Thymosin β4 serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G‐actin

FEBS Letters

Ballweber, Edda¹  Hannappel, Ewald²  Huff, Thomas²  Mannherz, Hans Georg¹  Müller, Christian S.G.²  Bonk, Thomas²  Becker, Cord-Michael²  Humeny, Andreas² 

[1] Cytoskeletal Laboratory, Abteilung für Anatomie und Embryologie, Ruhr-Universität Bochum, Universitätsstr. 150, D-44780 Bochum, Germany;Institut für Biochemie, Medizinische Fakultät, Universität Erlangen-Nürnberg, Fahrstr. 17, D-91054 Erlangen, Germany

关键词: Thymosin β4;    Transglutaminase;    Actin;    Dansylcadaverine;   

DOI  :  10.1016/S0014-5793(99)01670-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Thymosin β₄ possesses actin-sequestering activity and, like transglutaminases, is supposed to be involved in cellular events like angiogenesis, blood coagulation, apoptosis and wound healing. Thymosin β₄ serves as a specific glutaminyl substrate for transglutaminase and can be fluorescently labeled with dansylcadaverine. Two (Gln-23 and Gln-36) of the three glutamine residues were mainly involved in the transglutaminase reaction, while the third glutaminyl residue (Gln-39) was derivatized with a low efficiency. Labeled derivatives were able to inhibit polymerization of G-actin and could be cross-linked to G-actin by 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide. Fluorescently labeled thymosin β₄ may serve as a useful tool for further investigations in cell biology. Thymosin β₄ could provide a specific glutaminyl substrate for transglutaminase in vivo, because of the fast reaction observed in vitro occurring at thymosin β₄ concentrations which are found inside cells. Taking these data together, it is tempting to speculate that thymosin β₄ may serve as a glutaminyl substrate for transglutaminases in vivo and play an important role in transglutaminase-related processes.

【 授权许可】

Unknown