Receptor‐binding capability of pancreatic phospholipase A2 is separable from its enzymatic activity

FEBS Letters

Teraoka, Hiroshi¹  Arita, Hitoshi¹  Kishino, Junji¹  Ishizaki, Jun¹  Ohara, Osamu¹ 

[1] Shionogi Research Laboratories, Shionogi & Co., Ltd., 12-4, Sagisu 5-chome, Fukushima-ku, Osaka 553, Japan

关键词: Phospholipase A2;    Specific binding;    In vitro mutagenesis;    PLA2;    phospholipase A2;    PLA2-I;    mammalian group I (pancreatic) phospholipase A2;    PCR;    the polymerase chain reaction;   

DOI  :  10.1016/0014-5793(93)80149-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mammalian pancreatic phospholipase A₂ (PLA₂-I) has its specific receptor through which PLA₂-I induces a variety of biological responses. In this study, a fundamental relationship between the enzymatic and the receptor-binding activities of PLA₂-I was investigated. The specific binding of PLA₂-I to the receptor was found to be independent of Ca²⁺ which is requisite for the PLA₂ activity. On the basis of this observation, we designed and produced mutant PLA₂-Is without Ca²⁺-binding abilities in order to demonstrate that the structural requirement for the enzymatic activity of PLA₂-I is not identical with that for its receptor-binding reaction. These mutant PLA₂-Is lost almost all enzymatic activity through a disturbance at the Ca²⁺-binding site, as expected, but still retained a substantial affinity to the receptor, allowing us to conclude that the receptor-binding reaction of PLA₂-I is separable from its catalytic action.

【 授权许可】

Unknown