Classic and soma-restricted proteolipids are targeted to different subcellular compartments in oligodendrocytes
| Autor: | Vilma Schonmann, Erin C. Jacobs, Ernesto R. Bongarzone, Anthony T. Campagnoni |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Proteolipid protein 1
Fluorescent Antibody Technique Golgi Apparatus Biology Endoplasmic Reticulum Myelin assembly Mice Cellular and Molecular Neuroscience symbols.namesake Myelin immune system diseases Compact myelin medicine Animals Protein Isoforms Myelin Proteolipid Protein Transport Vesicles Myelin proteolipid Cells Cultured Myelin Sheath Organelles Qa-SNARE Proteins Proteolipids fungi Membrane Proteins Intracellular Membranes Golgi apparatus Subcellular localization Clathrin Cell Compartmentation nervous system diseases Cell biology Oligodendroglia Protein Transport medicine.anatomical_structure nervous system Biochemistry symbols lipids (amino acids peptides and proteins) |
| Zdroj: | Journal of Neuroscience Research. 65:477-484 |
| ISSN: | 1097-4547 0360-4012 |
| DOI: | 10.1002/jnr.1177 |
| Popis: | The myelin proteolipid (PLP) gene is very active in oligodendrocytes (OLs) and generates at least four proteins: the classic PLP and DM20 proteolipids, which are associated with compact myelin and the srPLP and srDM20, which are associated with the cell soma. These proteins are extremely hydrophobic and appear to follow the biosynthetic route used by secretory proteins. In this study, we have analyzed the subcellular distribution of the newly described sr-proteolipids and compared it to that of the classic proteolipids. Immunocytochemical analysis indicates that the sr-proteolipids and classic proteolipids are found in association with the endoplasmic reticulum (ER) and Golgi apparatus of mature OLs in vitro. Whereas the classic proteolipids become associated with the myelin-like sheets elaborated by OLs, the sr-proteolipids are not targeted to the myelin leaflets. The sr-proteolipids were associated with endosomes and with recycling vesicles as determined by double immunocytochemistry with markers such as syntaxin 6 and clathrin. In vivo, immunohistochemical analysis showed a distribution of the sr-proteolipids that was similar to that obtained in vitro, with a total absence of incorporation of srproteolipids into compact myelin. This differential subcellular localization is further evidence for a biological role for these products of the PLP/DM20 gene, which is different from that of the classic proteolipids. J. Neurosci. Res. 65:477‐ 484, 2001. © 2001 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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