Identification of a serine protease which activates the mouse heart adenosine 5',5''',P1,P4-tetraphosphate receptor

1 March 1993

journal article
Published by American Chemical Society (ACS) in Biochemistry

Vol. 32 (12) , 3119-3123
https://doi.org/10.1021/bi00063a025

Abstract

We have previously demonstrated that a serine protease dependent processing step is required for activation of the 30-kDa adenosine 5',5"',P1,P4-tetraphosphate (Ap4A) receptor. However, monoclonal antibodies (Mabs) against a 212-kDa polypeptide inhibit Ap4A binding to its receptor [Walker et al. (1993) Biochemistry 32, 1264-1269]. SDS-PAGE followed by autoradiography of [3H]diisopropylfluorophosphate (DIPF) covalently attached to membrane fractions reveals that the serine protease is the 212-kDa polypeptide or a proenzyme. Mabs against the 30-kDa Ap4A receptor are identified that inhibit Ap4A binding to its membrane receptor. These Mabs do not recognize the 212-kDa membrane protein but recognize four membrane proteins with molecular masses of 67, 55, 42, and 30 kDa. These data suggest that the precursor for the Ap4A receptor is a 67-kDa polypeptide which undergoes multiple cleavage events, at least one by the 212-kDa protein.

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