Zur Kenntnis der Porine des Menschen. V. Die Plasmalemmständigkeit von „Porin 31HL“ ist keine Folge einer Zell-Transformation

König, Ulrike; Götz, H.; Walter, Götz; Babel, Dagmar; Hohmeier, Hans-Ewald; Thinnes, Friedrich P.; Hilschmann, Norbert

doi:10.1515/bchm3.1991.372.2.565

Cited by 21 publications

(5 citation statements)

References 7 publications

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“…These findings are in agreement with immunohistochemical data documenting HL-VDAC immunoreactivity in several peripheral tissues (19,25). Consistent with this notion, numerous reports have shown the presence of a largeconductance anion channel in a variety of nonnervous cellsi.e., skeletal muscle (23), apical membranes of Cl--secretory epithelium (26), and FO myeloma cells of mice (27).…”

Section: Gca Gtc Gtc Cgc Ccg Tat Act Gat Ctt Agc Aaa Tct Gcc Agg Gat Gtcsupporting

confidence: 92%

Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.

Dermietzel

Hwang

Buettner

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

137

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We have cloned a protein from bovine brain, brain-derived voltage-dependent anion channel 1 (BR1-VDAC), that is identical to a recently sequenced plasmalemmal-bound porin from human lymphocytes. mRNA hybridization indicates that BR1-VDAC is widely distributed throughout nervous and nonnervous tissues. In situ localization substantiated that the BR1-VDAC is associated with the plasmalemma of astrocytes. A monoclonal antibody that recognizes the N terminus of the BR1-VDAC protein completely blocks an astrocytic high-conductance anion channel that has electrophysiological similarities with the mitochondrial VDAC. Since the high-conductance anion channel in astrocytes has been shown to respond to hypoosmotic solutions, its molecular identification provides the basis for a better understanding of volume regulation in brain tissue.Astrocytes are involved in the local homeostatic balancing of the interstitial cerebral fluid in brain. The correct condition of the interstitial cerebral fluid is crucial for normal functioning of the neuronal network. Astrocytes have a complement of neurotransmitter receptors and ion channels that form the backbone of this regulative capacity. Although physiological data on the diverse astrocytic receptor and channel types have been collected (1, 2), knowledge of their molecular composition is rare. Determining the molecular mechanisms involved in the homeostatic balancing of the interstitial cerebral fluid is, therefore, indispensible for an understanding of the properties of astrocytes and their concerted action in maintaining normal brain function. Among the various channel types electrophysiologically characterized in astrocytes (2, 3) is a large-conductance anion channel, described in cultured astrocytes (4-6) and cultured rat Schwann cells (7) and reported (8) to be present in astrocytes of intact optic nerves. Jalonen et al. (9) (30-34 kDa) and are considered to provide the pathway for the movement of nucleotides and various other substances into a variety of metabolic pathways (11-13). Compared with the large-conductance anion channel of astrocytes, they exhibit almost identical basic channel properties. (i) Singlechannel conductance is roughly 450 pS. (ii) They show ion selectivity for Cl-in the high-conductance state, which occurs at 0 mV transmembrane voltage. (iii) They respond symmetrically with respect to gating properties; i.e., they are in the high-conductance state at 0 mV and close to lowconductance states in response to application ofboth positive and negative potentials (14). The characteristic voltagedependent gating and the anion preference at low potentials have led to the term VDAC (11,12).VDACs in eukaryotes have been considered to be localized exclusively in mitochondria. Recently, however, an apparently plasmalemmal VDAC (plm-VDAC) protein highly homologous to mitochondrial porins has been sequenced from a human lymphocyte cell line by Edman degradation (15). Subsequently, another VDAC-like protein was found to copurify with the plasmalemmal-bound centra...

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Section: Gca Gtc Gtc Cgc Ccg Tat Act Gat Ctt Agc Aaa Tct Gcc Agg Gat Gtcsupporting

confidence: 92%

Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.

Dermietzel

Hwang

Buettner

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

137

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“…Although there is some evidence of controversy, 12 subcellular distribution of VDACs in compartments other than mitochondria has been previously described. [13][14][15][16][17][18][19] These observations are consistent with the existence of multiple genes encoding VDAC isoforms in mammals with various cellular functions. In particular, the association of the mitochondrial receptor for benzodiazepines (mBzR) with the voltagedependent anion channel (VDAC) has been reported 20 and indicates a possible auxiliary role for VDAC as a putative drug binding protein.…”

Section: Discussionsupporting

confidence: 72%

Isolation of a novel human voltage-dependent anion channel gene

1998

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The voltage-dependent anion channel of the mitochondrial outer membrane (VDAC) is a small, abundant pore-forming protein found in the outer membranes of all eukaryotic mitochondria. The VDAC protein is believed to control the movement of adenine nucleotides through the outer membrane and to be the mitochondrial binding site for hexokinase and glycerol kinase. Two human VDAC cDNAs (HVDAC1 and HVDAC2) have been previously isolated and mapped on chromosome X and 21, respectively. Here, we report the isolation of a novel third human VDAC cDNA, corresponding to the mouse MVDAC3 gene. The expression of this gene in various tissues and its chromosomal localization by polymerase chain reaction (PCR) using a human/rodent somatic cell mapping panel and by fluorescence in situ hybridization is also presented.

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“…This finding was subsequently confirmed by a number of studies employing several cell lines or tissues (normal and cultured lymphocytes [15,16], epithelial cells [17], astrocytes [18], the post‐synaptic membrane fraction from brain [19]) and flow cytometry as well as EM immunogold labelling and immunofluorescence techniques. Immunofluorescence showed a punctuate staining distribution on the cell surface, compatible with a localization in membrane subdomains of the protein.…”

Section: The Discovery Of Vdac In Plasma Membranementioning

confidence: 69%

Voltage‐dependent anion‐selective channel (VDAC) in the plasma membrane

et al. 2010

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Edited by Sandro Sonnino Keywords:Voltage-dependent anion-selective channel, Mitochondria Plasma membrane NADH-oxidoreductase Dynamic membrane protein redistribution a b s t r a c t Voltage-dependent anion channels (VDACs) have originally been characterized as mitochondrial porins. Starting in the late 1980s, however, evidence began to accumulate that VDACs can also be expressed in plasma membranes. In this review, we briefly revisit the historical milestones in the discovery of plasma membrane-bound VDAC, and we critically analyze the evidence for VDAC plasma membrane localization obtained from various purification strategies and recently from plasma membrane proteomics studies. We discuss the possible biological function and relevance of VDAC in the plasma membrane and finally discuss a hypothetical model of how VDAC may be targeted to the plasma membrane.

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Zur Kenntnis der Porine des Menschen. V. Die Plasmalemmständigkeit von „Porin 31HL“ ist keine Folge einer Zell-Transformation

Cited by 21 publications

References 7 publications

Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.

Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.

Isolation of a novel human voltage-dependent anion channel gene

Voltage‐dependent anion‐selective channel (VDAC) in the plasma membrane

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