Skip Navigation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Ida, M.
Right arrow Articles by Kojima-Aikawa, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ida, M.
Right arrow Articles by Kojima-Aikawa, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 2004, Vol. 135, No. 5 583-588
© 2004 The Japanese Biochemical Society

BIOCHEMISTRY

Human Annexin V Binds to Sulfatide: Contribution to Regulation of Blood Coagulation

Michiru Ida*, Ayano Satoh, Isamu Matsumoto and Kyoko Kojima-Aikawa§

The Graduate School of Humanities and Sciences, Ochanomizu University, 2-1-1 Otsuka, Bunkyo-ku, Tokyo 112-8610

Annexin V is a calcium-dependent phospholipid-binding protein that exhibits anticoagulant activity on binding to phosphatidylserine exposed on the activated surfaces of endothelial cells and platelets, inhibiting activation of factor X and prothrombin in the blood coagulation cascade. Sulfatide (galactosylceramide I3-sulfate), one of the glycosphingolipids of the platelet cell membrane, is thought to be involved in blood coagulation systems via activation of factor XII. In this study, we examined whether or not annexin V binds to sulfatide and affects the coagulant activity of sulfatide. Solid phase assaying of annexin V revealed that it binds specifically to sulfatide, i.e. not to galactosylceramide or gangliosides, in the presence of calcium ions. Affinity analysis by means of surface plasmon resonance showed that the KD of the interaction between annexin V and sulfatide is 1.2 µM. Kinetic turbidometric assaying of plasma coagulation initiated by CaCl2 revealed that the coagulation rate in the presence of sulfatide or phosphatidylserine was decreased by annexin V. These results suggest that annexin V regulates coagulability in the blood stream by binding not only to phosphatidylserine but also to sulfatide.

* Present address: Department of Perinatology, Institute for Developmental Research, Aichi Human Service Center, 713-8 Kagiya-cho, Kasugai, Aichi 480-0392.

§ To whom correspondence should be addressed. Tel: +81-3-5978-5345, Fax: +81-3-5978-5345, E-mail: kyoko{at}cc.ocha.ac.jp


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Immunol.Home page
Z. V. Popovic, R. Sandhoff, T. P. Sijmonsma, S. Kaden, R. Jennemann, E. Kiss, E. Tone, F. Autschbach, N. Platt, E. Malle, et al.
Sulfated Glycosphingolipid as Mediator of Phagocytosis: SM4s Enhances Apoptotic Cell Clearance and Modulates Macrophage Activity
J. Immunol., November 15, 2007; 179(10): 6770 - 6782.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
S. Nishioka, J.-i. Aikawa, M. Ida, I. Matsumoto, M. Street, M. Tsujimoto, and K. Kojima-Aikawa
Ligand-binding Activity and Expression Profile of Annexins in Caenorhabditis elegans
J. Biochem., January 1, 2007; 141(1): 47 - 55.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.