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Differential Expression of Syntrophins and Analysis of Alternatively Spliced Dystrophin Transcripts in the Mouse Brain
Author(s) -
Górecki Dariusz C.,
Lukasiuk Katarzyna,
Barnard Eric A.,
Abdulrazzak Hassan
Publication year - 1997
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.1997.tb01447.x
Subject(s) - dystrophin , dentate gyrus , biology , utrophin , neuroscience , microbiology and biotechnology , chemistry , hippocampal formation , anatomy , skeletal muscle
Abstract Expression of syntrophin genes, encoding members of the dystrophin‐associated protein complex, was studied in the mouse brain. In the hippocampal formation there is distinctive co‐localization of specific syntrophins with certain dystrophin isoforms in neurons, e.g. α 1 ,‐syntrophin with the C‐dystrophin in CA regions and β 2 ‐syntrophin with the G‐dystrophin in the dentate gyrus. Expression of the al‐syntrophin is predominant in CA regions and the olfactory bulb and it is also present in the cerebral cortex and the dentate gyrus. The β 2 ‐syntrophin mRNA is most abundant in the dentate gyrus and is also evident in the pituitary, the cerebral cortex and in Ammon's horn and in traces in the caudate putamen. The choroid plexus was labelled by both α 1 and β 2 ‐syntrophin‐specific probes. The expression of syntrophins in the brain correlates with expression of dystrophins and dystroglycan. There are brain areas such as the cerebral cortex where several different syntrophins and dystrophins are expressed together. Syntrophin expression co‐localizes with utrophin in the choroid plexus and caudate putamen. Finally, no syntrophin was detected in the cerebellar Purkinje cells where the specific dystrophin isoform (P‐type) is present. This specific distribution of syntrophins in the brain is particularly interesting, as muscle syntrophin interacts with neuronal nitric oxide synthase. This may suggest that the dystrophin‐associated protein complex may be involved in synaptic organisation and signal transduction machinery in both muscle and neurons. The dystrophin isoform, with exons 71–74 spliced out and hence lacking syntrophin binding sites, had been believed to be predominant in the brain, but our analyses using in situ hybridization, S1 nuclease protection and the semi‐quantitative polymerase chain reaction revealed that this alternatively spliced mRNA is a minor, low abundance form in the brain.