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FEBS Lett. 1996 Feb 19;380(3):219-23.

Adenosine deaminase affects ligand-induced signalling by interacting with cell surface adenosine receptors.

Author information

1
Departament de Bioquímica i Biologia Molecular, Facultat de Química, Universitat de Barcelona, Spain.

Abstract

Adenosine deaminase (ADA) is not only a cytosolic enzyme but can be found as an ecto-enzyme. At the plasma membrane, an adenosine deaminase binding protein (CD26, also known as dipeptidylpeptidase IV) has been identified but the functional role of this ADA/CD26 complex is unclear. Here by confocal microscopy, affinity chromatography and coprecipitation experiments we show that A1 adenosine receptor (A1R) is a second ecto-ADA binding protein. Binding of ADA to A1R increased its affinity for the ligand thus suggesting that ADA was needed for an effective coupling between A1R and heterotrimeric G proteins. This was confirmed by the fact that ASA, independently of its catalytic behaviour, enhanced the ligand-induced second messenger production via A1R. These findings demonstrate that, apart from the cleavage of adenosine, a further role of ecto-adenosine deaminase on the cell surface is to facilitate the signal transduction via A1R.

PMID:
8601428
DOI:
10.1016/0014-5793(96)00023-3
[Indexed for MEDLINE]
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