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Evidence for tissue-specific alternative splicing of the ovine insulin receptor gene

Published online by Cambridge University Press:  05 November 2021

P.D. McGrattan ,
A.R.G. Wylie  and
A.J. Bjourson
P.D. McGrattan
Affiliation:
The Queen’s University of Belfast, Newforge Lane, Belfast BT9 5PX, Northern Ireland
A.R.G. Wylie
Affiliation:
The Queen’s University of Belfast, Newforge Lane, Belfast BT9 5PX, Northern Ireland Department of Agriculture for Northern Ireland, Newforge Lane, Belfast BT9 5PX, Northern Ireland
A.J. Bjourson
Affiliation:
The Queen’s University of Belfast, Newforge Lane, Belfast BT9 5PX, Northern Ireland
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Extract

Alternative splicing of a discrete 36 base pair segment (exon 11) of the human and rat insulin receptor leads to the formation of high and low affinity isoforms differing as much as 3-fold in affinity for insulin. Alternative splicing is a common mechanism for generating protein isoforms and is often regulated in a tissue-specific fashion (Seino & Bell, 1989; Mosthaf et al., 1990). In humans, the lower affinity (B-isoform) mRNA transcript is predominantly expressed in tissues that are important for modulating glucose homeostasis such as the liver and muscle whereas the higher affinity (A-isoform) mRNA transcript is predominantly expressed in haematopoietic tissues such as spleen. Alternative splicing of the region of the ovine insulin receptor gene encoding exon 11 has recently been demonstrated (McGrattan et al., unpublished). The objective of the present study was to establish whether tissue-specific regulation of alternative splicing of the insulin receptor gene occurs in the ruminant animal.

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Proceedings of the British Society of Animal Science , Volume 1998 , 1998 , pp. 96
Copyright
Copyright © The British Society of Animal Science 1998

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References

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