The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER.

Rudgar Neussert; Claudia Müller; Vladimir M Milenkovic; Olaf Strauss

The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER.

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The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER. / Neussert, Rudgar; Müller, Claudia; Milenkovic, Vladimir M; Strauss, Olaf.

In: PFLUG ARCH EUR J PHY, Vol. 460, No. 1, 1, 2010, p. 163-175.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Neussert, R, Müller, C, Milenkovic, VM & Strauss, O 2010, 'The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER.', PFLUG ARCH EUR J PHY, vol. 460, no. 1, 1, pp. 163-175. <http://www.ncbi.nlm.nih.gov/pubmed/20411394?dopt=Citation>

APA

Neussert, R., Müller, C., Milenkovic, V. M., & Strauss, O. (2010). The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER. PFLUG ARCH EUR J PHY, 460(1), 163-175. [1]. http://www.ncbi.nlm.nih.gov/pubmed/20411394?dopt=Citation

Vancouver

Neussert R, Müller C, Milenkovic VM, Strauss O. The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER. PFLUG ARCH EUR J PHY. 2010;460(1):163-175. 1.

Bibtex

@article{bd48e8ee79af4ef782e08dacc31693db,

title = "The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER.",

abstract = "Bestrophin-1, mainly analyzed in overexpression experiments, functions as Ca(2+)-dependent Cl(-) channel. Analysis of endogenously expressed bestrophin-1 suggested an influence on intracellular Ca(2+). The aim of the study is to analyze the influence of endogenously expressed bestrophin-1 on Ca(2+) homeostasis. Primary cultures of retinal pigment epithelial (RPE) cells were established from wild-type and bestrophin-1-deficient mice. Intracellular free Ca(2+) ([Ca(2+)](i)) was recorded by Ca(2+) imaging; through immunocytochemistry and differential centrifugation, subcellular localization of bestrophin-1 was analyzed. RPE cells of bestrophin-1-deficient mice showed higher levels of resting [Ca(2+)](i) than cells from wild-type mice. In cells from knockout mice and wild-type mice, ATP led to increases in [Ca(2+)](i) subsequent to phospholipase C activation. ATP-induced Ca(2+) in bestrophin-1-deficient mice rose faster and decayed slower. In cells from wild-type mice, ATP led to [Ca(2+)](i) increase via depletion of Ca(2+) from thapsigargin-sensitive stores. In cells from bestrophin-1-deficient mice, ATP-dependent increase in [Ca(2+)](i) resulted in 40% of cells from depletion of bafilomycin-sensitive and in 60% from thapsigargin-sensitive Ca(2+) stores. After differential centrifugation, bestrophin-1 was found in fractions enriched of ClC-3 Cl channel and myosin-7A. Co-localization analysis of bestrophin-1, with beta-catenin or pan-cadherin, in fresh sections of porcine retina, revealed bestrophin-1 in the basolateral membrane. A portion of endogenously expressed bestrophin-1,localized in the endoplasmic reticulum, influenced uptake of Ca(2+) into Ca(2+) stores. Therefore, bestrophin-1 possibly conducts Cl(-) as counter ion for Ca(2+) uptake into cytosolic Ca(2+) stores.",

keywords = "Animals, Immunohistochemistry, Time Factors, inhibitors, Cells, Cultured, Mice, Mice, Knockout, Cytosol metabolism, Microscopy, Fluorescence, Calcium metabolism, Enzyme Activation, Enzyme Inhibitors pharmacology, Retinal Pigment Epithelium drug effects, Adenosine Triphosphate metabolism, Calcium Signaling drug effects, Calcium-Transporting ATPases antagonists, Centrifugation, Density Gradient, Chlorides metabolism, Endoplasmic Reticulum drug effects, Eye Proteins genetics, Homeostasis, Macrolides pharmacology, Swine, Thapsigargin pharmacology, Type C Phospholipases metabolism, Animals, Immunohistochemistry, Time Factors, inhibitors, Cells, Cultured, Mice, Mice, Knockout, Cytosol metabolism, Microscopy, Fluorescence, Calcium metabolism, Enzyme Activation, Enzyme Inhibitors pharmacology, Retinal Pigment Epithelium drug effects, Adenosine Triphosphate metabolism, Calcium Signaling drug effects, Calcium-Transporting ATPases antagonists, Centrifugation, Density Gradient, Chlorides metabolism, Endoplasmic Reticulum drug effects, Eye Proteins genetics, Homeostasis, Macrolides pharmacology, Swine, Thapsigargin pharmacology, Type C Phospholipases metabolism",

author = "Rudgar Neussert and Claudia M{\"u}ller and Milenkovic, {Vladimir M} and Olaf Strauss",

year = "2010",

language = "Deutsch",

volume = "460",

pages = "163--175",

journal = "PFLUG ARCH EUR J PHY",

issn = "0031-6768",

publisher = "Springer",

number = "1",

}

RIS

TY - JOUR

T1 - The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER.

AU - Neussert, Rudgar

AU - Müller, Claudia

AU - Milenkovic, Vladimir M

AU - Strauss, Olaf

PY - 2010

Y1 - 2010

N2 - Bestrophin-1, mainly analyzed in overexpression experiments, functions as Ca(2+)-dependent Cl(-) channel. Analysis of endogenously expressed bestrophin-1 suggested an influence on intracellular Ca(2+). The aim of the study is to analyze the influence of endogenously expressed bestrophin-1 on Ca(2+) homeostasis. Primary cultures of retinal pigment epithelial (RPE) cells were established from wild-type and bestrophin-1-deficient mice. Intracellular free Ca(2+) ([Ca(2+)](i)) was recorded by Ca(2+) imaging; through immunocytochemistry and differential centrifugation, subcellular localization of bestrophin-1 was analyzed. RPE cells of bestrophin-1-deficient mice showed higher levels of resting [Ca(2+)](i) than cells from wild-type mice. In cells from knockout mice and wild-type mice, ATP led to increases in [Ca(2+)](i) subsequent to phospholipase C activation. ATP-induced Ca(2+) in bestrophin-1-deficient mice rose faster and decayed slower. In cells from wild-type mice, ATP led to [Ca(2+)](i) increase via depletion of Ca(2+) from thapsigargin-sensitive stores. In cells from bestrophin-1-deficient mice, ATP-dependent increase in [Ca(2+)](i) resulted in 40% of cells from depletion of bafilomycin-sensitive and in 60% from thapsigargin-sensitive Ca(2+) stores. After differential centrifugation, bestrophin-1 was found in fractions enriched of ClC-3 Cl channel and myosin-7A. Co-localization analysis of bestrophin-1, with beta-catenin or pan-cadherin, in fresh sections of porcine retina, revealed bestrophin-1 in the basolateral membrane. A portion of endogenously expressed bestrophin-1,localized in the endoplasmic reticulum, influenced uptake of Ca(2+) into Ca(2+) stores. Therefore, bestrophin-1 possibly conducts Cl(-) as counter ion for Ca(2+) uptake into cytosolic Ca(2+) stores.

AB - Bestrophin-1, mainly analyzed in overexpression experiments, functions as Ca(2+)-dependent Cl(-) channel. Analysis of endogenously expressed bestrophin-1 suggested an influence on intracellular Ca(2+). The aim of the study is to analyze the influence of endogenously expressed bestrophin-1 on Ca(2+) homeostasis. Primary cultures of retinal pigment epithelial (RPE) cells were established from wild-type and bestrophin-1-deficient mice. Intracellular free Ca(2+) ([Ca(2+)](i)) was recorded by Ca(2+) imaging; through immunocytochemistry and differential centrifugation, subcellular localization of bestrophin-1 was analyzed. RPE cells of bestrophin-1-deficient mice showed higher levels of resting [Ca(2+)](i) than cells from wild-type mice. In cells from knockout mice and wild-type mice, ATP led to increases in [Ca(2+)](i) subsequent to phospholipase C activation. ATP-induced Ca(2+) in bestrophin-1-deficient mice rose faster and decayed slower. In cells from wild-type mice, ATP led to [Ca(2+)](i) increase via depletion of Ca(2+) from thapsigargin-sensitive stores. In cells from bestrophin-1-deficient mice, ATP-dependent increase in [Ca(2+)](i) resulted in 40% of cells from depletion of bafilomycin-sensitive and in 60% from thapsigargin-sensitive Ca(2+) stores. After differential centrifugation, bestrophin-1 was found in fractions enriched of ClC-3 Cl channel and myosin-7A. Co-localization analysis of bestrophin-1, with beta-catenin or pan-cadherin, in fresh sections of porcine retina, revealed bestrophin-1 in the basolateral membrane. A portion of endogenously expressed bestrophin-1,localized in the endoplasmic reticulum, influenced uptake of Ca(2+) into Ca(2+) stores. Therefore, bestrophin-1 possibly conducts Cl(-) as counter ion for Ca(2+) uptake into cytosolic Ca(2+) stores.

KW - Animals

KW - Immunohistochemistry

KW - Time Factors

KW - inhibitors

KW - Cells, Cultured

KW - Mice

KW - Mice, Knockout

KW - Cytosol metabolism

KW - Microscopy, Fluorescence

KW - Calcium metabolism

KW - Enzyme Activation

KW - Enzyme Inhibitors pharmacology

KW - Retinal Pigment Epithelium drug effects

KW - Adenosine Triphosphate metabolism

KW - Calcium Signaling drug effects

KW - Calcium-Transporting ATPases antagonists

KW - Centrifugation, Density Gradient

KW - Chlorides metabolism

KW - Endoplasmic Reticulum drug effects

KW - Eye Proteins genetics

KW - Homeostasis

KW - Macrolides pharmacology

KW - Swine

KW - Thapsigargin pharmacology

KW - Type C Phospholipases metabolism