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

McLemore EC, Tessier DJ, Flynn CR, Furnish EJ, Komalavilas P, Thresher JS, Joshi L, Stone WM, Fowl RJ, Brophy CM
Surgery. 2004 136 (3): 573-8

PMID: 15349104 · DOI:10.1016/j.surg.2004.04.024

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.

MeSH Terms (16)

Animals Aorta Blood Vessels Gene Products, tat Heat-Shock Proteins HSP20 Heat-Shock Proteins Humans In Vitro Techniques Myocytes, Smooth Muscle Peptide Fragments Phosphoproteins Platelet Aggregation Rabbits Recombinant Proteins Saphenous Vein Vasoconstriction

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