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Immunoblot analysis of dystrophin-related protein (DRP)
R Koga1, S Ishiura, M Takemitsu
1National Institute of Neuroscience, NCNP, Tokyo, Japan.
Abstract:
Polyclonal antibodies against the carboxy-terminal portion of dystrophin-related protein (DRP), the putative autosomal gene product which shares sequence homology with dystrophin, show the clear expression of DRP in mouse fetal muscle and in cultured human muscle cells, but not in mature mouse or human muscle. DRP has the same molecular mass as X-linked dystrophin and is recovered from the membrane fraction, but is associated with membranes more loosely than dystrophin.
Insights
Dystrophin-related protein (DRP) is expressed in fetal and cultured muscle cells but not mature muscle. DRP shares properties with dystrophin but associates more loosely with membranes.
Area of Science:
- Muscle biology
- Protein biochemistry
- Developmental biology
Background:
- Dystrophin-related protein (DRP) is homologous to dystrophin.
- The expression pattern and function of DRP are not fully understood.
Purpose of the Study:
- To investigate the expression and localization of DRP in muscle tissues.
- To compare DRP properties with dystrophin.
Main Methods:
- Polyclonal antibodies against the carboxy-terminal portion of DRP were generated.
- Expression was analyzed in mouse fetal muscle and cultured human muscle cells.
- DRP was recovered from the membrane fraction and its association strength was assessed.
Main Results:
- DRP was clearly expressed in mouse fetal muscle and cultured human muscle cells.
- DRP was not detected in mature mouse or human muscle.
- DRP exhibited the same molecular mass as X-linked dystrophin.
- DRP was associated more loosely with membranes than dystrophin.
Conclusions:
- DRP expression is developmentally regulated, present in fetal and early developmental stages.
- DRP is a distinct protein from dystrophin, with differences in membrane association.