The integrin PSI domain has an endogenous thiol isomerase function and is a novel target for antiplatelet therapy

Author:

Zhu Guangheng1,Zhang Qing123,Reddy Emily C.1,Carrim Naadiya14,Chen Yunfeng5,Xu Xiaohong Ruby16,Xu Miao16,Wang Yiming146,Hou Yan1,Ma Li14,Li Yan14,Rui Min14,Petruzziello-Pellegrini Tania N.146,Lavalle Christopher15,Stratton Tyler W.16,Lei Xi1,Adili Reheman1ORCID,Chen Pingguo14,Zhu Cheng7,Wilkins John A.8,Hynes Richard O.9,Freedman John1610,Ni Heyu145610

Affiliation:

1. Toronto Platelet Immunobiology Group and Department of Laboratory Medicine, Keenan Research Centre for Biomedical Science, St. Michael's Hospital, University of Toronto, Toronto, ON, Canada;

2. Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, Guangdong, China;

3. Institute of Sun Yat-sen University in Shenzhen, Shenzhen, Guangdong, China;

4. Canadian Blood Services, Toronto, ON, Canada;

5. Department of Physiology, and

6. Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada;

7. Coulter Department of Biomedical Engineering and Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA;

8. Department of Internal Medicine, University of Manitoba, Winnipeg, MB, Canada;

9. Howard Hughes Medical Institute, David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA; and

10. Department of Medicine, University of Toronto, Toronto, ON, Canada

Abstract

Key Points Integrin PSI domain has endogenous thiol-isomerase function. Novel anti-β3 PSI antibodies inhibit PDI-like activity and platelet adhesion/aggregation, and have antithrombotic therapeutic potential.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

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