Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal Myofibers

We examined the distribution of selected raft proteins on the sarcolemma of skeletal myofibers and the role of cholesterol environment in the distribution. Immunofluorescence staining showed that flotillin-1 and influenza hemagglutinin exhibited rafts that located in the domains deficient of the d...

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Main Authors: Mika Kaakinen, Tuula Kaisto, Paavo Rahkila, Kalervo Metsikkö
Format: Article
Language:English
Published: Hindawi Limited 2012-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2012/497572
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spelling doaj-374ff7681d474014a1b9f2d4901b82352020-11-24T21:48:21ZengHindawi LimitedBiochemistry Research International2090-22472090-22552012-01-01201210.1155/2012/497572497572Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal MyofibersMika Kaakinen0Tuula Kaisto1Paavo Rahkila2Kalervo Metsikkö3Department of Anatomy and Cell Biology, Institute of Biomedicine, University of Oulu, P.O. Box 5000, Aapistie 7, 90014 Oulu, FinlandDepartment of Anatomy and Cell Biology, Institute of Biomedicine, University of Oulu, P.O. Box 5000, Aapistie 7, 90014 Oulu, FinlandDepartment of Health Sciences, University of Jyväskylä, P.O. Box 35, 40014 Jyväskylä, FinlandDepartment of Anatomy and Cell Biology, Institute of Biomedicine, University of Oulu, P.O. Box 5000, Aapistie 7, 90014 Oulu, FinlandWe examined the distribution of selected raft proteins on the sarcolemma of skeletal myofibers and the role of cholesterol environment in the distribution. Immunofluorescence staining showed that flotillin-1 and influenza hemagglutinin exhibited rafts that located in the domains deficient of the dystrophin glycoprotein complex, but the distribution patterns of the two proteins were different. Cholesterol depletion from the sarcolemma by means of methyl-β-cyclodextrin resulted in distorted caveolar morphology and redistribution of the caveolin 3 protein. Concomitantly, the water permeability of the sarcolemma increased significantly. However, cholesterol depletion did not reshuffle flotillin 1 or hemagglutinin. Furthermore, a hemagglutinin variant that lacked a raft-targeting signals exhibited a similar distribution pattern as the native raft protein. These findings indicate that each raft protein exhibits a strictly defined distribution in the sarcolemma. Only the distribution of caveolin 3 that binds cholesterol was exclusively dependent on cholesterol environment.http://dx.doi.org/10.1155/2012/497572
collection DOAJ
language English
format Article
sources DOAJ
author Mika Kaakinen
Tuula Kaisto
Paavo Rahkila
Kalervo Metsikkö
spellingShingle Mika Kaakinen
Tuula Kaisto
Paavo Rahkila
Kalervo Metsikkö
Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal Myofibers
Biochemistry Research International
author_facet Mika Kaakinen
Tuula Kaisto
Paavo Rahkila
Kalervo Metsikkö
author_sort Mika Kaakinen
title Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal Myofibers
title_short Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal Myofibers
title_full Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal Myofibers
title_fullStr Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal Myofibers
title_full_unstemmed Caveolin 3, Flotillin 1 and Influenza Virus Hemagglutinin Reside in Distinct Domains on the Sarcolemma of Skeletal Myofibers
title_sort caveolin 3, flotillin 1 and influenza virus hemagglutinin reside in distinct domains on the sarcolemma of skeletal myofibers
publisher Hindawi Limited
series Biochemistry Research International
issn 2090-2247
2090-2255
publishDate 2012-01-01
description We examined the distribution of selected raft proteins on the sarcolemma of skeletal myofibers and the role of cholesterol environment in the distribution. Immunofluorescence staining showed that flotillin-1 and influenza hemagglutinin exhibited rafts that located in the domains deficient of the dystrophin glycoprotein complex, but the distribution patterns of the two proteins were different. Cholesterol depletion from the sarcolemma by means of methyl-β-cyclodextrin resulted in distorted caveolar morphology and redistribution of the caveolin 3 protein. Concomitantly, the water permeability of the sarcolemma increased significantly. However, cholesterol depletion did not reshuffle flotillin 1 or hemagglutinin. Furthermore, a hemagglutinin variant that lacked a raft-targeting signals exhibited a similar distribution pattern as the native raft protein. These findings indicate that each raft protein exhibits a strictly defined distribution in the sarcolemma. Only the distribution of caveolin 3 that binds cholesterol was exclusively dependent on cholesterol environment.
url http://dx.doi.org/10.1155/2012/497572
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