Voltage-dependent anion channels 1 and 2 are expressed in porcine oocytes

Cassará, M. Carolina; Menzel, Viviana A.; Hinsch, Klaus‐Dieter; Wrenzycki, C.; Hinsch, Elvira

doi:10.1042/bsr20090088

Cited by 13 publications

(9 citation statements)

References 43 publications

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“…VDAC1, an induced protein, is required for the maintenance of mitochondrial osmotic stability and NADH membrane permeability 63. VDAC subtypes are also expressed in mammalian oocytes 64. Finally, three gel mobility isoforms of BFR1 were identified, which were all repressed at late time points.…”

Section: Resultsmentioning

confidence: 99%

2‐D DIGE analysis of the budding yeast pH 6–11 proteome in meiosis

et al. 2010

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Meiosis is the cell division that generates haploid gametes from diploid precursors. To provide insight into the functional proteome of budding yeast during meiosis, a 2-D DIGE kinetic approach was used to study proteins in the pH 6-11 range. Nearly 600 protein spots were visualised and 79 spots exhibited statistically significant changes in abundance as cells progressed through meiosis. Expression changes of up to 41-fold were detected and protein sequence information was obtained for 48 spots. Single protein identifications were obtained for 21 spots including different gel mobility forms of 5 proteins. A large number of post-translational events are suggested for these proteins, including processing, modification and import. The data are incorporated into an online 2-DE map of meiotic proteins in budding yeast, which extends our initial DIGE investigation of proteins in the pH 4-7 range. Together, the analyses provide peptide sequence data for 84 protein spots, including 50 single-protein identifications and gel mobility isoforms of 8 proteins. The largest classes of identified proteins include carbon metabolism, protein catabolism, protein folding, protein synthesis and the oxidative stress response. A number of the corresponding genes are required for yeast meiosis and recent studies have identified similar classes of proteins expressed during mammalian meiosis. This proteomic investigation and the resulting protein reference map make an important contribution towards a more detailed molecular view of yeast meiosis.

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Section: Resultsmentioning

confidence: 99%

2‐D DIGE analysis of the budding yeast pH 6–11 proteome in meiosis

et al. 2010

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“…VDACs (voltage-dependent anion channels) are a widespread on the outer mitochondrial membranes of most organisms (De Pinto et al, 2003). The OMM functions as a link between mitochondrial metabolism and the rest of the cell (Cassara et al, 2009). Some other reports also demonstrated the presence of VDACs in the plasma membrane and other organelles (Bathori et al, 2000;Shoshan-Barmatz et al, 2006).…”

Section: Higher [Ca 2+ ] M Related To the Distribution Of Micumentioning

confidence: 90%

Mitochondrial Ca2 + Is Related to Mitochondrial Activity and Dynamic Events in Mouse Oocytes

Wang

Meng

et al. 2020

Front. Cell Dev. Biol.

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Mitochondrial energy insufficiency is strongly associated with oocyte activation disorders. Ca 2+ , especially that in the mitochondrial matrix, plays a pivotal role in mitochondrial energy supplementation, but the underlying mechanisms are still only poorly understood. An encoded mitochondrial matrix Ca 2+ probe (Mt-GCaMP6s) was introduced to observe mitochondrial Ca 2+ ([Ca 2+ ] m) dynamic changes during oocyte maturation and activation. We found that active mitochondria surrounding the nucleus showed a higher [Ca 2+ ] m than those distributed in the cortex during oocyte maturation. During oocyte partheno-activation, the patterns of Ca 2+ dynamic changes were synchronous in the cytoplasm and mitochondria. Such higher concentration of mitochondrial matrix Ca 2+ was closely related to the distribution of mitochondrial calcium uptake (MICU) protein. We further showed that higher [Ca 2+ ] m mitochondria around the chromosomes in oocytes might have a potential role in stimulating mitochondrial energy for calmodulin-responsive oocyte spindle formation, while synchronizing Ca 2+ functions in the cytoplasm and nuclear area are important for oocyte activation.

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“…Caveolae and caveolae-like domains were shown to contain VDAC (Bathori et al, 1999). The extra-mitochondrial localization of VDAC in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum, has been reported (Hinsch et al, 2004; Triphan et al, 2008; Cassara et al, 2010). VDAC2 was shown to be present in the membrane components of human spermatozoa (Liu et al, 2011).…”

Section: Vdac: Isoforms Location and Transport Activitymentioning

confidence: 99%

VDAC1: from structure to cancer therapy

2012

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Here, we review current evidence pointing to the function of VDAC1 in cell life and death, and highlight these functions in relation to cancer. Found at the outer mitochondrial membrane, VDAC1 assumes a crucial position in the cell, controlling the metabolic cross-talk between mitochondria and the rest of the cell. Moreover, its location at the boundary between the mitochondria and the cytosol enables VDAC1 to interact with proteins that mediate and regulate the integration of mitochondrial functions with other cellular activities. As a metabolite transporter, VDAC1 contributes to the metabolic phenotype of cancer cells. This is reflected by VDAC1 over-expression in many cancer types, and by inhibition of tumor development upon silencing VDAC1 expression. Along with regulating cellular energy production and metabolism, VDAC1 is also a key protein in mitochondria-mediated apoptosis, participating in the release of apoptotic proteins and interacting with anti-apoptotic proteins. The involvement of VDAC1 in the release of apoptotic proteins located in the inter-membranal space is discussed, as is VDAC1 oligomerization as an important step in apoptosis induction. VDAC also serves as an anchor point for mitochondria-interacting proteins, some of which are also highly expressed in many cancers, such as hexokinase (HK), Bcl2, and Bcl-xL. By binding to VDAC, HK provides both metabolic benefit and apoptosis-suppressive capacity that offers the cell a proliferative advantage and increases its resistance to chemotherapy. VDAC1-based peptides that bind specifically to HK, Bcl2, or Bcl-xL abolished the cell’s abilities to bypass the apoptotic pathway. Moreover, these peptides promote cell death in a panel of genetically characterized cell lines derived from different human cancers. These and other functions point to VDAC1 as a rational target for the development of a new generation of therapeutics.

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Voltage-dependent anion channels 1 and 2 are expressed in porcine oocytes

Cited by 13 publications

References 43 publications

2‐D DIGE analysis of the budding yeast pH 6–11 proteome in meiosis

2‐D DIGE analysis of the budding yeast pH 6–11 proteome in meiosis

Mitochondrial Ca2 + Is Related to Mitochondrial Activity and Dynamic Events in Mouse Oocytes

VDAC1: from structure to cancer therapy

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