Detection of von Willebrand factor-cleaving protease (ADAMTS-13) in human platelets

The hemostatic activity of von Willebrand factor (vWF) is strongly dependent on its multimeric structure, with the highest activity in ‘unusually large’ multimers secreted from endothelial cells. The multimeric structure is regulated by a plasma protease, vWF-cleaving protease (vWF-CP, or ADAMTS-13)...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2004-01, Vol.313 (1), p.212-216
Main Authors: Suzuki, Misako, Murata, Mitsuru, Matsubara, Yumiko, Uchida, Toshihiro, Ishihara, Hiroaki, Shibano, Toshiro, Ashida, Shin-ichiro, Soejima, Kenji, Okada, Yasunori, Ikeda, Yasuo
Format: Article
Language:English
Subjects:
Actins - analysis
Actins - biosynthesis
ADAM Proteins
ADAMTS-13
ADAMTS13 Protein
Antigens, CD20 - analysis
Antigens, CD20 - biosynthesis
Blood Platelets - enzymology
Blotting, Western
Expression
Flow Cytometry
Gene Expression
Humans
Metalloendopeptidases - biosynthesis
Metalloendopeptidases - blood
Platelets
Polymerase Chain Reaction - methods
Real-time PCR
RNA, Messenger - analysis
RNA, Messenger - biosynthesis
Thrombosis
TTP
von Willebrand Factor - metabolism
vWF
vWF-CP
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Summary:The hemostatic activity of von Willebrand factor (vWF) is strongly dependent on its multimeric structure, with the highest activity in ‘unusually large’ multimers secreted from endothelial cells. The multimeric structure is regulated by a plasma protease, vWF-cleaving protease (vWF-CP, or ADAMTS-13). ADAMTS-13 mRNA is variably expressed in liver and other tissues. Because 15–25% of circulating vWF is stored in platelets, the presence and function of ADAMTS-13 in platelets are important issues. Here we report ADAMTS-13 expression in human platelets. Western blot analysis and flow cytometric analysis on permeabilized platelets revealed the presence of ADAMTS-13 protein. Real-time PCR demonstrated that ADAMTS-13 mRNA is present in platelets of six healthy volunteers, with little quantitative difference. The presence of ADAMTS-13 in platelets may imply the functional role of this enzyme in the local regulation of platelet function at the site of vascular injury or thrombus formation, and provide a useful tool for the analysis of structure and function of this enzyme.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2003.11.111