ROLE OF COLLAGEN QUATERNARY STRUCTURE IN PLATELET - COLLAGEN INTERACTION

ROLE OF COLLAGEN QUATERNARY STRUCTURE IN PLATELET - COLLAGEN INTERACTION
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DOI:
10.1172/jci107896
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发表时间:
1974-01-01
影响因子:
15.9
通讯作者:
BENSUSAN, HB
BENSUSAN, HB
中科院分区:
医学1区
文献类型:
--
作者:
BRASS, LF;BENSUSAN, HB

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我们研究了血小板与胶原蛋白相互作用是否需要胶原蛋白的谱系结构。四级结构指的是胶原单体(对胶原)组装成聚合物(原生型原纤维)。以胎牛皮乙酸提取物为原料制备纯化的单体胶原蛋白。以牛跟腱胶原为分散体,单体胶原在37℃、pH 7.4条件下孵育制备聚合胶原。聚合状态通过电子显微镜证实。在没有血小板聚集的情况下,血小板血清素的释放被用来确定血小板:胶原相互作用的有效性。所有形式的胶原蛋白释放血清素都有一个滞后期,但聚合胶原蛋白的滞后期比单体胶原蛋白短。单体胶原也选择性地进行了磺化,将胶原的赖氨酸基团转化为精氨酸,同时保持极性基团的排列不变。单体胶原的胍基化增加了聚合速度,减少了血清素释放的滞后时间。葡萄糖胺(17 mM)阻滞聚合,抑制单体胶原释放血小板血清素,但对凝血酶和聚合胶原释放血小板血清素影响不大。在相同浓度下,葡萄糖胺不会降低血小板对胶原刺激的敏感性,也不会阻断血小板与胶原的相互作用。葡萄糖胺只对胶原蛋白有影响:胶原蛋白相互作用。半乳糖胺有类似的效果,但葡萄糖、半乳糖和n -乙酰糖胺没有效果。我们从这些数据中得出结论,胶原单体不能有效地与血小板相互作用,因此,胶原的四级结构在血小板对胶原的识别中起作用。
We have investigated whether collagen queternary structure is required for the platelet: collagen interaction. Quaternary structure refers to the assembly of collagen monomers (tropocollagen) into polymers (native-type fibrils). Purified monomeric collagen was prepared from acetic acid extracts of fetal calfskin. Polymeric collagen was prepared by dispersion of bovine Achilles tendon collagen and by incubation of monomeric collagen at 37°C and pH 7.4. The state of polymerization was confirmed by electron microscopy. Release of platelet serotonin in the absence of platelet aggregation was used to determine the effectiveness of the platelet: collagen interaction. All forms of collagen produced serotonin release only after a lag period, but polymeric collagen gave a shorter lag period than did monomeric collagen. Monomeric collagen was also quanidinated selectively to convert collagen lysine groups to homoarginine, while leaving the arrangement of polar groups intact. Guanidination of monomeric collagen increased the rate of polymerization and reduced the lag time in serotonin release. Glucosamine (17 mM) retarded polymerization and inhibited the release of platelet serotonin by monomeric collagen but had little effect on release produced by thrombin or polymeric collagen. At the same concentration, glucosamine did not reduce the sensitivity of platelets to stimulation by collagen or block the platelet: collagen interaction. The only effect of glucosamine was on the collagen: collagen interaction. Galactosamine had a similar effect, but glucose, galactose, andN-acetylglycosamine had no effect. We conclude from this data that collagen monomers cannot effectively interact with platelets and that, therefore, collagen quaternary structure has a role in the recognition of collagen by platelets.