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The presence of bestrophin-1 modulates the $Ca^{2+}$ recruitment from $Ca^{2+}$ stores in the ER

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Neussert, Rudgar Müller, Claudia Milenkovic, Vladimir M. Strauss, Olaf
Description	Country affiliation: Germany Author Affiliation: Neussert R ( Experimental Eye Research, Eye Hospital, University Hospital Hamburg-Eppendorf, Hamburg, Germany.)
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 β-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.
File Format	HTM / HTML
ISSN	00316768
Issue Number	1
Volume Number	460
e-ISSN	14322013
Journal	Pflügers Archiv - European Journal of Physiology
Language	English
Publisher	Springer
Publisher Date	2010-06-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Physiology Calcium Signaling Calcium Metabolism Chlorides Endoplasmic Reticulum Eye Proteins Retinal Pigment Epithelium Adenosine Triphosphate Animals Drug Effects Calcium-transporting Atpases Antagonists & Inhibitors Cells, Cultured Centrifugation, Density Gradient Cytosol Enzyme Activation Enzyme Inhibitors Pharmacology Genetics Homeostasis Immunohistochemistry Ion Channels Macrolides Mice Mice, Knockout Microscopy, Fluorescence Swine Thapsigargin Time Factors Type C Phospholipases Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Clinical Biochemistry

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