AI Article Synopsis
- Proteins often get their names based on the specific biological functions being studied, like acetylcholinesterase and agrin.
- Research has revealed that these proteins have alternative functions beyond their primary roles, such as in muscle development and regeneration.
- The study shows that agrin boosts interleukin 6 secretion in early muscle cells but loses this effect after they fuse into myotubes, indicating agrin's role changes based on the developmental stage.
Article Abstract
Proteins in living organisms have names that are usually derived from their function in the biochemical system their discoverer was investigating. Typical examples are acetylcholinesterase and agrin; however, for both of these, various other functions that are not related to the cholinergic system have been revealed. Our investigations have been focused on the alternative roles of acetylcholinesterase and agrin in the processes of muscle development and regeneration. Previously, we described a role for agrin in the development of excitability in muscle contraction. In this study, we report the effects of agrin on secretion of interleukin 6 in developing human muscle. At the myoblast stage, agrin increases interleukin 6 secretion. This effect seems to be general as it was observed in all of the cell models analysed (human, mouse, cell lines). After fusion of myoblasts into myotubes, the effects of agrin are no longer evident, although agrin has further effects at the innervation stage, at least in in vitro innervated human muscle. These effects of agrin are another demonstration of its non-synaptic roles that are apparently developmental-stage specific. Our data support the view that acetylcholinesterase and agrin participate in various processes during development of skeletal muscle.
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| http://dx.doi.org/10.1007/s12031-013-0188-0 | DOI Listing |
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