Aihara M, Sawada Y, Takami H, Kariya K, Kudo I, Kimura A, Yoshida Y
First Department of Internal Medicine, Hirosaki University School of Medicine, Japan.
Tohoku J Exp Med. 1989 Sep;159(1):37-44. doi: 10.1620/tjem.159.37.
A role of factor XIII (FXIII) on the interaction of human platelets with collagen was investigated using either formaldehyde fixed-washed platelets (FWP) or nonfixed platelets. The adhesion of FWP to bovine type I collagen was measured by using either an aggregometer or a collagen immobilized glass beads column. The interaction of non-fixed human platelets with collagen was measured with in vitro bleeding time (Thrombostat-4,000), which was performed by passing citrated whole blood through the filter covered with rat type I collagen under the constant shear stress. FWP adhesion to the collagen immobilized column (1,300 micrograms collagen) was not changed by the addition of commercial FXIII preparation (Fibrogammin); the adhesion was 42.7% in the presence of 1% human serum albumin, 42-43% in the presence of 1-2 U/ml of FXIII. The addition of rabbit antibody to FXIII to normal FWP did not change the degree of adhesion; 42.3% (1:100 anti-FXIII) and 46.1% (normal rabbit serum). Furthermore, platelets from the patient with congenital FXIII deficiency normally aggregated by bovine collagen and the adhesion of the patient FWP to the collagen was similar to that of normal FWP. Prolongation of partial thromboplastin time and the changes of thromboelastograph of normal plasma were observed after mixing with the collagen, and factor VIII, FXIII and von Willebrand factor were adsorbed by the collagen. The amount of FXIII in normal human plasma bound to collagen was 17, 23 and 54% at the concentration of the collagen 250, 500 and 1,000 micrograms/ml, respectively. The binding of plasma ristocetin cofactor was not different between normal control and the patient with FXIII deficiency. These data suggest that FXIII is not involved in human platelet interaction with the type I collagen, while FXIII in normal human plasma binds to the collagen.
使用甲醛固定洗涤血小板（FWP）或未固定血小板研究了因子 XIII（FXIII）在人血小板与胶原蛋白相互作用中的作用。通过使用凝集仪或胶原蛋白固定化玻璃珠柱来测量 FWP 与牛 I 型胶原蛋白的粘附。通过体外出血时间（Thrombostat - 4000）测量未固定的人血小板与胶原蛋白的相互作用，该过程是在恒定剪切应力下使枸橼酸化全血通过覆盖有大鼠 I 型胶原蛋白的滤器来进行的。添加商业 FXIII 制剂（纤维蛋白原）后，FWP 对胶原蛋白固定柱（1300 微克胶原蛋白）的粘附没有改变；在 1%人血清白蛋白存在下粘附率为 42.7%，在 1 - 2 U/ml 的 FXIII 存在下粘附率为 42 - 43%。向正常 FWP 中添加抗 FXIII 的兔抗体不会改变粘附程度；（1:100 抗 FXIII）为 42.3%，（正常兔血清）为 46.1%。此外，先天性 FXIII 缺乏患者的血小板通常能被牛胶原蛋白聚集，且该患者 FWP 与胶原蛋白的粘附与正常 FWP 相似。正常血浆与胶原蛋白混合后观察到部分凝血活酶时间延长和血栓弹性图变化，并且因子 VIII、FXIII 和血管性血友病因子被胶原蛋白吸附。在胶原蛋白浓度分别为 250、500 和 1000 微克/毫升时，正常人血浆中与胶原蛋白结合的 FXIII 量分别为 17%、23%和 54%。正常对照和 FXIII 缺乏患者之间血浆瑞斯托霉素辅因子的结合没有差异。这些数据表明 FXIII 不参与人血小板与 I 型胶原蛋白的相互作用，而正常人血浆中的 FXIII 与胶原蛋白结合。
