IDENTIFICATION OF A SERINE PROTEASE WHICH ACTIVATES THE MOUSE HEART ADENOSINE 5',5''',P1,P4-TETRAPHOSPHATE RECEPTOR

被引：19

作者：

WALKER, J ^{[1
]}

HILDERMAN, RH ^{[1
]}

机构：

[1] CLEMSON UNIV,DEPT BIOL SCI,CLEMSON,SC 29634

来源：

BIOCHEMISTRY | 1993年 / 32卷 / 12期

关键词：

D O I：

10.1021/bi00063a025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 [H-3]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.

引用

页码：3119 / 3123

页数：5

共 28 条

[1] THE ENDOTHELIN-CONVERTING ENZYME FROM HUMAN UMBILICAL VEIN IS A MEMBRANE-BOUND METALLOPROTEASE SIMILAR TO THAT FROM BOVINE AORTIC ENDOTHELIAL-CELLS [J].