JZUS - Journal of Zhejiang University SCIENCE

Journal of Zhejiang University SCIENCE B 2007 Vol.8 No.8 P.570-574

http://doi.org/10.1631/jzus.2007.B0570

Novel distribution pattern of fibrinolytic components in rabbit tissues extract: a preliminary study

Author(s): LU Xing-guo, WU Xian-guo, XU Xiao-hua, GONG Xu-bo, ZHOU Xuan, XU Gen-bo, ZHU Lei, ZHAO Xiao-ying
Affiliation(s): Department of Haematology, the Second Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou 310009, China; more
Corresponding email(s): xgwu1973@163.com
Key Words: Tissue extract, Fibrinolytic factors, Fibrinolytic inhibitors

Share this article to： More <<< Previous Article \|Next Article >>>

Abstract: Objective: The purpose of this work was to investigate the distribution pattern of fibrinolytic factors and their inhibitors in rabbit tissues. Methods: The components of the fibrinolytic system in extracts from a variety of rabbit tissues, including tissue plasminogen activator (tPA), plasminogen activator inhibitor-1 (PAI-1), plasminogen (Plg), plasmin (Pl) and α₂ plasmin inhibitor (α₂PI), were determined by colorimetric assay. Results: The tissue extracts in renal, small intestine, lung, brain and spleen demonstrated strong fibrinolytic function, in which high activity of tPA, Plg and Pl was manifested; whereas in skeletal muscle, tongue and stomach, higher activity of PAI-1 and α₂PI showed obviously. Also excellent linear correlations were found between levels of tPA and PAI-1, Pl and α₂PI, Plg and Pl. In related tissues, renal cortex and renal marrow showed distinctly higher activity of tPA and lower activity of PAI-1, with the levels of Plg and Pl in renal cortex being higher than those in renal marrow, where the α₂PI level was higher than that in renal cortex. Similarly, the levels of tPA, Plg and Pl in small intestine were higher than those in large intestine, but with respect to PAI-1 and α₂PI, the matter was reverse. In addition, the fibrinolytic activity in muscle tissue was lower, however, the levels of tPA, Plg, and Pl in cardiac muscle were obviously higher than those in skeletal muscles, and the levels of PAI-1 and α₂PI were significantly lower than those in skeletal muscle. Conclusion: Our data demonstrate that a remarkable difference of the fibrinolytic patterns exists in rabbit tissues, which has probable profound significance in understanding the relationship between the function of haemostasis or thrombosis and the physiologic function in tissues.

Reference

[1] Casslen, B., Bossmar, T., Lecander, I., Astedt, B., 1994. Plasminogen activators and plasminogen activator inhibitors in blood and tumour fluids of patients with ovarian cancer. Eur. J. Cancer, 30(9):1302-1309.

[2] Fang, C.L., Li, Y.P., Lu, X.G., 2005. Experimental study of procoagulant-active substance and its inhibitors in rabbits’ tissues extract. J. Chin. Microcirc., 9(4):267-268 (in Chinese).

[3] Gesualdo, L., Ranieri, E., Monno, R., Rossiello, M.R., Colucci, M., Semeraro, N., Grandaliano, G., Schena, F.P., Ursi, M., Cerullo, G., 1999. Angiotensin IV stimulates plasminogen activator inhibitor-1 expression in proximal tubular epithelial cells. Kidney Int., 56(2):461-470.

[4] Hatton, M.W., Southward, S.M., Ross, B.L., Clarke, B.J., Singh, G., Richardson, M., 2006. Relationships among tumor burden, tumor size, and the changing concentrations of fibrin degradation products and fibrinolytic factors in the pleural effusions of rabbits with VX2 lung tumors. J. Lab. Clin. Med., 147(1):27-35.

[5] Kurose, I., Miura, S., Suematsu, M., Serizawa, H., Fukumura, D., Asako, H., Hibi, T., Tsuchiya, M., 1992. Tissue-type plasminogen activator of colonic mucosa in ulcerative colitis. Evidence of endothelium-derived fibrinolytic activation. Dig. Dis. Sci., 37(2):307-311.

[6] Liu, Y.X., Feng, Q., Peng, X.R., Tor, N., 1994. Secretion of plasminogen activator inhibitor type 1 by cultured ovarian cells obtained from gonadotropin-treated immature rats. Sci. China B, 37(8):940-947.

[7] Lu, X.G., 1990. The Basis and Clinical of Blood Coagulation and Fibrinolysis. Unite Publishing House, Beijing, p.40-42 (in Chinese).

[8] Lu, X.G., Zhang, G.D., Xu, Y.L., 2003. The investigation of urokinase type and tissue type plasminogen activators in liver cancer tissue extract. Basic Med. Sci. Clin., 23(5):572-573 (in Chinese).

[9] Mayer, E.J., Fujita, T., Gardell, S.J., Shebuski, R.J., Reilly, C.F., 1990. The pharmacokinetics of plasminogen activator inhibitor-1 in the rabbit. Blood, 76(8):1514-1520.

[10] Padro, T., Quax, P.H., van den Hoogen, C.M., Roholl, P., Verheijen, J.H., Emeis, J.J., 1994. Tissue-type plasminogen activator and its inhibitor in rat aorta. Effect of endotoxin. Arterioscler. Thromb., 14(9):1459-1465.

[11] Schmitt, M., Sturmheit, A.S., Welk, A., Schnelldorfer, C., Harbeck, N., 2006. Procedures for the quantitative protein determination of urokinase and its inhibitor, PAI-1, in human breast cancer tissue extracts by ELISA. Methods Mol. Med., 120:245-265.

[12] Stenberg, B., Karlsson, L., Alpsten, M., Risberg, B., 1983. Reduction of gastric haemorrhage by fibrinolysis inhibition—an experimental study in rats. Thromb. Haemost., 49(2):106-108.

[13] Sumiyoshi, K., Baba, S., Sakaguchi, S., Urano, T., Takada, Y., Takada, A., 1991. Increase in levels of plasminogen activator and type-1 plasminogen activator inhibitor in human breast cancer: possible roles in tumor progression and metastasis. Thromb. Res., 63(1):59-71.

[14] Umeda, T., Eguchi, Y., Okino, K., Kodama, M., Hattori, T., 1997. Cellular localization of urokinase-type plasminogen activator, its inhibitors, and their mRNAs in breast cancer tissues. J. Pathol., 183(4):388-397.

[15] Zekanowska, E., Cieslinski, K., Rosc, D., 2004. Plasminogen activator inhibitor type 1 (PAI-1) in blood and tissue extracts of patients with non-small cell lung cancer. Pneumonol. Alergol. Pol., 72(9):409-414 (in Polish).

Open peer comments: Debate/Discuss/Question/Opinion

<1>

Similar articles

- Go to

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

Reference