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Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase
- Source :
- European Journal of Neuroscience. 18:1837-1847
- Publication Year :
- 2003
- Publisher :
- Wiley, 2003.
-
Abstract
- We analysed the expression of PRiMA (proline-rich membrane anchor), the membrane anchor of acetylcholinesterase (AChE), by in situ hybridization in the mouse brain. We compared the pattern of PRiMA transcripts with that of AChE transcripts, as well as those of choline acetyltransferase and M1 muscarinic receptors which are considered pre- and postsynaptic cholinergic markers. We also analysed cholinesterase activity and its molecular forms in several brain structures. The results suggest that PRiMA expression is predominantly or exclusively related to the cholinergic system and that anchoring of cholinesterases to cell membranes by PRiMA represents a limiting factor for production of the AChE tailed splice variant (AChET)-PRiMA complex, which represents the major AChE component in the brain. This enzyme species is mostly associated with cholinergic neurons because the pattern of PRiMA mRNA expression largely coincides with that of ChAT. We also show that, in both mouse and human, PRiMA proteins exist as two alternative splice variants which differ in their cytoplasmic regions.
- Subjects :
- Male
Molecular Sequence Data
Nerve Tissue Proteins
In situ hybridization
Biology
Choline O-Acetyltransferase
Mice
chemistry.chemical_compound
Postsynaptic potential
Animals
Humans
RNA, Messenger
Cholinergic neuron
In Situ Hybridization
Cholinesterase
Mice, Inbred BALB C
Reverse Transcriptase Polymerase Chain Reaction
General Neuroscience
Receptor, Muscarinic M1
Brain
Membrane Proteins
Acetylcholinesterase
Molecular biology
Choline acetyltransferase
humanities
Alternative Splicing
Membrane protein
chemistry
biology.protein
Autoradiography
Cholinergic
Subjects
Details
- ISSN :
- 14609568 and 0953816X
- Volume :
- 18
- Database :
- OpenAIRE
- Journal :
- European Journal of Neuroscience
- Accession number :
- edsair.doi.dedup.....3500ae2207af09a31f18f19effc1745c
- Full Text :
- https://doi.org/10.1046/j.1460-9568.2003.02914.x