Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age
Background: Old human red blood cells (RBCs) have a reduced surface area with respect to young RBCs. If this decrease occurred through the release of vesicles similar to the spectrin-free vesicles that are shed in vitro under different experimental conditions or during storage, there would be no dec...
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| Format: | Article |
| Language: | English |
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Cell Physiol Biochem Press GmbH & Co KG
2017-06-01
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| Series: | Cellular Physiology and Biochemistry |
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| Online Access: | http://www.karger.com/Article/FullText/478769 |
| _version_ | 1818887890630868992 |
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| author | Annarita Ciana Cesare Achilli Giampaolo Minetti |
| author_facet | Annarita Ciana Cesare Achilli Giampaolo Minetti |
| author_sort | Annarita Ciana |
| collection | DOAJ |
| description | Background: Old human red blood cells (RBCs) have a reduced surface area with respect to young RBCs. If this decrease occurred through the release of vesicles similar to the spectrin-free vesicles that are shed in vitro under different experimental conditions or during storage, there would be no decrease of membrane-skeleton, but only of lipid bilayer surface area, during RBC ageing in vivo. However, we observed a decrease in spectrin and other membrane-skeletal proteins in old RBCs. Because RBCs contain components of the ubiquitin-proteasome system and other hydrolytic systems for protein degradation, we asked whether increased membrane-skeleton fragments could be detected in older RBCs. Methods: Four different anti-spectrin antibodies and an antibody anti-ubiquitin conjugates were used to analyse, by Western blotting, fragments of spectrin and other proteins in RBCs of different age separated in density gradients and characterized for their protein 4.1a/4.1b ratio as a cell age parameter. Results: spectrin fragments do exist in RBCs of all ages, they represent a minute fraction of all spectrin, are membrane-bound and not cytoplasmic and do not increase with cell age. Besides spectrin, other membrane-skeletal components decrease with cell age. Conclusion: Observed results challenge the commonly accepted view that decrease in cell membrane throughout RBC life in vivo occurs via the release of spectrin-free vesicles. |
| first_indexed | 2024-12-19T16:44:25Z |
| format | Article |
| id | doaj.art-b3ca5f06136b4b1e96c05feb6c1e8941 |
| institution | Directory Open Access Journal |
| issn | 1015-8987 1421-9778 |
| language | English |
| last_indexed | 2024-12-19T16:44:25Z |
| publishDate | 2017-06-01 |
| publisher | Cell Physiol Biochem Press GmbH & Co KG |
| record_format | Article |
| series | Cellular Physiology and Biochemistry |
| spelling | doaj.art-b3ca5f06136b4b1e96c05feb6c1e89412022-12-21T20:13:41ZengCell Physiol Biochem Press GmbH & Co KGCellular Physiology and Biochemistry1015-89871421-97782017-06-014231139115210.1159/000478769478769Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different AgeAnnarita CianaCesare AchilliGiampaolo MinettiBackground: Old human red blood cells (RBCs) have a reduced surface area with respect to young RBCs. If this decrease occurred through the release of vesicles similar to the spectrin-free vesicles that are shed in vitro under different experimental conditions or during storage, there would be no decrease of membrane-skeleton, but only of lipid bilayer surface area, during RBC ageing in vivo. However, we observed a decrease in spectrin and other membrane-skeletal proteins in old RBCs. Because RBCs contain components of the ubiquitin-proteasome system and other hydrolytic systems for protein degradation, we asked whether increased membrane-skeleton fragments could be detected in older RBCs. Methods: Four different anti-spectrin antibodies and an antibody anti-ubiquitin conjugates were used to analyse, by Western blotting, fragments of spectrin and other proteins in RBCs of different age separated in density gradients and characterized for their protein 4.1a/4.1b ratio as a cell age parameter. Results: spectrin fragments do exist in RBCs of all ages, they represent a minute fraction of all spectrin, are membrane-bound and not cytoplasmic and do not increase with cell age. Besides spectrin, other membrane-skeletal components decrease with cell age. Conclusion: Observed results challenge the commonly accepted view that decrease in cell membrane throughout RBC life in vivo occurs via the release of spectrin-free vesicles.http://www.karger.com/Article/FullText/478769Spectrinp55MEMBRANE skeletonVesiculationExosomesEctosomesRed blood cell ageingProtein 4.1Ankyrin |
| spellingShingle | Annarita Ciana Cesare Achilli Giampaolo Minetti Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age Cellular Physiology and Biochemistry Spectrin p55 MEMBRANE skeleton Vesiculation Exosomes Ectosomes Red blood cell ageing Protein 4.1 Ankyrin |
| title | Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age |
| title_full | Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age |
| title_fullStr | Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age |
| title_full_unstemmed | Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age |
| title_short | Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age |
| title_sort | spectrin and other membrane skeletal components in human red blood cells of different age |
| topic | Spectrin p55 MEMBRANE skeleton Vesiculation Exosomes Ectosomes Red blood cell ageing Protein 4.1 Ankyrin |
| url | http://www.karger.com/Article/FullText/478769 |
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