The presence of bestrophin-1 modulates the Ca2+ recruitment from Ca2+ stores in the ER.
Standard
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, Jahrgang 460, Nr. 1, 1, 2010, S. 163-175.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
Harvard
APA
Vancouver
Bibtex
}
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
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
M3 - SCORING: Zeitschriftenaufsatz
VL - 460
SP - 163
EP - 175
JO - PFLUG ARCH EUR J PHY
JF - PFLUG ARCH EUR J PHY
SN - 0031-6768
IS - 1
M1 - 1
ER -