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...
Saved in:
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2012-01-01
|
| Series: | Biochemistry Research International |
| Online Access: | http://dx.doi.org/10.1155/2012/497572 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832559960428380160 |
|---|---|
| author | Mika Kaakinen Tuula Kaisto Paavo Rahkila Kalervo Metsikkö |
| author_facet | Mika Kaakinen Tuula Kaisto Paavo Rahkila Kalervo Metsikkö |
| author_sort | Mika Kaakinen |
| collection | DOAJ |
| 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. |
| format | Article |
| id | doaj-art-374ff7681d474014a1b9f2d4901b8235 |
| institution | Kabale University |
| issn | 2090-2247 2090-2255 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Biochemistry Research International |
| spelling | doaj-art-374ff7681d474014a1b9f2d4901b82352025-02-03T01:28:40ZengWileyBiochemistry 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 |
| 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 |
| title | 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_short | 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 |
| url | http://dx.doi.org/10.1155/2012/497572 |
| work_keys_str_mv | AT mikakaakinen caveolin3flotillin1andinfluenzavirushemagglutininresideindistinctdomainsonthesarcolemmaofskeletalmyofibers AT tuulakaisto caveolin3flotillin1andinfluenzavirushemagglutininresideindistinctdomainsonthesarcolemmaofskeletalmyofibers AT paavorahkila caveolin3flotillin1andinfluenzavirushemagglutininresideindistinctdomainsonthesarcolemmaofskeletalmyofibers AT kalervometsikko caveolin3flotillin1andinfluenzavirushemagglutininresideindistinctdomainsonthesarcolemmaofskeletalmyofibers |