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Nucleic Acids Research, 1991, Vol. 19, No. 17 4709-4716
© 1991


MOLECULAR BIOLOGY

The muscle specific domain of mouse N-CAM: structure and alternative splicing patterns

Marion Hamshere, George Dickson1 and Ian Eperon*

Department of Biochemistry, University of Leicester Leicester LE1 7RH UK 1Department of Experimental Pathology, UMDS, Guys Hospital London Bridge, London SE1 9RT, UK

* To whom correspondence should be addressed

Received May 2, 1991. Revised August 5, 1991. Accepted August 5, 1991.

The neural cell adhesion molecule (N-CAM) is an important mediator of calcium independent cell-cell interactions. Variations In the primary structure of the protein are due to alternative splicing of pre-mRNA in the region encoding the extracellular, trans-membrane and cytoplasmic domains. in order to identify the patterns of exon usage during development of skeletal muscle and brain of the mouse, a coupled reverse transcriptase/polymerase chain reaction was used to identify the murine homologues of the muscle-specific domain (MSD), located between exons 12 and 13 in human N-CAM mRNA. The cDNAs produced have been cloned and sequenced, or analysed directly. The amplification reactions were shown to maintain the concentration ratios of the initial cDNAs. The results indicate that the mouse homologue to exon MSD1a is under tissue and developmental regulation that is independent of exons MSD1b and MSD1c. The inclusion of the triplet exon AAG is also regulated in a cell- and stage-specific manner, which is independent of the other alternatively spliced exons of this domain.


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