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McNally, T. et al.

McNally, Grihalde, Pederson, Ogiela, Djuric, Collins, Lin, Reilly,

Cloning and characterization of the glucagon receptor from cynomologous monkey.

The glucagon receptor was cloned from cynolomologous monkey. A frame-shift mutation at the 3' end of the monkey transcript results in a C-terminal extension of 14 amino acids. This extension is not observed in either the human or rodent glucagon receptors. Monkey glucagon receptor was expressed in CHO cells, either with (mkGCGR) or without (mkGCGRDelta14) the 14-amino acid C-terminal extension to approximate the human receptor. Both forms of the monkey receptor bound glucagon with similar affinity and showed glucagon-stimulated cAMP production, however the full-length form of the monkey receptor (mkGCGR) was less sensitive to glucagon in its ability to stimulate cAMP than the shortened form (mkGCGRDelta14). PCR of genomic DNA from baboon and rhesus monkeys suggests that they express a form of the receptor similar to that of cynomologous monkey, while in chimpanzee, the receptor is similar to the human form.[1]

References

Cloning and characterization of the glucagon receptor from cynomologous monkey. McNally, T., Grihalde, N.D., Pederson, T.M., Ogiela, C.A., Djuric, S.W., Collins, C.A., Lin, C.W., Reilly, R.M. Peptides (2004) [Pubmed]

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