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Molecular Pharmacology

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Abstract

Glycoprotein nature of the A2-adenosine receptor binding subunit.

W W Barrington, K A Jacobson and G L Stiles
Molecular Pharmacology August 1990, 38 (2) 177-183;
W W Barrington
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K A Jacobson
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G L Stiles
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Abstract

Mammalian A2-adenosine receptor binding subunits (A2AR) can be visualized by covalent labeling with the photoaffinity crosslinking ligand 125I-2-[4-[2-[2-[(4-aminophenyl)methylcarbonylamino] ethylaminocarbonyl]ethyl]phenyl]ethylamino-5'-N-ethylcarboxamidoad enosine or directly with the azide derivative described in this paper. The protein comprising the A2-adenosine receptor binding subunit migrates with a Mr of 45,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In this study, the glycoproteins representing the radiolabeled A1- and A2-adenosine receptor binding subunit from bovine brain were compared by partial peptide maps and following treatment with exo- and endoglycosidases. Peptide maps using two separate proteases reveal that the A1- and A2-adenosine receptor binding subunits share no common peptide fragments by two-dimensional gel electrophoresis. Endoglycosidase F treatment of labeled A2AR results in a single labeled peptide of Mr 38,000 without intermediate peptides, suggesting a single N-linked carbohydrate chain. The labeled A2AR demonstrates a sensitivity to neuraminidase, as evidenced by an increased mobility on gel electrophoresis, suggesting the receptors contain a glycan component containing terminal sialic acid. Treatment of the labeled A2AR with alpha-mannosidase reveals two distinct populations of A2ARs, one of which is sensitive and the other resistant to the enzyme. The nonadditivity of sequential treatments with the two exoglycosidases suggests, a heterogeneous population of A2AR containing either complex- or high mannose-type carbohydrate chains. These data suggest the A2AR is a Mr 45,000 glycoprotein with a single carbohydrate chain of either the complex or high mannose type. In addition, the A1- and A2ARs are distinct glycoproteins, as evidenced by their differing molecular weights (before and after deglycosylation) and distinct peptide maps.

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Molecular Pharmacology
Vol. 38, Issue 2
1 Aug 1990
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Abstract

Glycoprotein nature of the A2-adenosine receptor binding subunit.

W W Barrington, K A Jacobson and G L Stiles
Molecular Pharmacology August 1, 1990, 38 (2) 177-183;

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Abstract

Glycoprotein nature of the A2-adenosine receptor binding subunit.

W W Barrington, K A Jacobson and G L Stiles
Molecular Pharmacology August 1, 1990, 38 (2) 177-183;
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