m ), consistent with greater mitochondrial uncoupling. BMCP1 expression also decreased mitochondrial production of ROS. These data suggest that BMCP1 can modify mitochondrial respiratory ef®ciency and mitochondrial oxidant production, and raise the possibility that BMCP1 might alter the vulnerability of brain to both acute injury and to neurodegenerative conditions.

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Section: Resultsmentioning

confidence: 99%

BMCP1: a mitochondrial uncoupling protein in neurons which regulates mitochondrial function and oxidant production

Kim-Han

Reichert

Quick

et al. 2001

Journal of Neurochemistry

102

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“…2). These features are common to most mitochondrial targeting sequences [31], and an algorithm‐based analysis (http://psort.nibb.ac.jp/) indicated mitochondrial matrix localization. In addition, a motif for cleavage by the two‐protease model [32] is found in this region between Gly33 and Gln34 (Fig.…”

Section: Resultsmentioning

confidence: 99%

Human mitochondrial thioredoxin reductase

Miranda‐Vizuete

Damdimopoulos

Pedrajas

et al. 1999

European Journal of Biochemistry

169

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We have isolated a 1918-bp cDNA from a human adrenal cDNA library which encodes a novel thioredoxin reductase (TrxR2) of 521 amino acid residues with a calculated molecular mass of 56.2 kDa. It is highly homologous to the previously described cytosolic enzyme (TrxR1), including the conserved active site CVNVGC and the FAD-binding and NADPH-binding domains. However, human TrxR2 differs from human TrxR1 by the presence of a 33-amino acid extension at the N-terminus which has properties characteristic of a mitochondrial translocation signal. Northern-blot analysis identified one mRNA species of 2.2 kb with highest expression in prostate, testis and liver. We expressed human TrxR2 as a fusion protein with green fluorescent protein and showed that in vivo it is localized in mitochondria. Removal of the mitochondrial targeting sequence abolishes the mitochondrial translocation. Finally, we determined the genomic organization of the human TrxR2 gene, which consists of 18 exons spanning about 67 kb, and its chromosomal localization at position 22q11.2.

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“…Lipid vesicles mimic the biological membranes (21) and earlier studies have shown that although the apocytochrome c can pass through the vesicles (22), the holoprotein can be encapsulated inside the lipid vesicles for several hours (12,22). We have demonstrated that small concentrations of the reactive oxygen species such as H 2 O 2 and O 2 Ϫ cause release of the protein from the vesicle.…”

mentioning

confidence: 84%