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Thymosin β 4 serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G‐actin 1
Author(s) -
Huff Thomas,
Ballweber Edda,
Humeny Andreas,
Bonk Thomas,
Becker Cord-Michael,
Müller Christian S.G.,
Mannherz Hans Georg,
Hannappel Ewald
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01670-1
Subject(s) - tissue transglutaminase , chemistry , thymosin , biochemistry , actin , substrate (aquarium) , in vivo , carbodiimide , biophysics , enzyme , biology , ecology , microbiology and biotechnology
Thymosin β 4 possesses actin‐sequestering activity and, like transglutaminases, is supposed to be involved in cellular events like angiogenesis, blood coagulation, apoptosis and wound healing. Thymosin β 4 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 β 4 may serve as a useful tool for further investigations in cell biology. Thymosin β 4 could provide a specific glutaminyl substrate for transglutaminase in vivo, because of the fast reaction observed in vitro occurring at thymosin β 4 concentrations which are found inside cells. Taking these data together, it is tempting to speculate that thymosin β 4 may serve as a glutaminyl substrate for transglutaminases in vivo and play an important role in transglutaminase‐related processes.