作者
Ok-Hee Jeon, Dongbum Kim, Yong-Jun Choi, Seung-Hee Kim, Won-Seok Choi, Doo-Sik Kim
发表日期
2007/1/1
期刊
Thrombosis research
卷号
119
期号
5
页码范围
609-619
出版商
Pergamon
简介
INTRODUCTION
A Disintegrin and Metalloproteinase (ADAM) proteins are a family of multifunctional proteins containing disintegrin and metalloproteinase domains that perform both adhesive and proteolytic functions in cell–cell and cell–matrix interactions. ADAM15 is unique among these proteins in having an Arg–Gly–Asp (RGD) motif in its disintegrin-like domain. This motif is known to interact with the integrin αIIbβ3 on platelets.
MATERIALS AND METHODS
We cloned and expressed the human ADAM15 disintegrin-like domain and its derivatives in Pichia pastoris, and purified them by chromatographic fractionation. We then characterized the integrin binding specificities and their antiplatelet activities of the proteins. Antiplatelet function was assessed by inhibition of platelet adhesion and aggregation.
RESULTS
The yeast-expressed ADAM15 disintegrin-like domains were able to inhibit the binding of αIIbβ3 as …
引用总数
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