Fibrinogenによる赤血球の集合現象

-Fibrinogenと赤血球との相互作用-

抄録

The effect of enzymatic degradation of fibrinogen and various high molecular weight compounds on the fibrinogen-induced aggregation of human erythrocytes was quantitatively examined by using a rheoscope combined with a television image analyzer and a computer. (i) Fibrinogen of 305 kDa, resulted from the enzymatic removal of a part of the C-terminal region of A a chains, had the same ability of erythrocyte aggregation as native fibrinogen of 340 kDa. (ii) Sialic acids in fibrinogen did not participate in the interaction between fibrinogen and erythrocyte, while those in erythrocyte surface greatly affected the erythrocyte aggregation. (iii) Among fibrinogen degradation products by plasmin, fragments X and Y induced erythrocyte aggregation in slow velocity compared with fibrinogen, while fragments D and E did not induce it. (iv) The fibrinogen-induced erythrocyte aggregation was accelerated by albumin (which itself could not aggregate erythrocytes), but was not affected by the fibrinogen degradation products, dextran of 40 kDa and polyglutamic acids of 20 kDa and 8 kDa. The interaction between fibrinogen (probably at the D domain of fibrinogen ) and erythocyte surface was discussed, and a molecular mechanism for the interaction of fibrinogen and immunoglobulin G with erythrocytes in the presence of albumin was proposed. (J. Jpn. Soc. Biorheol., 1 (1), 27~37, 1987).