VDAC/porin is present in sarcoplasmic reticulum from skeletal muscle

Shoshan‐Barmatz, Varda; Hadad, Nurith; Feng, Wei; Shafir, Iris; Orr, Irit; Varsányi, Magdolna; Heilmeyer, Ludwig

doi:10.1016/0014-5793(96)00442-5

Cited by 118 publications

(92 citation statements)

References 47 publications

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“…[29][30][31] Such modification was shown to inhibit HK-I binding, 32 and to induce VDAC channel closure. 30,31 Thus, it is expected that the HK-I binding activity of VDAC mutated at Glu72 would be reduced or eliminated. Therefore, binding of HK-I to mitochondria isolated from yeast expressing native or E72Q-mVDAC1 was compared (Figure 1a).…”

Section: Hk-i Binds To Yeast Mitochondria Expressing Native But Not Ementioning

confidence: 99%

“…EGTA, EDTA), the ligation center for divalent cations binds through a carboxylate group or neutral oxygen center. DCCD, which specifically reacts with carboxyl groups, has been shown to label specifically VDAC [29][30][31][32] and inhibit its channel activity. 30,31 De Pinto et al 29 have identified Glu72 as the DCCD binding amino acid in VDAC.…”

Section: Vdac Divalent Cation Binding Sitesmentioning

confidence: 99%

“…DCCD, which specifically reacts with carboxyl groups, has been shown to label specifically VDAC [29][30][31][32] and inhibit its channel activity. 30,31 De Pinto et al 29 have identified Glu72 as the DCCD binding amino acid in VDAC. Our results show that replacement of Glu72 by glutamine eliminated RuR and Ru360 inhibition of VDAC channel activity ( Figure 2) and also HK-I binding to isolated mitochondria (Figure 1).…”

Section: Vdac Divalent Cation Binding Sitesmentioning

confidence: 99%

“…We have shown that HK-I and RuR directly interact with purified VDAC reconstituted into a PLB to induce channel closure. 7,10,12,25,31 Thus, it is probable that the effects of these reagents in preventing cell death are related to their interaction with VDAC. These reagents, however, are not specific for VDAC, and thus either the reagent or overexpression of HK-I could act via perturbation of cell physiology via other, VDAC-independent, mechanisms.…”

Section: A Single Amino-acid Mutation In Vdac1 Prevents Hk-i-and Rur-mentioning

confidence: 99%

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The voltage-dependent anion channel-1 modulates apoptotic cell death

et al. 2005

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The role of the voltage-dependent anion channel (VDAC) in cell death was investigated using the expression of native and mutated murine VDAC1 in U-937 cells and VDAC inhibitors. Glutamate 72 in VDAC1, shown previously to bind dicyclohexylcarbodiimide (DCCD), which inhibits hexokinase isoform I (HK-I) binding to mitochondria, was mutated to glutamine. Binding of HK-I to mitochondria expressing E72Q-mVDAC1, as compared to native VDAC1, was decreased by B70% and rendered insensitive to DCCD. HK-I and ruthenium red (RuR) reduced the VDAC1 conductance but not that of E72Q-mVDAC1. Overexpression of native or E72Q-mVDAC1 in U-937 cells induced apoptotic cell death (80%). RuR or overexpression of HK-I prevented this apoptosis in cells expressing native but not E72Q-mVDAC1. Thus, a single amino-acid mutation in VDAC prevented HK-I-or RuR-mediated protection against apoptosis, suggesting the direct VDAC regulation of the mitochondria-mediated apoptotic pathway and that the protective effects of RuR and HK-I rely on their binding to VDAC.

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Section: Hk-i Binds To Yeast Mitochondria Expressing Native But Not Ementioning

confidence: 99%

Section: Vdac Divalent Cation Binding Sitesmentioning

confidence: 99%

Section: Vdac Divalent Cation Binding Sitesmentioning

confidence: 99%

Section: A Single Amino-acid Mutation In Vdac1 Prevents Hk-i-and Rur-mentioning

confidence: 99%

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The voltage-dependent anion channel-1 modulates apoptotic cell death

et al. 2005

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“…It is now recognized that VDAC is involved in many physiological and pathophysiological processes, including energy metabolism and cell apoptosis [6,[9][10][11]. Furthermore, VDAC is found in the plasma membrane or other non-mitochondrial cellular components, which implies that VDAC has novel functions [12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Analysis and difference of voltage-dependent anion channel mRNA in ejaculated spermatozoa from normozoospermic fertile donors and infertile patients with idiopathic asthenozoospermia

Liu

Wang

et al. 2010

J Assist Reprod Genet

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Purpose To analyze the abundance and difference of voltagedependent anion channel (VDAC) mRNA in ejaculated spermatozoa from normozoospermic fertile donors and infertile patients with idiopathic asthenozoospermia. Methods High motile and low motile spermatozoa were separated respectively from ejaculates of 36 donors and 40 patients using a discontinuous Percoll gradient centrifugation. Real-Time PCR was performed to detect mRNA abundance and difference of three VDAC subtypes between two groups with different sperm motility.Results Real-Time PCR demonstrated that three VDAC mRNAs were present in mature spermatozoa. The VDAC2 mRNA level in ejaculated spermatozoa of patients was significantly higher than that of donors. No significant differences of VDAC1 and VDAC3 mRNA levels were found between two groups. Conclusion The high abundance of VDAC2 mRNA seemed to have a positive correlation with low sperm motility. The abnormal expression of VDAC might be related to male infertility with idiopathic asthenozoospermia.

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Proteome analysis of matrix vesicles isolated from femurs of chicken embryo

et al. 2007

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Matrix vesicles (MVs) are extracellular organelles that initiate mineral formation, accumulating inorganic phosphate (P(i)) and calcium leading to the formation of hydroxyapatite (HA) crystals, the main mineral component of bones. MVs are produced during bone formation, as well as during the endochondral calcification of cartilage. MVs are released into the extracellular matrix from osseous cells such as osteoblasts and hypertrophic chondrocytes. In this report, using 1-D SDS-PAGE, in-gel tryptic digestion and an LC-MS-MS/MS protein identification protocol, we characterized the proteome of MVs isolated from chicken embryo (Gallus gallus) bones and cartilage. We identified 126 gene products, including proteins related to the extracellular matrix and ion transport, as well as enzymes, cytoskeletal, and regulatory proteins. Among the proteins recognized for the first time in MVs were aquaporin 1, annexin A1 (AnxA1), AnxA11, glycoprotein HT7, G(i) protein alpha2, and scavenger receptor type B. The pathways for targeting the identified proteins into MVs and their particular functions in the biomineralization process are discussed. Obtaining a knowledge of the functions and roles of these proteins during embryonic mineralization is a prerequisite for the overall understanding of the initial mineral formation mechanisms.

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VDAC/porin is present in sarcoplasmic reticulum from skeletal muscle

Cited by 118 publications

References 47 publications

The voltage-dependent anion channel-1 modulates apoptotic cell death

The voltage-dependent anion channel-1 modulates apoptotic cell death

Analysis and difference of voltage-dependent anion channel mRNA in ejaculated spermatozoa from normozoospermic fertile donors and infertile patients with idiopathic asthenozoospermia

Proteome analysis of matrix vesicles isolated from femurs of chicken embryo

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