Back to Search Start Over

Transducible recombinant small heat shock-related protein, HSP20, inhibits vasospasm and platelet aggregation

Authors :
Richard J. Fowl
Padmini Komalavilas
Elizabeth J. Furnish
Deron J. Tessier
C. Robert Flynn
Colleen M. Brophy
Elisabeth C. McLemore
Jeffrey S. Thresher
William M. Stone
Lokesh Joshi
Source :
Surgery. 136:573-578
Publication Year :
2004
Publisher :
Elsevier BV, 2004.

Abstract

Background Human saphenous vein (HSV) is the autologous conduit of choice for peripheral vascular reconstruction. Injury during harvest leads to vasospasm and a thrombogenic endoluminal surface. A proteomic transduction approach was developed to prevent vein graft vasospasm and thrombosis. Methods Recombinant HSP20 protein linked to the TAT protein transduction domain was generated in a bacterial expression system (TAT-HSP20). The effect of this protein on the inhibition of smooth muscle contraction was determined using rings of rabbit aorta and HSV in a muscle bath. In addition, the effects of TAT-HSP20 on platelet aggregation were determined in vitro using human citrated whole blood. Results Recombinant TAT-HSP20 inhibited norepinephrine-induced contraction of rabbit aortic and HSV segments. Similarly, TAT-HSP20 induced smooth muscle relaxation in HSV segments precontracted with norepinephrine. In human-citrated whole blood, platelet aggregation was significantly inhibited by TAT-HSP20 in a dose-dependent manner. Conclusions The results of this study demonstrate that recombinant TAT-HSP20 inhibits vascular smooth muscle contraction and platelet aggregation. This suggests that HSP20 may be an ideal effector molecule to target as a proteomic approach to enhance early vein graft patency rates by preventing acute vasospasm and thrombosis.

Details

ISSN :
00396060
Volume :
136
Database :
OpenAIRE
Journal :
Surgery
Accession number :
edsair.doi.dedup.....a31c247dbe82b7db5fbbbf461b3a239a
Full Text :
https://doi.org/10.1016/j.surg.2004.04.024