Copyright © 2006, European Society of Cardiology
Localization and characterization of a novel secreted protein SCUBE1 in human platelets
aInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan
bInstitute of Cellular and Organismic Biology, Academia Sinica, Taipei, Taiwan
cGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan
dInstitute of Anatomy and Cell Biology, College of Medicine, National Taiwan University, Taipei, Taiwan
eGraduate Institute of Medical Sciences and Department of Pathology, School of Medicine, Taipei Medical University, Taipei, Taiwan
fSection of Cardiology, Department of Internal Medicine, National Taiwan University Hospital, Taipei, Taiwan
gSection of Cardiology, Department of Internal Medicine, Taoyuan General Hospital Department of Health Executive Yuan, Taoyuan, Taiwan
hInstitute of Pharmacology, School of Medicine, National Yang-Ming University, Taipei, Taiwan
* Corresponding author. Institute of Biomedical Sciences, Academia Sinica, 128, Academia Road, Sec. 2, Taipei 11529, Taiwan. Tel.: +886 2 2652 3943; fax: +886 2 2785 8847. Email address: rbyang{at}ibms.sinica.edu.tw
Objective: The aim of the study was to investigate the protein expression and function of a novel secreted protein in the vascular system, named SCUBE1 for signal peptide, CUB (Complement proteins C1r/C1s, Uegf, and Bmp1) and epidermal growth factor-like (EGF)-like domain containing protein 1.
Methods and results Immunohistochemical analysis demonstrated that the SCUBE1 staining is mainly confined to the intravascular platelet-rich thrombus in vascular tissue samples. While quantitative real-time RT-PCR verified that the SCUBE1 mRNA is expressed in human platelets, numerous immunolocalization techniques revealed that the preformed SCUBE1 protein is stored in the 
-granules and translocated to the surface upon platelet stimulation. A smaller SCUBE1 fragment, possibly formed by limited proteolysis after being released from the storage granules, was detected in thrombus lysate by Western blot analysis. Interestingly, deposition of SCUBE1 into the subendothelial matrix of the atherosclerotic plaques was evidenced by immunohistochemistry. In addition, studies of platelet adhesion and ristocetin-induced platelet agglutination showed that fragments containing the amino-terminal EGF-like repeats were able to support platelet adhesion and enhance the ristocetin-induced platelet agglutination, respectively.
Conclusion These data suggest that platelet-derived SCUBE1 could function as a novel adhesive molecule and its matrix-bound and soluble fragments may play critical (patho)physiological roles in cardiovascular biology.
KEYWORDS Atherosclerosis; Electron microscopy; Extracellular matrix; Histo(patho)logy; Platelets
Time for primary review 28 days
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