The levels of both lipid rafts and raft-located acetylcholinesterase dimers increase in muscle of mice with muscular dystrophy by merosin deficiency
| Autor: | Encarnación Muñoz-Delgado, Francisco J. Campoy, Cecilio J. Vidal, María F. Montenegro, M.T. Moral-Naranjo |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Nucleotidase activity
Caveolin 3 Mice Transgenic Biology Caveolae Mice chemistry.chemical_compound Membrane Microdomains medicine Animals Muscular dystrophy Muscle Skeletal 5'-Nucleotidase Molecular Biology Lipid raft Sarcolemma Wild type Dystrophy Cholinesterase Muscular Dystrophy Animal medicine.disease Acetylcholinesterase Cell biology Mice Inbred C57BL Ecto-5’-nucleotidase (CD73) Biochemistry chemistry Molecular Medicine Laminin Protein Multimerization |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1802:754-764 |
| ISSN: | 0925-4439 |
| DOI: | 10.1016/j.bbadis.2010.05.011 |
| Popis: | Wild type and dystrophic (merosin-deficient) Lama2dy mice muscles were compared for their density of lipid rafts. The 5-fold higher level of caveolin-3 and the 2-3 times higher level of ecto-5’-nucleotidase activity in raft preparations (Triton X-100-resistant membranes) of dystrophic muscle supported expansion of caveolar and non-caveolar lipid rafts. The presence in rafts of glycosylphosphatidylinositol (GPI)-linked acetylcholinesterase (AChE) dimers, which did not arise from erythrocyte or nerve, not only revealed for the first time the capacity of the myofibre for translating the AChE-H mRNA but also an unrecognized pathway for targeting AChE-H to specialized membrane domains of the sarcolemma. Rafts of dystrophic muscle contained a 5-fold higher AChE activity/mg protein. RT-PCR for 3’-alternative mRNAs of AChE revealed AChE-T mRNA prevailing over AChE-R and AChE-H mRNAs in wild type mouse muscle. It also displayed principal 5’-alternative AChE mRNAs with exons E1c and E1e (the latter coding for N-terminally extended subunits) and fewer with E1d, E1a and E1b. The levels of AChE and butyrylcholinesterase mRNAs were unaffected by dystrophy. Finally, the decreased level of proline-rich membrane anchor (PRiMA) mRNA in Lama2dy muscle provided for a rational explanation to the loss of PRiMA-bearing AChE tetramers in dystrophic muscle. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect