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KMID : 0370219970410020247
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Yakhak Hoeji
1997 Volume.41 No. 2 p.247 ~ p.254
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Protein Fraction Extracted from the Earthworm Lumbricus rubellus Activates Proteinase Activated Receptor-2 and is Effective on Hemokinesis
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이철규/Lee CK
신장식/최영근/임채곤/조일환/김철/Shin JS/Choi YK/Lim CK/Cho IH/Kim C
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Abstract
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The proteinase-activated receptor (PAR-2) belongs to the family of seven transmembrane region receptors, like the thrombin receptor, it is activated by specific proteolytic cleavage of its extracellular amino terminus and a synthetic peptide (SLIGRL). The earthworm protein fraction (EPF) extracted from Lumbricus rubellus elicted dose- and endothelium-dependent relaxations in phenylephrine-contracted rat thoracic aorta, whereas heat inactivated EPF (0.5 micro g/ml) had no effect. In the presence of the nitric oxide synthase inhibitor NG-methyl-L-arginine (1.8 micro M), EPF (0.5 micro g/ml induced relaxations were partially inhibited. Furthermore, EPF (0.5 micro g/ml) dramatically caused relaxation of thrombin-desenstized rat thoracic aorta. These results indicate that EPF activates PAR-2 in vascular endothelial cell. Intravenous injection of EPF (20 mg/kg, bolus) into anesthetized rats produced a marked depressor response. EPF (0 ~ 80 micro g/ml, gradient) was very effective on increasing of perfusion volume in rabbit ear vessel preparations. These results imply the usefulness of EPF as a vascular smooth muscle relaxant and indicate that the activation of PAR-2 may be a mechanism of EPF on hemokinetic improvement.
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