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

Elisabeth C. McLemore, Deron J. Tessier, C. Robert Flynn, Elizabeth J. Furnish, Padmini Komalavilas, Jeffrey S. Thresher, Lokesh Joshi, William M. Stone, Richard J. Fowl, Colleen M. Brophy

Research output: Contribution to journalArticle

18 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)573-578
Number of pages6
JournalSurgery
Volume136
Issue number3
DOIs
StatePublished - Sep 2004

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Small Heat-Shock Proteins
Platelet Aggregation
Recombinant Proteins
Saphenous Vein
Muscle Contraction
Proteomics
Smooth Muscle
Veins
Norepinephrine
Thrombosis
Rabbits
Transplants
Muscle Relaxation
Baths
Vascular Smooth Muscle
Blood Vessels
Aorta
Blood Platelets
Muscles
Wounds and Injuries

ASJC Scopus subject areas

  • Surgery

Cite this

McLemore, E. C., Tessier, D. J., Robert Flynn, C., Furnish, E. J., Komalavilas, P., Thresher, J. S., ... Brophy, C. M. (2004). Transducible recombinant small heat shock-related protein, HSP20, inhibits vasospasm and platelet aggregation. Surgery, 136(3), 573-578. https://doi.org/10.1016/j.surg.2004.04.024

Transducible recombinant small heat shock-related protein, HSP20, inhibits vasospasm and platelet aggregation. / McLemore, Elisabeth C.; Tessier, Deron J.; Robert Flynn, C.; Furnish, Elizabeth J.; Komalavilas, Padmini; Thresher, Jeffrey S.; Joshi, Lokesh; Stone, William M.; Fowl, Richard J.; Brophy, Colleen M.

In: Surgery, Vol. 136, No. 3, 09.2004, p. 573-578.

Research output: Contribution to journalArticle

McLemore, EC, Tessier, DJ, Robert Flynn, C, Furnish, EJ, Komalavilas, P, Thresher, JS, Joshi, L, Stone, WM, Fowl, RJ & Brophy, CM 2004, 'Transducible recombinant small heat shock-related protein, HSP20, inhibits vasospasm and platelet aggregation', Surgery, vol. 136, no. 3, pp. 573-578. https://doi.org/10.1016/j.surg.2004.04.024
McLemore EC, Tessier DJ, Robert Flynn C, Furnish EJ, Komalavilas P, Thresher JS et al. Transducible recombinant small heat shock-related protein, HSP20, inhibits vasospasm and platelet aggregation. Surgery. 2004 Sep;136(3):573-578. https://doi.org/10.1016/j.surg.2004.04.024
McLemore, Elisabeth C. ; Tessier, Deron J. ; Robert Flynn, C. ; Furnish, Elizabeth J. ; Komalavilas, Padmini ; Thresher, Jeffrey S. ; Joshi, Lokesh ; Stone, William M. ; Fowl, Richard J. ; Brophy, Colleen M. / Transducible recombinant small heat shock-related protein, HSP20, inhibits vasospasm and platelet aggregation. In: Surgery. 2004 ; Vol. 136, No. 3. pp. 573-578.
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AU - Komalavilas, Padmini

AU - Thresher, Jeffrey S.

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AB - 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.

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