HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by HUFF, T. Articles by HANNAPPEL, E. Search for Related Content PubMed PubMed Citation Articles by HUFF, T. Articles by HANNAPPEL, E.

Thymosin ß₄ is released from human blood platelets and attached by factor XIIIa (transglutaminase) to fibrin and collagen

Institute of Biochemistry, Faculty of Medicine, University Erlangen-Nuremberg, 91054 Erlangen, Germany

¹Correspondence: Institute of Biochemistry, Faculty of Medicine, University Erlangen-Nuremberg, Fahrstr. 17, 91054 Erlangen, Germany. E-mail: thymosin{at}biochem.uni-erlangen.de

The ß-thymosins constitute a family of highly conserved and extremely water-soluble 5 kDa polypeptides. Thymosin ß₄ is the most abundant member; it is expressed in most cell types and is regarded as the main intracellular G-actin sequestering peptide. There is increasing evidence for extracellular functions of thymosin ß₄. For example, thymosin ß₄ increases the rate of attachment and spreading of endothelial cells on matrix components and stimulates the migration of human umbilical vein endothelial cells. Here we show that thymosin ß₄ can be cross-linked to proteins such as fibrin and collagen by tissue transglutaminase. Thymosin ß₄ is not cross-linked to many other proteins and its cross-linking to fibrin is competed by another family member, thymosin ß₁₀. After activation of human platelets with thrombin, thymosin ß₄ is released and cross-linked to fibrin in a time- and calcium-dependent manner. We suggest that thymosin ß₄ cross-linking is mediated by factor XIIIa, a transglutaminase that is coreleased from stimulated platelets. This provides a mechanism to increase the local concentration of thymosin ß₄ near sites of clots and tissue damage, where it may contribute to wound healing, angiogenesis and inflammatory responses.—Huff, T., Otto, A. M., Müller, C. S. G., Meier, M., Hannappel, E. Thymosin ß₄ is released from human blood platelets and attached by factor XIIIa (transglutaminase) to fibrin and collagen.

Key Words: ß-thymosins • cross-linking • actin

This article has been cited by other articles:

				B. J. Xu, Y. Shyr, X. Liang, L.-j. Ma, E. M. Donnert, J. D. Roberts, X. Zhang, V. Kon, N. J. Brown, R. M. Caprioli, et al. Proteomic Patterns and Prediction of Glomerulosclerosis and Its Mechanisms J. Am. Soc. Nephrol., October 1, 2005; 16(10): 2967 - 2975. [Abstract] [Full Text] [PDF]

				A. L. Clark and J. G.F. Cleland Anemia and Chronic Heart Failure: Are We Asking the Right Questions? Circulation, September 20, 2005; 112(12): 1681 - 1683. [Full Text] [PDF]

				T. Huff, O. Rosorius, A. M. Otto, C. S. G. Muller, E. Ballweber, E. Hannappel, and H. G. Mannherz Nuclear localisation of the G-actin sequestering peptide thymosin {beta}4 J. Cell Sci., October 15, 2004; 117(22): 5333 - 5341. [Abstract] [Full Text] [PDF]

				K. N. I. Al-Nedawi, M. Czyz, R. Bednarek, J. Szemraj, M. Swiatkowska, A. Cierniewska-Cieslak, J. Wyczolkowska, and C. S. Cierniewski Thymosin {beta}4 induces the synthesis of plasminogen activator inhibitor 1 in cultured endothelial cells and increases its extracellular expression Blood, February 15, 2004; 103(4): 1319 - 1324. [Abstract] [Full Text] [PDF]

				A. L. Goldstein Thymosin {beta}4: A New Molecular Target for Antitumor Strategies J Natl Cancer Inst, November 19, 2003; 95(22): 1646 - 1647. [Full Text] [PDF]

				A. S. Weyrich and G. A. Zimmerman Evaluating the relevance of the platelet transcriptome Blood, August 15, 2003; 102(4): 1550 - 1551. [Full Text] [PDF]