Premium
Isoform‐dependent activation of adenylyl cyclase by proteolysis
Author(s) -
Ebina Toshiaki,
Toya Yoshiyuki,
Oka Naoki,
Kawabe Jun-ichi,
Schwencke Carsten,
Ishikawa Yoshihiro
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01475-5
Subject(s) - adenylyl cyclase , adcy10 , gene isoform , proteolysis , adcy9 , adcy6 , trypsin , gs alpha subunit , chemistry , biochemistry , proteases , enzyme activator , adcy3 , thrombin , enzyme , biology , platelet , gene , immunology
Recent findings have suggested that the cellular proteolytic system plays a major role in the regulation of various intra‐ and extra‐cellular signaling. It was previously shown that proteolytic treatment of adenylyl cyclase leads to the activation of this enzyme. We demonstrate that this activation occurs in an adenylyl cyclase isoform‐dependent manner. The type II isoform was strongly activated (∼500%), the type III isoform was modestly activated (∼30%), and the type V isoform was inhibited by trypsin. Activation of type II adenylyl cyclase occurred in trypsin dose‐ and time‐dependent manners and was blocked by a trypsin inhibitor in a dose‐dependent manner. Other proteases, such as thrombin and plasminogen, similarly activated the type II isoform, but not the others. Our data suggest that proteolytic activation is an isoform‐ and thus cell type‐dependent mechanism of altering adenylyl cyclase catalytic activity.